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L-alpha-Alanine, also known simply as alanine, is a naturally occurring non-essential amino acid that plays a crucial role in the synthesis of proteins in the body. It is an important component of muscle tissue, involved in regulating blood sugar levels, energy production, and neurotransmitter synthesis. L-alpha-Alanine is also studied for its potential to promote physical and mental well-being, improve athletic performance, and reduce muscle fatigue, making it an essential compound for various physiological functions.

56-41-7

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56-41-7 Usage

Uses

Used in Nutritional Supplements:
L-alpha-Alanine is used as a nutritional supplement to support muscle growth and repair, as it is a key component of muscle tissue. It helps in the synthesis of proteins, which is essential for maintaining and building muscle mass.
Used in Energy Production:
L-alpha-Alanine is used as an energy source in the body, as it is involved in the production of energy through metabolic processes. It helps in maintaining energy levels during physical activities and supports overall energy metabolism.
Used in Blood Sugar Regulation:
L-alpha-Alanine is used as a regulator of blood sugar levels, as it plays a role in glucose metabolism. It helps in maintaining stable blood sugar levels and supports the body's ability to utilize glucose for energy.
Used in Neurotransmitter Synthesis:
L-alpha-Alanine is used as a precursor for the synthesis of neurotransmitters, which are essential for proper communication between nerve cells. It supports the nervous system's function and contributes to mental well-being.
Used in Athletic Performance Enhancement:
L-alpha-Alanine is used as a performance enhancer in sports and athletic activities, as it has been studied for its potential to improve physical performance and reduce muscle fatigue. It helps in enhancing endurance and recovery during intense physical exertion.
Used in Pharmaceutical Industry:
L-alpha-Alanine is used in the pharmaceutical industry for the development of drugs and medications that target various physiological functions, such as muscle growth, energy metabolism, and neurotransmitter synthesis.
Used in Food and Beverage Industry:
L-alpha-Alanine is used in the food and beverage industry as a flavor enhancer and a component in certain dietary supplements. It contributes to the taste and nutritional value of various food products and supplements.

Check Digit Verification of cas no

The CAS Registry Mumber 56-41-7 includes 5 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 2 digits, 5 and 6 respectively; the second part has 2 digits, 4 and 1 respectively.
Calculate Digit Verification of CAS Registry Number 56-41:
(4*5)+(3*6)+(2*4)+(1*1)=47
47 % 10 = 7
So 56-41-7 is a valid CAS Registry Number.
InChI:InChI=1/C3H7NO2/c1-2(4)3(5)6/h2H,4H2,1H3,(H,5,6)/t2-/m0/s1

56-41-7 Well-known Company Product Price

  • Brand
  • (Code)Product description
  • CAS number
  • Packaging
  • Price
  • Detail
  • TCI America

  • (A0179)  L-Alanine  >99.0%(T)

  • 56-41-7

  • 25g

  • 210.00CNY

  • Detail
  • TCI America

  • (A0179)  L-Alanine  >99.0%(T)

  • 56-41-7

  • 250g

  • 990.00CNY

  • Detail
  • Alfa Aesar

  • (A15804)  L-Alanine, 99%   

  • 56-41-7

  • 25g

  • 194.0CNY

  • Detail
  • Alfa Aesar

  • (A15804)  L-Alanine, 99%   

  • 56-41-7

  • 100g

  • 545.0CNY

  • Detail
  • Alfa Aesar

  • (A15804)  L-Alanine, 99%   

  • 56-41-7

  • 500g

  • 2506.0CNY

  • Detail
  • Sigma-Aldrich

  • (44526)  L-Alanine  certified reference material, TraceCERT®

  • 56-41-7

  • 44526-100MG

  • 1,117.35CNY

  • Detail
  • Sigma-Aldrich

  • (PHR1110)  L-Alanine  pharmaceutical secondary standard; traceable to USP and PhEur

  • 56-41-7

  • PHR1110-1G

  • 732.19CNY

  • Detail
  • Sigma-Aldrich

  • (A0325000)  Alanine  European Pharmacopoeia (EP) Reference Standard

  • 56-41-7

  • A0325000

  • 1,880.19CNY

  • Detail
  • USP

  • (1012509)  L-Alanine  United States Pharmacopeia (USP) Reference Standard

  • 56-41-7

  • 1012509-200MG

  • 4,588.74CNY

  • Detail
  • Sigma

  • (A7469)  L-Alanine  from non-animal source, meets EP, USP testing specifications, suitable for cell culture, ≥98.5%

  • 56-41-7

  • A7469-10MG

  • 167.31CNY

  • Detail
  • Sigma

  • (A7469)  L-Alanine  from non-animal source, meets EP, USP testing specifications, suitable for cell culture, ≥98.5%

  • 56-41-7

  • A7469-25G

  • 331.11CNY

  • Detail
  • Sigma

  • (A7469)  L-Alanine  from non-animal source, meets EP, USP testing specifications, suitable for cell culture, ≥98.5%

  • 56-41-7

  • A7469-100G

  • 479.70CNY

  • Detail

56-41-7SDS

SAFETY DATA SHEETS

According to Globally Harmonized System of Classification and Labelling of Chemicals (GHS) - Sixth revised edition

Version: 1.0

Creation Date: Aug 12, 2017

Revision Date: Aug 12, 2017

1.Identification

1.1 GHS Product identifier

Product name L-alanine

1.2 Other means of identification

Product number -
Other names H-ALA-OH

1.3 Recommended use of the chemical and restrictions on use

Identified uses For industry use only. Food additives -> Flavoring Agents
Uses advised against no data available

1.4 Supplier's details

1.5 Emergency phone number

Emergency phone number -
Service hours Monday to Friday, 9am-5pm (Standard time zone: UTC/GMT +8 hours).

More Details:56-41-7 SDS

56-41-7Synthetic route

N-carbamoyl-DL-alanine
77340-50-2

N-carbamoyl-DL-alanine

L-alanin
56-41-7

L-alanin

Conditions
ConditionsYield
With NH4Cl-NH4OH buffer pH 8.5; nickel dichloride at 60℃; for 24h; N-carbamyl-L-amino acid aminohydrolase;100%
With sodium phosphate buffer; N-carmamyl-L-amino acid aminohydrolase of Pseudomonas sp. strain NS671; water; manganese(II) at 30℃; for 0.5h; Product distribution;18.1 mmol
L-N-Boc-Ala
15761-38-3

L-N-Boc-Ala

L-alanin
56-41-7

L-alanin

Conditions
ConditionsYield
With water at 170℃; for 0.05h; Microwave irradiation;100%
With water at 150℃; for 2h; Subcritical conditions;100%
With tetradecyl(trihexyl)phosphonium bistriflamide; trifluoroacetic acid at 130℃; for 0.116667h; Ionic liquid;98%
sodium pyruvate
113-24-6

sodium pyruvate

L-alanin
56-41-7

L-alanin

Conditions
ConditionsYield
With sodium formate; ammonium chloride; NADH In aq. phosphate buffer at 25℃; for 6h; pH=8.0; Kinetics; Reagent/catalyst; Green chemistry; Enzymatic reaction;100%
With zinc(II) perchlorate; (R)-15-amino-methyl-14-hydroxy-5,5-dimethyl-2,8-dithia<9>(2,5)pyridinophane In methanol for 24h; Ambient temperature;72%
Proc-Ala-OH
220930-89-2

Proc-Ala-OH

L-alanin
56-41-7

L-alanin

Conditions
ConditionsYield
With resin bound tetrathiomolybdate In methanol at 28℃; for 1.5h; ultrasonic bath;100%
Conditions
ConditionsYield
With hydrogenchloride pH=6.5; pH-value;100%
(S)-N-(tert-butoxycarbonyl)alanine methyl ester
28875-17-4

(S)-N-(tert-butoxycarbonyl)alanine methyl ester

L-alanin
56-41-7

L-alanin

Conditions
ConditionsYield
With water at 100℃; for 4h;99%
(S)-2-[(2,3,4,5,6-pentafluorophenoxy)phenoxyphosphorylamino]propionic acid isopropyl ester
1256490-52-4

(S)-2-[(2,3,4,5,6-pentafluorophenoxy)phenoxyphosphorylamino]propionic acid isopropyl ester

A

L-alanin
56-41-7

L-alanin

B

2,3,4,5,6-pentafluorophenol
771-61-9

2,3,4,5,6-pentafluorophenol

C

phenol
108-95-2

phenol

Conditions
ConditionsYield
With sodium hydroxide In methanol; water at 25 - 60℃; for 4h; Reagent/catalyst; Temperature; Solvent;A 94.2%
B 95.7%
C 98.2%
(2S,5S)-N-<(S)-N-bis(methylthio)methylenealanyl>-2,5-bis(methoxymethoxymethyl)pyrrolidine
108437-91-8

(2S,5S)-N-<(S)-N-bis(methylthio)methylenealanyl>-2,5-bis(methoxymethoxymethyl)pyrrolidine

L-alanin
56-41-7

L-alanin

Conditions
ConditionsYield
With hydrogenchloride for 4h; Heating;97%
L-Cysteine
52-90-4

L-Cysteine

L-alanin
56-41-7

L-alanin

Conditions
ConditionsYield
With [4,4’-bis(1,1-dimethylethyl)-2,2’-bipyridine-N1,N1‘]bis [3,5-difluoro-2-[5-(trifluoromethyl)-2-pyridinyl-N]phenyl-C]iridium(III) hexafluorophosphate; triethyl phosphite In aq. phosphate buffer; acetonitrile at 20℃; for 0.5h; pH=6.5; Catalytic behavior; Solvent; Reagent/catalyst; Irradiation;96%
With tris(2,2'-bipyridyl)ruthenium dichloride; trisodium tris(3-sulfophenyl)phosphine In water at 20℃; for 16h; Inert atmosphere; Irradiation;84%
With triethyl borane; triethyl phosphite 1.) THF, CH3CN, RT, 90 min, 2.) THF, CH3CN, RT, irradiation, 6.5 h; Multistep reaction;
With nickel In water at 60℃; for 0.5h; Product distribution; desulfurization;
rac-Ala-OH
302-72-7

rac-Ala-OH

L-alanin
56-41-7

L-alanin

Conditions
ConditionsYield
In water at 37℃; for 10h; NADH, ammonium chloride, sodium formate, D-amino acid oxidase, catalase, leucine dehydrogenase, formate dehydrogenase, Tris-HCl buffer, pH 8.5;95%
optische Spaltung;
With D-amino acid oxide ase-substance
N-Cbz-Ala
1142-20-7

N-Cbz-Ala

L-alanin
56-41-7

L-alanin

Conditions
ConditionsYield
With hydrogen; K3[Co(CN)5] In methanol at 20℃; for 3h;94%
With hydrogen; hydroxyapatite-bound Pd In methanol at 40℃; under 760 Torr; for 1.5h; Product distribution; Further Variations:; Catalysts;92%
at 35℃; for 0.0833333h; Rate constant; pH 6.0; amino acid urethane hydrolase from Streptococcus faecalis;
Boc-Ala-Merrifield resin

Boc-Ala-Merrifield resin

L-alanin
56-41-7

L-alanin

Conditions
ConditionsYield
With dimethyl ether-poly(hydrogen fluoride) at 0℃; for 1h;94%
H-Ala-OBzl
17831-01-5

H-Ala-OBzl

L-alanin
56-41-7

L-alanin

Conditions
ConditionsYield
With hydrogen; K3[Co(CN)5] In methanol at 20℃; for 3h;92%
at 25℃; for 0.833333h; enzyme alcalase from Bacillus licheniforms; pH 8.2;
With E. coli BL21 Star (DE3) S30 extract In aq. buffer at 37℃; for 6h; pH=7.5;
C3H7NO2*H3N*ClH

C3H7NO2*H3N*ClH

L-alanin
56-41-7

L-alanin

Conditions
ConditionsYield
With ruthenium nanoparticles dispersed in a polyvinylpyrrolidone matrix; amberlyst A-21 In methanol; dichloromethane92%
hexan-1-amine
111-26-2

hexan-1-amine

(S)-2-(3,5-Dinitro-4-oxo-4H-pyridin-1-yl)-propionic acid
78641-65-3

(S)-2-(3,5-Dinitro-4-oxo-4H-pyridin-1-yl)-propionic acid

A

L-alanin
56-41-7

L-alanin

B

1-hexyl-3,5-dinitro-4-pyridone
74197-48-1

1-hexyl-3,5-dinitro-4-pyridone

Conditions
ConditionsYield
In pyridine for 1.5h; Product distribution;A 91.7%
B n/a
2-oxo-propionic acid
127-17-3

2-oxo-propionic acid

A

L-alanin
56-41-7

L-alanin

B

D-Alanine
338-69-2

D-Alanine

Conditions
ConditionsYield
With CC10H14NOSCH2CH2CH3N(CH3)2 (5); zinc diacetate In methanol at 30℃; Product distribution; pH 4.00; other reagents;A 9%
B 91%
With 5-((3-(dimethylamino)propyl)thio)-4-(aminomethyl)-3-hydroxyl-5,6,7,8-tetraquinoline In methanol at 30℃; Product distribution; stereoselective transamination at pH=4.00, various reagents and pH;A 7 % Chromat.
B 93 % Chromat.
With ethylenediaminetetraacetic acid; D-(R)-phenylalanine at 20℃; for 24h; pH=8; Product distribution; Further Variations:; Reagents; transamination;
(3S,5S)-3-Methyl-5-phenyl-morpholin-2-one

(3S,5S)-3-Methyl-5-phenyl-morpholin-2-one

L-alanin
56-41-7

L-alanin

Conditions
ConditionsYield
With hydrogen; trifluoroacetic acid; palladium dihydroxide In methanol; water under 3750.3 Torr; for 24h;91%
L-cystine
56-89-3

L-cystine

L-alanin
56-41-7

L-alanin

Conditions
ConditionsYield
With triethyl borane; tributylphosphine; sodium hydrogencarbonate; triethyl phosphite In propan-1-ol for 36h; Ambient temperature; Irradiation;90%
With tris(2-carboxyethyl)phosphine; [4,4’-bis(1,1-dimethylethyl)-2,2’-bipyridine-N1,N1‘]bis [3,5-difluoro-2-[5-(trifluoromethyl)-2-pyridinyl-N]phenyl-C]iridium(III) hexafluorophosphate In aq. phosphate buffer; acetonitrile at 37℃; for 1h; pH=6.5; Temperature; Inert atmosphere; Schlenk technique; Sealed tube;85%
With water; nickel at 45℃;
With nickel In water at 60℃; for 0.5h; Product distribution; desulfurization;
(3S,6S)-1,4-N,N-((S)-1-phenyleth-1-yl)-3,6-dimethylpiperazine-2,5-dione
143746-60-5

(3S,6S)-1,4-N,N-((S)-1-phenyleth-1-yl)-3,6-dimethylpiperazine-2,5-dione

L-alanin
56-41-7

L-alanin

Conditions
ConditionsYield
With hydrogen iodide for 1h; Heating;90%
C13H19BN2O2

C13H19BN2O2

L-alanin
56-41-7

L-alanin

Conditions
ConditionsYield
With acetic acid Hydrolysis;90%
L-cystine dimethyl ester
1069-29-0

L-cystine dimethyl ester

L-alanin
56-41-7

L-alanin

Conditions
ConditionsYield
With triethyl borane; tributylphosphine; sodium hydrogencarbonate; triethyl phosphite In propan-1-ol for 36h; Ambient temperature; Irradiation;88%
(S)-2-<(R)-2-hydroxy-1-phenylethylamino>propanoic acid
145058-00-0

(S)-2-<(R)-2-hydroxy-1-phenylethylamino>propanoic acid

L-alanin
56-41-7

L-alanin

Conditions
ConditionsYield
With formic acid; palladium In methanol; water for 168h; Ambient temperature;86%
(2S,4'S)-2-(2'-oxo-4'-phenyloxazolidin-3'-yl)propanoic acid

(2S,4'S)-2-(2'-oxo-4'-phenyloxazolidin-3'-yl)propanoic acid

L-alanin
56-41-7

L-alanin

Conditions
ConditionsYield
With ammonia; lithium In tetrahydrofuran; tert-butyl alcohol at -70℃; for 0.0833333h; Elimination; Birch-Evans method;84%
(1S)-1-(furan-2-yl)ethanamine
27948-38-5

(1S)-1-(furan-2-yl)ethanamine

L-alanin
56-41-7

L-alanin

Conditions
ConditionsYield
With ozone In methanol at -78℃; for 0.25h;82%
p-methoxybenzyloxycarbonyl-Phe-OMe
97985-98-3

p-methoxybenzyloxycarbonyl-Phe-OMe

α-alanine propyl ester

α-alanine propyl ester

A

L-alanin
56-41-7

L-alanin

B

Moz-Phe-D-Ala-O(nPr)

Moz-Phe-D-Ala-O(nPr)

Conditions
ConditionsYield
Stage #1: α-alanine propyl ester With Alcalase; water In tert-butyl alcohol at 25℃; pH=8.5; kinetic resolution;
Stage #2: p-methoxybenzyloxycarbonyl-Phe-OMe With Alcalase In tert-butyl alcohol Condensation;
A n/a
B 81%

A

L-alanin
56-41-7

L-alanin

B

D-Alanine
338-69-2

D-Alanine

C

D-norvaline
2013-12-9

D-norvaline

D

L-Norvaline
6600-40-4

L-Norvaline

Conditions
ConditionsYield
With (S)-1-(N,N-dimethylaminomethyl)-2-formylcymantrene; sodium methylate; copper (I) acetate for 1h; Ambient temperature;A 78.31%
B 21.69%
C 60.57%
D 39.43%
With (S)-1-(N,N-dimethylaminomethyl)-2-formylcymantrene; sodium methylate; copper (I) acetate for 3h; Ambient temperature;A 76.83%
B 23.15%
C 73.8%
D 26.2%
With (R)-1-(N,N-dimethylaminomethyl)-2-formylcymantrene; sodium methylate; copper (I) acetate for 1h; Ambient temperature;A 26.8%
B 73.2%
C 42.16%
D 57.84%
With (R)-1-(N,N-dimethylaminomethyl)-2-formylcymantrene; sodium methylate; copper (I) acetate for 1h; Ambient temperature;A 26.8%
B 73.2%
C 42.16%
D 57.84%
(2R,5R)-2,5-Bis-methoxymethyl-pyrrolidine-1-carboxylic acid ((S)-1-carbamoyl-ethyl)-amide
137910-12-4

(2R,5R)-2,5-Bis-methoxymethyl-pyrrolidine-1-carboxylic acid ((S)-1-carbamoyl-ethyl)-amide

L-alanin
56-41-7

L-alanin

Conditions
ConditionsYield
With hydrogenchloride Heating;78%
methanol
67-56-1

methanol

L-tyrosyl-L-alanine
730-08-5

L-tyrosyl-L-alanine

A

benzyl methyl ether
538-86-3

benzyl methyl ether

B

L-alanin
56-41-7

L-alanin

Conditions
ConditionsYield
With potassium hydroxide; [bis(acetoxy)iodo]benzene at 0 - 5℃; for 1.5h;A 71%
B n/a
(S)-Alaninol
2749-11-3

(S)-Alaninol

L-alanin
56-41-7

L-alanin

Conditions
ConditionsYield
With (6-di-tert-butylphosphinomethyl-2,2’-bipyridyl)Ru(CO)HCl; sodium hydroxide In 1,4-dioxane; water at 20℃;71%
methanol
67-56-1

methanol

L-alanin
56-41-7

L-alanin

L-Alanine methyl ester
10065-72-2

L-Alanine methyl ester

Conditions
ConditionsYield
With thionyl chloride at 20℃; for 48h; Reflux;100%
Stage #1: methanol With thionyl chloride at 0℃; for 0.166667h;
Stage #2: L-alanin at 20℃; for 12h;
97%
With thionyl chloride at 8 - 10℃; Reflux;96.68%
L-alanin
56-41-7

L-alanin

chloroformic acid ethyl ester
541-41-3

chloroformic acid ethyl ester

N-ethoxycarbonyl-L-alanine
16639-86-4

N-ethoxycarbonyl-L-alanine

Conditions
ConditionsYield
With sodium hydroxide at 15℃; for 1h; pH=9;100%
With sodium hydrogencarbonate In water at 20℃; for 24h;94%
With sodium hydroxide for 2h; Ambient temperature; pH=9-10;91%
L-alanin
56-41-7

L-alanin

benzyl chloroformate
501-53-1

benzyl chloroformate

N-Cbz-Ala
1142-20-7

N-Cbz-Ala

Conditions
ConditionsYield
With sodium hydroxide In water at 0 - 20℃;100%
With sodium hydroxide In water at 0 - 20℃; for 5h;99%
With sodium carbonate In water at 0 - 20℃; for 24h;98%
formaldehyd
50-00-0

formaldehyd

L-alanin
56-41-7

L-alanin

N,N-dimethyl-L-alanine
2812-31-9

N,N-dimethyl-L-alanine

Conditions
ConditionsYield
With palladium 10% on activated carbon; hydrogen In ethanol at 20℃; for 20h;100%
With 10 mol% palladium on carbon; hydrogen In water at 20℃; under 760.051 Torr; for 36.5h; Reflux;99%
With sodium dihydrogenphosphate; zinc at 30℃; for 20h;92%
ethanol
64-17-5

ethanol

L-alanin
56-41-7

L-alanin

L-Alanine ethyl ester
3082-75-5

L-Alanine ethyl ester

Conditions
ConditionsYield
With thionyl chloride100%
With thionyl chloride
With hydrogenchloride
methanol
67-56-1

methanol

L-alanin
56-41-7

L-alanin

L-alanine methyl ester hydrochloride
2491-20-5

L-alanine methyl ester hydrochloride

Conditions
ConditionsYield
Stage #1: methanol With thionyl chloride at -15 - 0℃;
Stage #2: L-alanin for 3h; Reflux;
100%
With thionyl chloride at -20 - 22℃; for 49h;100%
With thionyl chloride at 40℃; for 3.5h;99%
ethanol
64-17-5

ethanol

L-alanin
56-41-7

L-alanin

(S)-alanine ethyl ester hydrochloride
1115-59-9

(S)-alanine ethyl ester hydrochloride

Conditions
ConditionsYield
With thionyl chloride for 4h; Reflux;100%
With hydrogenchloride for 12h; Reflux;99%
With thionyl chloride99%
L-alanin
56-41-7

L-alanin

di-tert-butyl dicarbonate
24424-99-5

di-tert-butyl dicarbonate

L-N-Boc-Ala
15761-38-3

L-N-Boc-Ala

Conditions
ConditionsYield
In 1,4-dioxane; water at 0 - 20℃; for 1h;100%
With sodium hydroxide In tetrahydrofuran; water at 20℃; for 17h;100%
With sodium hydroxide In tetrahydrofuran; water at 0 - 30℃; for 4.5h;98%
Conditions
ConditionsYield
With hydrogenchloride In water for 0.5h;100%
With hydrogenchloride In water
With hydrogenchloride In water at 20℃;
L-alanin
56-41-7

L-alanin

Allyl chloroformate
2937-50-0

Allyl chloroformate

N-allyloxycarbonyl-L-alanine
90508-28-4

N-allyloxycarbonyl-L-alanine

Conditions
ConditionsYield
With sodium hydroxide In water for 3h; Condensation;100%
With sodium hydroxide at 20℃; for 2h;99%
With sodium hydroxide at 0℃; for 1h;30%
L-alanin
56-41-7

L-alanin

toluene-4-sulfonic acid
104-15-4

toluene-4-sulfonic acid

benzyl alcohol
100-51-6

benzyl alcohol

L-alanine benzyl ester p-toluenesulfonate
42854-62-6

L-alanine benzyl ester p-toluenesulfonate

Conditions
ConditionsYield
In benzene for 10h; Reflux; Inert atmosphere;100%
at 50 - 62℃; under 15.0015 Torr; for 5.5h;98.6%
In cyclohexane; water for 4h; Dean-Stark; Reflux;92%
L-alanin
56-41-7

L-alanin

isopropyl alcohol
67-63-0

isopropyl alcohol

alanine isopropyl ester hydrochloride
39613-92-8, 62062-56-0, 62062-65-1

alanine isopropyl ester hydrochloride

Conditions
ConditionsYield
With hydrogenchloride at 80 - 85℃; for 4h; Inert atmosphere;100%
With hydrogenchloride at 80 - 85℃; for 4h;100%
With thionyl chloride at 0℃; Reflux;95%
L-alanin
56-41-7

L-alanin

1,4,5,8-naphthalenetetracarboxylic dianhydride
81-30-1

1,4,5,8-naphthalenetetracarboxylic dianhydride

(S)-2-[7-(1-carboxyethyl)-1,3,6,8-tetraoxo-3,6,7,8-tetrahydro-1H-benzo[lmn][3,8]phenanthrolin-2-yl]-propionic acid

(S)-2-[7-(1-carboxyethyl)-1,3,6,8-tetraoxo-3,6,7,8-tetrahydro-1H-benzo[lmn][3,8]phenanthrolin-2-yl]-propionic acid

Conditions
ConditionsYield
In N,N-dimethyl-formamide at 110℃; for 13h;100%
With pyridine for 12h; Heating;91%
With acetic acid for 36h; Reflux;90%
1-(2-hydroxy-2-methylpropoxy)-2,2,6,6-tetramethyl-piperidin-4-one
290821-85-1

1-(2-hydroxy-2-methylpropoxy)-2,2,6,6-tetramethyl-piperidin-4-one

L-alanin
56-41-7

L-alanin

4-(1-carboxyethylamino)-1-(2-hydroxy-2-methylpropoxy)-2,2,6,6-tetramethylpiperidine potassium salt

4-(1-carboxyethylamino)-1-(2-hydroxy-2-methylpropoxy)-2,2,6,6-tetramethylpiperidine potassium salt

Conditions
ConditionsYield
With potassium hydroxide; hydrogen; platinum(IV) oxide In methanol at 60℃; under 2327.23 Torr; for 4h;100%
L-alanin
56-41-7

L-alanin

4-bromo-2-fluoronitrobenzene
321-23-3

4-bromo-2-fluoronitrobenzene

2-(5-bromo-2-nitrophenylamino)propionic acid
99548-52-4

2-(5-bromo-2-nitrophenylamino)propionic acid

Conditions
ConditionsYield
With potassium carbonate In ethanol; water100%
With potassium carbonate In ethanol; water100%
nickel(II) nitrate hexahydrate

nickel(II) nitrate hexahydrate

L-alanin
56-41-7

L-alanin

(S)-N-(2-benzoylphenyl)-1-benzylpyrrolidine-2-carboxamide
96293-17-3, 105024-93-9, 105112-33-2

(S)-N-(2-benzoylphenyl)-1-benzylpyrrolidine-2-carboxamide

((S)-2-N-(N-benzylprolyl)aminobenzophenone)(alanine) Ni(II) complex

((S)-2-N-(N-benzylprolyl)aminobenzophenone)(alanine) Ni(II) complex

Conditions
ConditionsYield
With sodium methylate In methanol Addn. of a soln. of MeONa within 5-10 min to a mixt. of alanine, ligand and Ni-compound, heated to 60°C, allowing the mixt. to stand 1-2 h.; neutralizing the hot soln. (AcOH), pouring the mixt. into water, filtration, washing (water), drying in air.;100%
L-alanin
56-41-7

L-alanin

L-alanine-18O2 hydrochloride

L-alanine-18O2 hydrochloride

Conditions
ConditionsYield
With hydrogenchloride; 18O-labeled water In 1,4-dioxane at 100℃; for 48h; Sealed tube;100%
L-alanin
56-41-7

L-alanin

N-(allyloxycarbonyloxy)succinimide
135544-68-2

N-(allyloxycarbonyloxy)succinimide

N-allyloxycarbonyl-L-alanine
90508-28-4

N-allyloxycarbonyl-L-alanine

Conditions
ConditionsYield
With potassium carbonate In tetrahydrofuran; water at 0 - 20℃;100%
L-alanin
56-41-7

L-alanin

L-alanine hydrochloride

L-alanine hydrochloride

Conditions
ConditionsYield
With hydrogenchloride; 18O-labeled water In 1,4-dioxane at 100℃; for 48h; Sealed tube;100%
L-alanin
56-41-7

L-alanin

chloroacetic acid
79-11-8

chloroacetic acid

L-glutamic acid N,N-diacetic acid tetra sodium salt

L-glutamic acid N,N-diacetic acid tetra sodium salt

Conditions
ConditionsYield
With potassium iodide; sodium hydroxide In water at 20 - 85℃; for 4.5h;99.83%
L-alanin
56-41-7

L-alanin

4-methyl-benzaldehyde
104-87-0

4-methyl-benzaldehyde

C11H13NO2

C11H13NO2

Conditions
ConditionsYield
In 1,2-dichloro-ethane for 4h; Reflux;99.8%
L-alanin
56-41-7

L-alanin

chloroacetic acid
79-11-8

chloroacetic acid

N,N-bis(carboxymethyl)-DL-alanine trisodium salt
164462-16-2

N,N-bis(carboxymethyl)-DL-alanine trisodium salt

Conditions
ConditionsYield
With sodium hydroxide In water at 87 - 90℃; for 1.5h; pH=10 - 10.5; Temperature; pH-value; Large scale;99.75%
phthalic anhydride
85-44-9

phthalic anhydride

L-alanin
56-41-7

L-alanin

Phth-L-Ala-OH
4192-28-3

Phth-L-Ala-OH

Conditions
ConditionsYield
In water for 0.5h; microwave irradiation;99%
at 140℃; for 0.166667h;98%
at 170℃; for 2.5h;94%
L-alanin
56-41-7

L-alanin

N-(9H-fluoren-2-ylmethoxycarbonyloxy)succinimide
82911-69-1

N-(9H-fluoren-2-ylmethoxycarbonyloxy)succinimide

N-[(9H-fluoren-9-ylmethoxy)carbonyl]-L-alanine
35661-39-3

N-[(9H-fluoren-9-ylmethoxy)carbonyl]-L-alanine

Conditions
ConditionsYield
With sodium carbonate In 1,4-dioxane; water at 20℃; for 18h;99%
With sodium carbonate In N,N-dimethyl-formamide for 0.166667h; Ambient temperature;96%
With sodium carbonate In 1,4-dioxane; water at 20℃; for 18h;

56-41-7Relevant articles and documents

Squamins C–F, four cyclopeptides from the seeds of Annona globiflora

Sosa-Rueda, Javier,Domínguez-Meléndez, Vanihamin,Ortiz-Celiseo, Araceli,López-Fentanes, Fernando C.,Cuadrado, Cristina,Fernández, José J.,Daranas, Antonio Hernández,Cen-Pacheco, Francisco

, (2021/08/04)

Four cyclic octapeptides, squamins C–F, were isolated from the seeds of Annona globiflora Schltdl. These compounds share part of their amino acid sequence, -Pro-Met(O)-Tyr-Gly-Thr-, with previously reported squamins A and B. Their structures were determined using NMR spectroscopic techniques together with quantum mechanical calculations (QM-NMR), ESI-HRMS data and a modified version of Marfey's chromatographic method. All compounds showed cytotoxic activity against DU-145 (human prostate cancer) and HeLa (human cervical carcinoma) cell lines. Clearly, A. globiflora is an important source of bioactive molecules, which could promote the sustainable exploitation of this undervalued specie.

Recreating the natural evolutionary trend in key microdomains provides an effective strategy for engineering of a thermomicrobial N-demethylase

Gu, Zhenghua,Guo, Zitao,Shao, Jun,Shen, Chen,Shi, Yi,Tang, Mengwei,Xin, Yu,Zhang, Liang

, (2022/03/09)

N-demethylases have been reported to remove the methyl groups on primary or secondary amines, which could further affect the properties and functions of biomacromolecules or chemical compounds; however, the substrate scope and the robustness of N-demethylases have not been systematically investigated. Here we report the recreation of natural evolution in key microdomains of the Thermomicrobium roseum sarcosine oxidase (TrSOX), an N-demethylase with marked stability (melting temperature over 100 C) and enantioselectivity, for enhanced substrate scope and catalytic efficiency on -C-N-bonds. We obtained the structure of TrSOX by crystallization and X-ray diffraction (XRD) for the initial framework. The natural evolution in the nonconserved residues of key microdomains—including the catalytic loop, coenzyme pocket, substrate pocket, and entrance site—was then identified using ancestral sequence reconstruction (ASR), and the substitutions that accrued during natural evolution were recreated by site-directed mutagenesis. The single and double substitution variants catalyzed the N-demethylation of N-methyl-L-amino acids up to 1800- and 6000-fold faster than the wild type, respectively. Additionally, these single substitution variants catalyzed the terminal N-demethylation of non-amino-acid compounds and the oxidation of the main chain -C-N- bond to a -C=N- bond in the nitrogen-containing heterocycle. Notably, these variants retained the enantioselectivity and stability of the initial framework. We conclude that the variants of TrSOX are of great potential use in N-methyl enantiomer resolution, main-chain Schiff base synthesis, and alkaloid modification or degradation.

Direct monitoring of biocatalytic deacetylation of amino acid substrates by1H NMR reveals fine details of substrate specificity

De Cesare, Silvia,McKenna, Catherine A.,Mulholland, Nicholas,Murray, Lorna,Bella, Juraj,Campopiano, Dominic J.

supporting information, p. 4904 - 4909 (2021/06/16)

Amino acids are key synthetic building blocks that can be prepared in an enantiopure form by biocatalytic methods. We show that thel-selective ornithine deacetylase ArgE catalyses hydrolysis of a wide-range ofN-acyl-amino acid substrates. This activity was revealed by1H NMR spectroscopy that monitored the appearance of the well resolved signal of the acetate product. Furthermore, the assay was used to probe the subtle structural selectivity of the biocatalyst using a substrate that could adopt different rotameric conformations.

Highly Stable Zr(IV)-Based Metal-Organic Frameworks for Chiral Separation in Reversed-Phase Liquid Chromatography

Jiang, Hong,Yang, Kuiwei,Zhao, Xiangxiang,Zhang, Wenqiang,Liu, Yan,Jiang, Jianwen,Cui, Yong

supporting information, p. 390 - 398 (2021/01/13)

Separation of racemic mixtures is of great importance and interest in chemistry and pharmacology. Porous materials including metal-organic frameworks (MOFs) have been widely explored as chiral stationary phases (CSPs) in chiral resolution. However, it remains a challenge to develop new CSPs for reversed-phase high-performance liquid chromatography (RP-HPLC), which is the most popular chromatographic mode and accounts for over 90% of all separations. Here we demonstrated for the first time that highly stable Zr-based MOFs can be efficient CSPs for RP-HPLC. By elaborately designing and synthesizing three tetracarboxylate ligands of enantiopure 1,1′-biphenyl-20-crown-6, we prepared three chiral porous Zr(IV)-MOFs with the framework formula [Zr6O4(OH)8(H2O)4(L)2]. They share the same flu topological structure but channels of different sizes and display excellent tolerance to water, acid, and base. Chiral crown ether moieties are periodically aligned within the framework channels, allowing for stereoselective recognition of guest molecules via supramolecular interactions. Under acidic aqueous eluent conditions, the Zr-MOF-packed HPLC columns provide high resolution, selectivity, and durability for the separation of a variety of model racemates, including unprotected and protected amino acids and N-containing drugs, which are comparable to or even superior to several commercial chiral columns for HPLC separation. DFT calculations suggest that the Zr-MOF provides a confined microenvironment for chiral crown ethers that dictates the separation selectivity.

Inherently chiral dialkyloxy-calix[4]arene acetic acids as enantiodiscriminating additives for high-performance liquid chromatography separation of d,l-amino acids

Kalchenko, Olga I.,Trybrat, Oleksandr O.,Yesypenko, Oleksandr A.,Dyakonenko, Viktoriya V.,Shishkina, Svitlana V.,Kalchenko, Vitali I.

, p. 722 - 730 (2021/08/26)

Inherently chiral dialkyloxy-calix[4]arene acetic acids with asymmetric placement of substituents on the lower rim of the macrocycle were first studied as enantiodiscriminating additives to the mobile phase MeCN/H2O/HCOOH (75/25/0.02 by volume) in the high-performance liquid chromatography (HPLC) separation of d,l-alanine and d,l-valine on the achiral stationary phase ZORBAX Original CN. The dependence of enantio-binding properties on the position of alkyl groups is demonstrated. The highest resolution (1.65) and enantioselectivity (1.80) were obtained for the 1,2-dipropyloxy-calix[4]arene acetic acid.

Biosynthesis ofl-alanine fromcis-butenedioic anhydride catalyzed by a triple-enzyme cascadeviaa genetically modified strain

Cui, Ruizhi,Liu, Zhongmei,Yu, Puyi,Zhou, Li,Zhou, Zhemin

supporting information, p. 7290 - 7298 (2021/09/28)

In industry,l-alanine is biosynthesized using fermentation methods or catalyzed froml-aspartic acid by aspartate β-decarboxylase (ASD). In this study, a triple-enzyme system was developed to biosynthesizel-alanine fromcis-butenedioic anhydride, which was cost-efficient and could overcome the shortcomings of fermentation. Maleic acid formed bycis-butenedioic anhydride dissolving in water was transformed tol-alanineviafumaric acid andl-asparagic acid catalyzed by maleate isomerase (MaiA), aspartase (AspA) and ASD, respectively. The enzymatic properties of ASD from different origins were investigated and compared, as ASD was the key enzyme of the triple-enzyme cascade. Based on cofactor dependence and cooperation with the other two enzymes, a suitable ASD was chosen. Two of the three enzymes, MaiA and ASD, were recombinant enzymes cloned into a dual-promoter plasmid for overexpression; another enzyme, AspA, was the genomic enzyme of the host cell, in which AspA was enhanced by a T7promoter. Two fumarases in the host cell genome were deleted to improve the utilization of the intermediate fumaric acid. The conversion of whole-cell catalysis achieved 94.9% in 6 h, and the productivity given in our system was 28.2 g (L h)?1, which was higher than the productivity that had been reported. A catalysis-extraction circulation process for the synthesis ofl-alanine was established based on high-density fermentation, and the wastewater generated by this process was less than 34% of that by the fermentation process. Our results not only established a new green manufacturing process forl-alanine production fromcis-butenedioic anhydride but also provided a promising strategy that could consider both catalytic ability and cell growth burden for multi-enzyme cascade catalysis.

Engineering the large pocket of an (S)-selective transaminase for asymmetric synthesis of (S)-1-amino-1-phenylpropane

Liu, He,Wang, Hualei,Wei, Dongzhi,Xie, Youyu,Xu, Feng,Xu, Xiangyang,Yang, Lin

, p. 2461 - 2470 (2021/04/22)

Amine transaminases offer an environmentally benign chiral amine asymmetric synthesis route. However, their catalytic efficiency towards bulky chiral amine asymmetric synthesis is limited by the natural geometric structure of the small pocket, representing a great challenge for industrial applications. Here, we rationally engineered the large binding pocket of an (S)-selective ?-transaminase BPTA fromParaburkholderia phymatumto relieve the inherent restriction caused by the small pocket and efficiently transform the prochiral aryl alkyl ketone 1-propiophenone with a small substituent larger than the methyl group. Based on combined molecular docking and dynamic simulation analyses, we identified a non-classical substrate conformation, located in the active site with steric hindrance and undesired interactions, to be responsible for the low catalytic efficiency. By relieving the steric barrier with W82A, we improved the specific activity by 14-times compared to WT. A p-p stacking interaction was then introduced by M78F and I284F to strengthen the binding affinity with a large binding pocket to balance the undesired interactions generated by F44. T440Q further enhanced the substrate affinity by providing a more hydrophobic and flexible environment close to the active site entry. Finally, we constructed a quadruple variant M78F/W82A/I284F/T440Q to generate the most productive substrate conformation. The 1-propiophenone catalytic efficiency of the mutant was enhanced by more than 470-times in terms ofkcat/KM, and the conversion increased from 1.3 to 94.4% compared with that of WT, without any stereoselectivity loss (ee > 99.9%). Meanwhile, the obtained mutant also showed significant activity improvements towards various aryl alkyl ketones with a small substituent larger than the methyl group ranging between 104- and 230-fold, demonstrating great potential for the efficient synthesis of enantiopure aryl alkyl amines with steric hindrance in the small binding pocket.

Targeted Isolation of Asperheptatides from a Coral-Derived Fungus Using LC-MS/MS-Based Molecular Networking and Antitubercular Activities of Modified Cinnamate Derivatives

Chao, Rong,Hou, Xue-Mei,Xu, Wei-Feng,Hai, Yang,Wei, Mei-Yan,Wang, Chang-Yun,Gu, Yu-Cheng,Shao, Chang-Lun

, p. 11 - 19 (2021/01/14)

Under the guidance of MS/MS-based molecular networking, four new cycloheptapeptides, namely, asperheptatides A-D (1-4), were isolated together with three known analogues, asperversiamide A-C (5-7), from the coral-derived fungus Aspergillus versicolor. The planar structures of the two major compounds, asperheptatides A and B (1 and 2), were determined by comprehensive spectroscopic data analysis. The absolute configurations of the amino acid residues were determined by advanced Marfey's method. The two structurally related trace metabolites, asperheptatides C and D (3 and 4), were characterized by ESI-MS/MS fragmentation methods. A series of new derivatives (8-26) of asperversiamide A (5) were semisynthesized. The antitubercular activities of 1, 2, and 5-26 against Mycobacterium tuberculosis H37Ra were also evaluated. Compounds 9, 13, 23, and 24 showed moderate activities with MIC values of 12.5 μM, representing a potential new class of antitubercular agents.

Leveraging Peptaibol Biosynthetic Promiscuity for Next-Generation Antiplasmodial Therapeutics

Lee, Jin Woo,Collins, Jennifer E.,Wendt, Karen L.,Chakrabarti, Debopam,Cichewicz, Robert H.

supporting information, p. 503 - 517 (2021/03/01)

Malaria remains a worldwide threat, afflicting over 200 million people each year. The emergence of drug resistance against existing therapeutics threatens to destabilize global efforts aimed at controlling Plasmodium spp. parasites, which is expected to leave vast portions of humanity unprotected against the disease. To address this need, systematic testing of a fungal natural product extract library assembled through the University of Oklahoma Citizen Science Soil Collection Program has generated an initial set of bioactive extracts that exhibit potent antiplasmodial activity (EC50 25 μM, selectivity index > 250). The unique chemodiversity afforded by these fungal isolates serves to unlock new opportunities for translating peptaibols into a bioactive scaffold worthy of further development.

Mechanistic Insight into the Origin of Stereoselectivity in the Ribose-Mediated Strecker Synthesis of Alanine

Legnani, Luca,Darù, Andrea,Jones, Alexander X.,Blackmond, Donna G.

supporting information, p. 7852 - 7858 (2021/05/26)

Enantioenriched amino acids are produced in a hydrolytic kinetic resolution of racemic aminonitriles mediated by chiral pentose sugars. Experimental kinetic and spectroscopic results combined with DFT computational studies and microkinetic modeling help to identify the nature of the intermediate species and provide insight into the stereoselectivity of their hydrolysis in the prebiotically relevant ribose-alanine system. These studies support a synergistic role for sugars and amino acids in the emergence of homochirality in biological molecules.

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