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1113-60-6

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1113-60-6 Usage

Occurrence

Reported found in blue cheese, provolone cheese, beer and cocoa

Uses

β-Hydroxypyruvic Acid is a metabolite involved in the pathway of carbon in photorespiration. It can also be used to treat fiber.

Definition

ChEBI: A 2-oxo monocarboxylic acid that is pyruvic acid in which one of the methyl hydrogens is substituted by a hydroxy group. It is an intermediate involved in the glycine and serine metabolism.

Biochem/physiol Actions

Metabolite involved in the pathway of carbon in photorespiration.

Check Digit Verification of cas no

The CAS Registry Mumber 1113-60-6 includes 7 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 4 digits, 1,1,1 and 3 respectively; the second part has 2 digits, 6 and 0 respectively.
Calculate Digit Verification of CAS Registry Number 1113-60:
(6*1)+(5*1)+(4*1)+(3*3)+(2*6)+(1*0)=36
36 % 10 = 6
So 1113-60-6 is a valid CAS Registry Number.
InChI:InChI=1/C3H4O4/c4-1-2(5)3(6)7/h4H,1H2,(H,6,7)/p-1

1113-60-6SDS

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 3-hydroxypyruvic acid

1.2 Other means of identification

Product number -
Other names 3-hydroxy-2-oxopropanoic acid

1.3 Recommended use of the chemical and restrictions on use

Identified uses For industry use only.
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:1113-60-6 SDS

1113-60-6Synthetic route

glycerol
56-81-5

glycerol

A

glycolic Acid
79-14-1

glycolic Acid

B

3-hydroxy-2-oxopropionic acid
1113-60-6

3-hydroxy-2-oxopropionic acid

C

dihydroxyacetone
96-26-4

dihydroxyacetone

Conditions
ConditionsYield
With pyridine; dodecacarbonyl triosmium; dihydrogen peroxide In acetonitrile at 60℃; for 13h; Kinetics; Temperature;A 8%
B 1.5%
C 7.5%
With pyridine; dodecacarbonyl triosmium; dihydrogen peroxide In acetonitrile at 60℃; for 5h; Kinetics; Temperature;A 4%
B 2.7%
C 8.3%
D-Serine
312-84-5

D-Serine

3-hydroxy-2-oxopropionic acid
1113-60-6

3-hydroxy-2-oxopropionic acid

Conditions
ConditionsYield
With D-amino acid oxide ase from rat's kidney; oxygen
With 2,2'-azinobis(3-ethylbenzthiazolinesulfonate); recombinant Trigonopsis variabilis D-amino acid oxidase, Arg169Ala/Arg220Ala mutant; horseradish peroxidase at 30℃; pH=8; Kinetics; Reagent/catalyst; Temperature; aq. phosphate buffer; Enzymatic reaction;
With human D-amino acid oxidase; Aspergillus niger catalase; flavin adenine dinucleotide at 37℃; for 0.25h; pH=8.3; aq. phosphate buffer; Enzymatic reaction;
DL-threo-β-hydroxyaspartic acid
4294-45-5

DL-threo-β-hydroxyaspartic acid

chloroamine-T
127-65-1

chloroamine-T

A

3-hydroxy-2-oxopropionic acid
1113-60-6

3-hydroxy-2-oxopropionic acid

B

Glyoxal
131543-46-9

Glyoxal

Conditions
ConditionsYield
reag.die neutralen Salze;
L-Tartaric acid
87-69-4

L-Tartaric acid

3-hydroxy-2-oxopropionic acid
1113-60-6

3-hydroxy-2-oxopropionic acid

Conditions
ConditionsYield
Electrolysis.Elektrolyse in wss. Loesung an Platin;
dihydroxyacetone
96-26-4

dihydroxyacetone

3-hydroxy-2-oxopropionic acid
1113-60-6

3-hydroxy-2-oxopropionic acid

Conditions
ConditionsYield
With copper(I) sulfate; copper(II) sulfate at 80℃;
bromopyruvic acid
1113-59-3

bromopyruvic acid

3-hydroxy-2-oxopropionic acid
1113-60-6

3-hydroxy-2-oxopropionic acid

Conditions
ConditionsYield
With sodium hydroxide; water
With sodium hydroxide In water
With alkaline buffer
With lithium hydroxide Yield given;
With alkaline buffer Rate constant; Kinetics; the mechanism of the reaction was investigated by polarography in aqueous solution;
2-oxo-propionic acid
127-17-3

2-oxo-propionic acid

3-hydroxy-2-oxopropionic acid
1113-60-6

3-hydroxy-2-oxopropionic acid

Conditions
ConditionsYield
With iodine; glycine
glyceric acid
473-81-4

glyceric acid

3-hydroxy-2-oxopropionic acid
1113-60-6

3-hydroxy-2-oxopropionic acid

Conditions
ConditionsYield
With αβ-dihydroxyacid dehydratase EC 4.2.1.9 of Salmonella typhimurium Product distribution; αβ-dihydroxyacid dehydratase activity;
With Fructose 1,6-bisphosphate; Bacillus stearothermophilus; triethanolamine hydrochloride; NADH at 25℃; Rate constant; Equilibrium constant; also in presence of Gln102 or Asn enzyme;
3-hydroxy-2-oxopropionic acid
1113-60-6

3-hydroxy-2-oxopropionic acid

Conditions
ConditionsYield
With benzylviologen cation radical In water at 25℃; Equilibrium constant; cell free extract of Proteus vulgaris (potassium phosphate buffer pH 7.0), Vmax;
3-hydroxy-2-oxopropionic acid
1113-60-6

3-hydroxy-2-oxopropionic acid

Conditions
ConditionsYield
With Fructose 1,6-bisphosphate; oxidized form of nicotineamide adenine dinucleotide In water at 25℃; Rate constant; pH 8.5, reaction in the presence of L-lactate dehydrogenase from Bacillus stearothermophilus (BSLDH 102R) or other enzymes;
2,3-Dihydroxy-propionic acid
473-81-4, 600-19-1, 6000-40-4, 28305-26-2

2,3-Dihydroxy-propionic acid

3-hydroxy-2-oxopropionic acid
1113-60-6

3-hydroxy-2-oxopropionic acid

Conditions
ConditionsYield
With Fructose 1,6-bisphosphate; oxidized form of nicotineamide adenine dinucleotide In water at 25℃; Rate constant; pH 8.5, reaction in the presence of L-lactate dehydrogenase from Bacillus stearothermophilus (BSLDH 102R) or other enzymes;
L-serin
56-45-1

L-serin

3-hydroxy-2-oxopropionic acid
1113-60-6

3-hydroxy-2-oxopropionic acid

Conditions
ConditionsYield
With HEPES buffer; pyridoxal 5'-phosphate; glyoxylate gloxylate aminotransferase;
With potassium nitrososulfonate In various solvent(s) at 26.9℃; Thermodynamic data; Rate constant; ΔH (activ.), ΔS (activ.);
With L-alanine dehydrogenase from Bacillus subtilis; nicotinamide adenine dinucleotide In aq. phosphate buffer at 25℃; pH=8; Enzymatic reaction;
With transaminase Enzymatic reaction;
With recombinant Pseudoalteromonas luteoviolacea L-amino acid oxidase In aq. phosphate buffer at 37℃; for 0.25h; pH=7.4; Enzymatic reaction;
dihydroxyacetone
96-26-4

dihydroxyacetone

copper(II) sulfate
7758-99-8

copper(II) sulfate

3-hydroxy-2-oxopropionic acid
1113-60-6

3-hydroxy-2-oxopropionic acid

Conditions
ConditionsYield
at 80℃;
collodium wool

collodium wool

3-hydroxy-2-oxopropionic acid
1113-60-6

3-hydroxy-2-oxopropionic acid

glyceric acid
473-81-4

glyceric acid

dihydrogen peroxide
7722-84-1

dihydrogen peroxide

ferro salt

ferro salt

3-hydroxy-2-oxopropionic acid
1113-60-6

3-hydroxy-2-oxopropionic acid

hydroxy-pyruvic acid , lithium salt

hydroxy-pyruvic acid , lithium salt

3-hydroxy-2-oxopropionic acid
1113-60-6

3-hydroxy-2-oxopropionic acid

Conditions
ConditionsYield
With ion exchanger (H+-form)
nitrocellulose

nitrocellulose

3-hydroxy-2-oxopropionic acid
1113-60-6

3-hydroxy-2-oxopropionic acid

α-amino-α'-oxy-succinic acid , neutral salts

α-amino-α'-oxy-succinic acid , neutral salts

A

3-hydroxy-2-oxopropionic acid
1113-60-6

3-hydroxy-2-oxopropionic acid

B

Glyoxal
131543-46-9

Glyoxal

Conditions
ConditionsYield
With sodium hypochlorite
With chloroamine-T
DL-threo-β-hydroxyaspartic acid
4294-45-5

DL-threo-β-hydroxyaspartic acid

sodium hypochlorite

sodium hypochlorite

A

3-hydroxy-2-oxopropionic acid
1113-60-6

3-hydroxy-2-oxopropionic acid

B

Glyoxal
131543-46-9

Glyoxal

Conditions
ConditionsYield
reag.die neutralen Salze;
L-Tartaric acid
87-69-4

L-Tartaric acid

water
7732-18-5

water

A

3-hydroxy-2-oxopropionic acid
1113-60-6

3-hydroxy-2-oxopropionic acid

B

2,3-dioxo-propionic acid
815-53-2

2,3-dioxo-propionic acid

C

dihydroxytartaric acid
76-30-2

dihydroxytartaric acid

D

2-oxo-propionic acid
127-17-3

2-oxo-propionic acid

Conditions
ConditionsYield
Diese Reaktion geben auch die Natriumsalze; weitere Produkte:Formylessigsaeure, Mesoxalsaeure, Tartronsaeure, Glyoxylsaeure,usw..Electrolysis;
glycerol
56-81-5

glycerol

A

glycolic Acid
79-14-1

glycolic Acid

B

3-hydroxy-2-oxopropionic acid
1113-60-6

3-hydroxy-2-oxopropionic acid

C

glyceric acid
473-81-4

glyceric acid

D

dihydroxyacetone
96-26-4

dihydroxyacetone

Conditions
ConditionsYield
With tris(μ-oxo)di[(1,4,7-trimethyl-1,4,7-triazanonane)manganese(IV)] hexafluorophosphate; dihydrogen peroxide; oxalic acid In water; acetonitrile at 22℃; for 0.5h; Kinetics; Concentration; Reagent/catalyst; Time;A 0.1 %Chromat.
B 0.7 %Chromat.
C 0.1 %Chromat.
D 4.2 %Chromat.
α-ketoglutaric acid
328-50-7

α-ketoglutaric acid

L-serin
56-45-1

L-serin

A

3-hydroxy-2-oxopropionic acid
1113-60-6

3-hydroxy-2-oxopropionic acid

B

L-glutamic acid
56-86-0

L-glutamic acid

Conditions
ConditionsYield
With Erwinia carotovora subsp. carotovora aromatic aminotransferase PAT1 Enzymatic reaction;
glycerol
56-81-5

glycerol

A

formic acid
64-18-6

formic acid

B

glycolic Acid
79-14-1

glycolic Acid

C

tartronic acid
80-69-3

tartronic acid

D

3-hydroxy-2-oxopropionic acid
1113-60-6

3-hydroxy-2-oxopropionic acid

E

glyceric acid
473-81-4

glyceric acid

F

dihydroxyacetone
96-26-4

dihydroxyacetone

G

oxalic acid
144-62-7

oxalic acid

H

Glyoxilic acid
298-12-4

Glyoxilic acid

Conditions
ConditionsYield
With oxygen; sodium hydroxide In water at 49.84℃; for 2h;
With oxygen; sodium hydroxide In water at 49.84℃; for 2h;
glycerol
56-81-5

glycerol

A

glycolic Acid
79-14-1

glycolic Acid

B

tartronic acid
80-69-3

tartronic acid

C

3-hydroxy-2-oxopropionic acid
1113-60-6

3-hydroxy-2-oxopropionic acid

D

glyceric acid
473-81-4

glyceric acid

E

acetonedicarboxylic acid
473-90-5

acetonedicarboxylic acid

F

oxalic acid
144-62-7

oxalic acid

Conditions
ConditionsYield
With 0.4 wt.% gold/carbon nanospheres; oxygen; sodium hydroxide at 59.84℃; under 3750.38 Torr; for 4h;
glycerol
56-81-5

glycerol

A

formic acid
64-18-6

formic acid

B

glycolic Acid
79-14-1

glycolic Acid

C

tartronic acid
80-69-3

tartronic acid

D

3-hydroxy-2-oxopropionic acid
1113-60-6

3-hydroxy-2-oxopropionic acid

E

glyceric acid
473-81-4

glyceric acid

F

dihydroxyacetone
96-26-4

dihydroxyacetone

G

malonic acid
141-82-2

malonic acid

H

acetonedicarboxylic acid
473-90-5

acetonedicarboxylic acid

I

oxalic acid
144-62-7

oxalic acid

J

2-oxo-propionic acid
127-17-3

2-oxo-propionic acid

K

Glyceraldehyde
56-82-6

Glyceraldehyde

L

Glyoxilic acid
298-12-4

Glyoxilic acid

Conditions
ConditionsYield
With sodium hydroxide In water at 25℃; Reagent/catalyst; Electrochemical reaction;
lanasol yellow 4G

lanasol yellow 4G

A

acetamide
60-35-5

acetamide

B

3-hydroxy-2-oxopropionic acid
1113-60-6

3-hydroxy-2-oxopropionic acid

C

2-hydroxyiminopropanoic acid
2211-14-5

2-hydroxyiminopropanoic acid

D

2-hydroxyacrylic acid
19071-34-2

2-hydroxyacrylic acid

E

4-hydroxysalicylic acid
89-86-1

4-hydroxysalicylic acid

F

2,5-dihydroxybenzoic acid.
490-79-9

2,5-dihydroxybenzoic acid.

G

ethanimidic acid

ethanimidic acid

H

acetic acid
64-19-7

acetic acid

Conditions
ConditionsYield
With potassium bromate; sodium sulfate for 8h; pH=6; Kinetics; Reagent/catalyst; Irradiation; Electrochemical reaction;
glycerol
56-81-5

glycerol

A

3-hydroxy-2-oxopropionic acid
1113-60-6

3-hydroxy-2-oxopropionic acid

B

acetic acid
64-19-7

acetic acid

Conditions
ConditionsYield
With dihydrogen peroxide In acetonitrile at 80℃; for 24h; Catalytic behavior; Sonication; Sealed tube;
glycerol
56-81-5

glycerol

A

formic acid
64-18-6

formic acid

B

3-hydroxy-2-oxopropionic acid
1113-60-6

3-hydroxy-2-oxopropionic acid

C

glyceric acid
473-81-4

glyceric acid

D

Glycolaldehyde
141-46-8

Glycolaldehyde

Conditions
ConditionsYield
With dihydrogen peroxide at 60℃; for 24h; Sonication; Sealed tube;
glycerol
56-81-5

glycerol

A

formic acid
64-18-6

formic acid

B

3-hydroxy-2-oxopropionic acid
1113-60-6

3-hydroxy-2-oxopropionic acid

C

glyceric acid
473-81-4

glyceric acid

Conditions
ConditionsYield
With dihydrogen peroxide; nickel In acetonitrile at 80℃; for 24h; Sonication; Sealed tube;
3-hydroxy-2-oxopropionic acid
1113-60-6

3-hydroxy-2-oxopropionic acid

D-Serine
312-84-5

D-Serine

Conditions
ConditionsYield
With isopropylamine In aq. buffer for 20h; pH=7.0; Enzymatic reaction;95%
With (R)-selective ω-transaminase from arthrobacter sp.; isopropylamine In aq. phosphate buffer at 37℃; for 2h; pH=7; Reagent/catalyst; Enzymatic reaction;n/a
1,2-dimethoxybenzene
91-16-7

1,2-dimethoxybenzene

3-hydroxy-2-oxopropionic acid
1113-60-6

3-hydroxy-2-oxopropionic acid

5,6-dimethoxy-1,2-indanedione
42337-64-4

5,6-dimethoxy-1,2-indanedione

Conditions
ConditionsYield
Stage #1: 3-hydroxy-2-oxopropionic acid With chlorosulfonic acid In dichloromethane at 0 - 20℃; for 3h; Large scale;
Stage #2: 1,2-dimethoxybenzene In dichloromethane at 0 - 20℃; for 7h; Large scale;
90%
Stage #1: 1,2-dimethoxybenzene; 3-hydroxy-2-oxopropionic acid With methanesulfonic acid; phosphorus pentoxide In dichloromethane at 0 - 60℃; for 6h; Large scale;
Stage #2: 1,2-dimethoxybenzene In dichloromethane at 0 - 20℃; for 7h; Large scale;
89%
3-hydroxy-2-oxopropionic acid
1113-60-6

3-hydroxy-2-oxopropionic acid

(R)-(+)-4-hydroxy-2-methylidene-5-oxo-pentanenitrile

(R)-(+)-4-hydroxy-2-methylidene-5-oxo-pentanenitrile

(-)-(4R,5S)-4,5,7-trihydroxy-2-methylidene-6-oxo-heptanenitrile
681826-38-0

(-)-(4R,5S)-4,5,7-trihydroxy-2-methylidene-6-oxo-heptanenitrile

Conditions
ConditionsYield
With thiamine pyrophosphate; transketolase from S. cerevisiae; magnesium chloride In various solvent(s) at 20℃; for 14h; pH=7.5;73%
3-hydroxy-2-oxopropionic acid
1113-60-6

3-hydroxy-2-oxopropionic acid

D-ribose
50-69-1

D-ribose

sedoheptulose
3019-74-7

sedoheptulose

Conditions
ConditionsYield
With thiamine pyrophosphate; magnesium chloride at 25℃; spinach transketolase, pH 7.5;70%
With thiamine pyrophosphate; magnesium chloride; transketolase from spinach In water glycyl-glycine buffer 0,05 M (pH 7.5);
3-hydroxy-2-oxopropionic acid
1113-60-6

3-hydroxy-2-oxopropionic acid

(2R,3S)-2,3-Dihydroxy-pent-4-enal
143168-74-5

(2R,3S)-2,3-Dihydroxy-pent-4-enal

5,6-dideoxy-D-arabino-hept-5-en-2-ulose
143106-72-3

5,6-dideoxy-D-arabino-hept-5-en-2-ulose

Conditions
ConditionsYield
With sodium hydroxide; thiamine diphosphate; Lithium hydroxypyruvate; magnesium chloride In water 3-5 d, transketolase (EC 2.2.1.1) from yeast;63%
3-hydroxy-2-oxopropionic acid
1113-60-6

3-hydroxy-2-oxopropionic acid

D-erythro-4,5-dideoxy-pent-4-enose
89886-12-4

D-erythro-4,5-dideoxy-pent-4-enose

5,6-dideoxy-L-xylo-hept-5-en-2-ulose
143106-71-2

5,6-dideoxy-L-xylo-hept-5-en-2-ulose

Conditions
ConditionsYield
With sodium hydroxide; thiamine diphosphate; Lithium hydroxypyruvate; magnesium chloride In water 3-5 d, transketolase (EC 2.2.1.1) from yeast;60%
3-hydroxy-2-oxopropionic acid
1113-60-6

3-hydroxy-2-oxopropionic acid

Glycolaldehyde
141-46-8

Glycolaldehyde

L-erythrulose
533-50-6

L-erythrulose

Conditions
ConditionsYield
With thiamine pyrophosphate; magnesium chloride; transketolase from spinach 0.1 M glycylglycine buffer, pH 7.5;60%
With sodium hydroxide; thiamine diphosphate; Lithium hydroxypyruvate; magnesium chloride In water 3-5 d, transketolase (EC 2.2.1.1) from yeast;60%
at 37℃; transketolase, thiamine pyrophosphate, MgCl2, glycylglycine buffer pH 7.6; other aldehydes;
With thiamine pyrophosphate; magnesium chloride; transketolase from spinach In water glycyl-glycine buffer 0,05 M (pH 7.5);
at 37℃; transketolase, thiamine pyrophosphate, MgCl2, glycylglycine buffer pH 7.6;
D-Glyceraldehyde
453-17-8

D-Glyceraldehyde

3-hydroxy-2-oxopropionic acid
1113-60-6

3-hydroxy-2-oxopropionic acid

fructonic acid
669-90-9

fructonic acid

Conditions
ConditionsYield
With recombinant aldolase B2T1L6 from Burkholderia phytofirmans; manganese(ll) chloride In aq. buffer for 20h; pH=8; Catalytic behavior; Reagent/catalyst; Aldol Addition; Green chemistry; Enzymatic reaction; stereoselective reaction;55%
3-hydroxy-2-oxopropionic acid
1113-60-6

3-hydroxy-2-oxopropionic acid

C5H10O2S
1186294-83-6

C5H10O2S

C7H14O4S
1186294-81-4

C7H14O4S

Conditions
ConditionsYield
With transketolase pH=7.5;47%
3-hydroxy-2-oxopropionic acid
1113-60-6

3-hydroxy-2-oxopropionic acid

(+/-)-2-hydroxybutanal
86943-35-3

(+/-)-2-hydroxybutanal

5,6-dideoxy-D-threo-hex-2-ulose
117625-98-6

5,6-dideoxy-D-threo-hex-2-ulose

Conditions
ConditionsYield
With thiamine diphosphate; magnesium chloride transketolase (TK) (EC 2.2.1.1), pH 7.5;45%
With sodium hydroxide; thiamine diphosphate; Lithium hydroxypyruvate; magnesium chloride In water 3-5 d, transketolase (EC 2.2.1.1) from yeast;45%
3-hydroxy-2-oxopropionic acid
1113-60-6

3-hydroxy-2-oxopropionic acid

3-vinyl-2-hydroxypropanal
138851-90-8

3-vinyl-2-hydroxypropanal

5,6,7-trideoxy-D-threo-hept-5-en-ulose
143106-70-1

5,6,7-trideoxy-D-threo-hept-5-en-ulose

Conditions
ConditionsYield
With sodium hydroxide; thiamine diphosphate; Lithium hydroxypyruvate; magnesium chloride In water 3-5 d, transketolase (EC 2.2.1.1) from yeast;45%
2-hydroxypropanal
3913-65-3

2-hydroxypropanal

3-hydroxy-2-oxopropionic acid
1113-60-6

3-hydroxy-2-oxopropionic acid

(3S,4R)-1,3,4-trihydroxypentan-2-one
80648-97-1

(3S,4R)-1,3,4-trihydroxypentan-2-one

Conditions
ConditionsYield
With sodium hydroxide; thiamine diphosphate; Lithium hydroxypyruvate; magnesium chloride In water 3-5 d, transketolase (EC 2.2.1.1) from yeast;44%
With sodium hydroxide; thiamine diphosphate; Lithium hydroxypyruvate; magnesium chloride In water 3-5 d, transketolase (EC 2.2.1.1) from yeast; other aldehydes;44%
3-hydroxy-2-oxopropionic acid
1113-60-6

3-hydroxy-2-oxopropionic acid

4-hydroxy-2-methylidene-5-oxo-pentanenitrile

4-hydroxy-2-methylidene-5-oxo-pentanenitrile

A

(S)-(-)-4-hydroxy-2-methylidene-5-oxo-pentanenitrile

(S)-(-)-4-hydroxy-2-methylidene-5-oxo-pentanenitrile

B

(-)-(4R,5S)-4,5,7-trihydroxy-2-methylidene-6-oxo-heptanenitrile
681826-38-0

(-)-(4R,5S)-4,5,7-trihydroxy-2-methylidene-6-oxo-heptanenitrile

Conditions
ConditionsYield
With thiamine pyrophosphate; transketolase from S. cerevisiae; magnesium chloride In various solvent(s) at 20℃; for 14h; pH=7.5;A 43%
B 38%
3-hydroxy-2-oxopropionic acid
1113-60-6

3-hydroxy-2-oxopropionic acid

2-hydroxylpentanal
87503-46-6

2-hydroxylpentanal

5,6,7-trideoxy-D-threo-2-heptulose
143106-67-6

5,6,7-trideoxy-D-threo-2-heptulose

Conditions
ConditionsYield
With sodium hydroxide; thiamine diphosphate; Lithium hydroxypyruvate; magnesium chloride In water 3-5 d, transketolase (EC 2.2.1.1) from yeast;39%
3-hydroxy-2-oxopropionic acid
1113-60-6

3-hydroxy-2-oxopropionic acid

2-hydroxy-3-methoxypropionaldehyde
35830-93-4

2-hydroxy-3-methoxypropionaldehyde

5-O-methyl-D-threo-2-pentulose
143106-68-7

5-O-methyl-D-threo-2-pentulose

Conditions
ConditionsYield
With sodium hydroxide; thiamine diphosphate; Lithium hydroxypyruvate; magnesium chloride In water 3-5 d, transketolase (EC 2.2.1.1) from yeast;38%
3-hydroxy-2-oxopropionic acid
1113-60-6

3-hydroxy-2-oxopropionic acid

acetaldehyde
75-07-0

acetaldehyde

4-Deoxy-L-erythrulose
139573-33-4

4-Deoxy-L-erythrulose

Conditions
ConditionsYield
With thiamine pyrophosphate; magnesium chloride; transketolase from spinach In water for 24h; glycyl-glycine buffer 0,05 M (pH 7.5);36%
3-hydroxy-2-oxopropionic acid
1113-60-6

3-hydroxy-2-oxopropionic acid

4-Deoxy-L-erythrulose
139573-33-4

4-Deoxy-L-erythrulose

6-deoxy-L-xylo-hexulose
18545-94-3

6-deoxy-L-xylo-hexulose

Conditions
ConditionsYield
With thiamine pyrophosphate; Tris buffer; magnesium chloride In water for 48h; transketolase, Serratia liquefaciens;35%
3-hydroxy-2-oxopropionic acid
1113-60-6

3-hydroxy-2-oxopropionic acid

(+/-)-2-hydroxy-3-butenal
75326-51-1

(+/-)-2-hydroxy-3-butenal

5,6-dideoxy-D-threo-hex-5-en-2-ulose
143106-69-8

5,6-dideoxy-D-threo-hex-5-en-2-ulose

Conditions
ConditionsYield
With sodium hydroxide; thiamine diphosphate; Lithium hydroxypyruvate; magnesium chloride In water for 96h; transketolase (EC 2.2.1.1) from yeast, pH 6.5;30%
3-hydroxy-2-oxopropionic acid
1113-60-6

3-hydroxy-2-oxopropionic acid

2,3-dihydroxybutyraldehyde
5144-76-3, 14214-86-9

2,3-dihydroxybutyraldehyde

A

6-deoxy-L-xylo-hexulose
18545-94-3

6-deoxy-L-xylo-hexulose

B

5-deoxy-D-fructose
4429-06-5

5-deoxy-D-fructose

Conditions
ConditionsYield
With thiamine pyrophosphate; HEPES buffer; magnesium chloride In water spinach transketolase enzyme extract;A 23%
B 25%
3-hydroxy-2-oxopropionic acid
1113-60-6

3-hydroxy-2-oxopropionic acid

Glyceraldehyde
56-82-6

Glyceraldehyde

xylulose
551-84-8

xylulose

Conditions
ConditionsYield
With thiamine pyrophosphate; magnesium chloride; transketolase from spinach 0.1 M glycylglycine buffer, pH 7.5;24%
3-hydroxy-2-oxopropionic acid
1113-60-6

3-hydroxy-2-oxopropionic acid

propionaldehyde
123-38-6

propionaldehyde

(3S)-1,3-dihydroxypentan-2-one
147523-69-1

(3S)-1,3-dihydroxypentan-2-one

Conditions
ConditionsYield
at 37℃; transketolase, thiamine pyrophosphate, MgCl2, glycylglycine buffer pH 7.6;23%
3-hydroxy-2-oxopropionic acid
1113-60-6

3-hydroxy-2-oxopropionic acid

2-oxopropanal
78-98-8

2-oxopropanal

(3S)-1,3-dihydroxypentan-2,4-dione
147523-70-4

(3S)-1,3-dihydroxypentan-2,4-dione

Conditions
ConditionsYield
at 37℃; transketolase, thiamine pyrophosphate, MgCl2, glycylglycine buffer pH 7.6;16%
With thiamine pyrophosphate; magnesium chloride; transketolase from spinach In water glycyl-glycine buffer 0,05 M (pH 7.5);
3-hydroxy-2-oxopropionic acid
1113-60-6

3-hydroxy-2-oxopropionic acid

4-deoxy-L-threose
37428-70-9

4-deoxy-L-threose

6-deoxy-L-xylo-hexulose
18545-94-3

6-deoxy-L-xylo-hexulose

Conditions
ConditionsYield
With thiamine pyrophosphate; Tris buffer; magnesium chloride In water at 30℃; for 20h; transketolase;15%
3-hydroxy-2-oxopropionic acid
1113-60-6

3-hydroxy-2-oxopropionic acid

3-Deoxy-DL-glycero-tetrose
143106-66-5

3-Deoxy-DL-glycero-tetrose

5-deoxy-D-threo-hex-2-ulose
92574-10-2

5-deoxy-D-threo-hex-2-ulose

Conditions
ConditionsYield
With sodium hydroxide; thiamine diphosphate; Lithium hydroxypyruvate; magnesium chloride In water 3-5 d, transketolase (EC 2.2.1.1) from yeast;7%
D(+)-α-hydroxy-isocaproaldehyde

D(+)-α-hydroxy-isocaproaldehyde

3-hydroxy-2-oxopropionic acid
1113-60-6

3-hydroxy-2-oxopropionic acid

C8H16O4
1186294-80-3

C8H16O4

Conditions
ConditionsYield
With transketolase pH=7.5;5%
3-hydroxy-2-oxopropionic acid
1113-60-6

3-hydroxy-2-oxopropionic acid

copper diacetate
142-71-2

copper diacetate

A

formic acid
64-18-6

formic acid

B

methylammonium carbonate
15719-64-9, 15719-76-3, 97762-63-5

methylammonium carbonate

Conditions
ConditionsYield
at 50℃;
3-hydroxy-2-oxopropionic acid
1113-60-6

3-hydroxy-2-oxopropionic acid

potassium cyanide
151-50-8

potassium cyanide

A

D-tartaric acid
147-71-7

D-tartaric acid

B

meso-tartaric acid
147-73-9

meso-tartaric acid

Conditions
ConditionsYield
beim Kochen des Reaktionsprodukts mit verd.Schwefelsaeure;
3-hydroxy-2-oxopropionic acid
1113-60-6

3-hydroxy-2-oxopropionic acid

phenylhydrazine acetate
72358-76-0

phenylhydrazine acetate

2,3-bis-phenylhydrazono-propionic acid
75640-08-3

2,3-bis-phenylhydrazono-propionic acid

3-hydroxy-2-oxopropionic acid
1113-60-6

3-hydroxy-2-oxopropionic acid

Conditions
ConditionsYield
With benzylviologen cation radical In water at 25℃; Equilibrium constant; cell free extract of Proteus vulgaris (potassium phosphate buffer pH 7.0), Vmax;
With sodium amalgam; water
With hydrogen; 1,1'-dibenzyl-4,4'-bipyridinium In water at 35℃; under 760 Torr; biosynthesis by Proteus vulgaris (potassium phosphate buffer pH 7.0);

1113-60-6Relevant articles and documents

One-Pot Preparation of d-Amino Acids Through Biocatalytic Deracemization Using Alanine Dehydrogenase and Ω-Transaminase

Han, Sang-Woo,Shin, Jong-Shik

, p. 3678 - 3684 (2018)

d-Amino acids are pharmaceutically important building blocks, leading to a great deal of research efforts to develop cost-effective synthetic methods. Preparation of d-amino acids by deracemization has been conceptually attractive owing to facile synthesis of racemic amino acids by Strecker synthesis. Here, we demonstrated biocatalytic deracemization of aliphatic amino acids into d-enantiomers by running cascade reactions; (1) stereoinversion of l-amino acid to a d-form by amino acid dehydrogenase and ω-transaminase and (2) regeneration of NAD+ by NADH oxidase. Under the cascade reaction conditions containing 100?mM isopropylamine and 1?mM NAD+, complete deracemization of 100?mM dl-alanine was achieved after 24?h with 95% reaction yield of d-alanine (> 99% eeD, 52% isolation yield). Graphical Abstract: [Figure not available: see fulltext.].

MECHANISTIC STUDY OF THE ALDOL CONDENSATION OCCURING IN THE ALKALINE SOLUTION OF 3-HYDROXY 2-OXO PROPRANOATE (Β HYDROXYPYRUVATE)

Fleury, Daniele,Fleury, M. B.,Platzer, Nicole

, p. 493 - 502 (1981)

With 3-bromo-2-oxopropanoate (β bromopyruvate) and its ethyl ester, the ionisation of the gemdiol of the hydrated form BrCH2-C(OH)2-COOR 1 initiates the elimination of the bromide anion yielding 3-hydroxy-2-oxopropanoate 2 (β-hydroxypyruvate).The mechanism of the reaction was investigated essentially by polarography in aqueous solution.In neutral ( and acid) media, the polarographic behaviour of 2 resembled that of other α-ketoacids: reduction at the mercury electrode yielded glycerate.In alkaline media, there was evidence of the carbanion enolate .3'.The overall rate constant was determined according to a kinetic law of the type: : found k = 1.56 min-1 in NaOH 0.5N at 25 deg.In the pH range 10.5 to 11.5, 3' existed in minor amounts and initiated a slow aldol codensation with the tautomer 3-oxo-2-hydroxypropanoate 4 (tartrone semialdehyde) according to a kinetic low of the type found at 25 deg., at pH 11.0.The aldol product was isolated as a sodium salt and its structure established by 13CNMR.

One-Pot Cascade Synthesis of (3S)-Hydroxyketones Catalyzed by Transketolase via Hydroxypyruvate Generated in Situ from d-Serine by d-Amino Acid Oxidase

L'enfant, Mélanie,Bruna, Felipe,Lorillière, Marion,Ocal, Nazim,Fessner, Wolf-Dieter,Pollegioni, Loredano,Charmantray, Franck,Hecquet, Laurence

, p. 2550 - 2558 (2019)

We described an efficient in situ generation of hydroxypyruvate from d-serine catalyzed by a d-amino acid oxidase from Rhodotorula gracilis. This strategy revealed an interesting alternative to the conventional chemical synthesis of hydroxypyruvate starting from toxic bromopyruvate or to the enzymatic transamination from l-serine requiring an additional substrate as amino acceptor. Hydroxypyruvate thus produced was used as donor substrate of transketolases from Escherichia coli or from Geobacillus stearothermophilus catalyzing the stereoselective formation of a carbon?carbon bond. The enzymatic cascade reaction was performed in one-pot in the presence of d-serine and appropriate aldehydes for the synthesis of valuable (3S)-hydroxyketones, which were obtained with high enantio- and diastereoselectivity and in good yield. The efficiency of the process was based on the irreversibility of both reactions allowing complete conversion of d-serine and aldehydes. (Figure presented.).

Selective Oxidation of Glycerol to Glyceric Acid in Base-Free Aqueous Solution at Room Temperature Catalyzed by Platinum Supported on Carbon Activated with Potassium Hydroxide

Tan, Hua,Tall, Omar E.,Liu, Zhaohui,Wei, Nini,Yapici, Tahir,Zhan, Tong,Hedhill, Mohamed Nejib,Han, Yu

, p. 1699 - 1707 (2016)

Pt supported on KOH-activated mesoporous carbon (K-AMC) was used to catalyze glycerol oxidation under base-free conditions at room temperature. To study the relationship between the carbon surface chemistry and the catalytic performance of the K-AMC-based Pt catalysts, different levels of surface oxygen functional groups (SOFGs) on the AMC supports were induced by thermal treatment at different temperatures under inert or H2 gas. A strong effect of the surface chemistry was observed on AMC-supported Pt catalysts for glycerol oxidation. The presence of carboxylic acid groups impedes the adsorption of glycerol, which leads to the reduction of catalytic activity, whereas the presence of high-desorption-temperature SOFGs, such as phenol, ether, and carbonyl/quinone groups, provide hydrophilicity to the carbon surface that improves the adsorption of glycerol molecules on Pt metal surface, which is beneficial for the catalytic activity.

Mg-Al mixed oxides supported bimetallic au-pd nanoparticles with superior catalytic properties in aerobic oxidation of benzyl alcohol and glycerol

Wang, Liang,Zhang, Wei,Zeng, Shangjing,Su, Dangsheng,Meng, Xiangju,Xiao, Fengshou

, p. 2189 - 2197 (2012)

Nano-sized Au and Pd catalysts are favorable for oxidations with molecular oxygen, and the preparation of this kind of nanoparticles with high catalytic activities is strongly desirable. We report a successful synthesis of bimetallic Au-Pd nanoparticles w

Role of the active site residues arginine-216 and arginine-237 in the substrate specificity of mammalian D-aspartate oxidase

Katane, Masumi,Saitoh, Yasuaki,Maeda, Kazuhiro,Hanai, Toshihiko,Sekine, Masae,Furuchi, Takemitsu,Homma, Hiroshi

, p. 467 - 476 (2011)

d-Aspartate oxidase (DDO) and d-amino acid oxidase (DAO) are flavin adenine dinucleotide-containing flavoproteins that catalyze the oxidative deamination of d-amino acids. Unlike DAO, which acts on several neutral and basic d-amino acids, DDO is highly specific for acidic d-amino acids. Based on molecular modeling and simulated annealing docking analyses, a recombinant mouse DDO carrying two substitutions (Arg-216 to Leu and Arg-237 to Tyr) was generated (R216L-R237Y variant). This variant and two previously constructed single-point mutants of mouse DDO (R216L and R237Y variants) were characterized to investigate the role of Arg-216 and Arg-237 in the substrate specificity of mouse DDO. The R216L-R237Y and R216L variants acquired a broad specificity for several neutral and basic d-amino acids, and showed a considerable decrease in activity against acidic d-amino acids. The R237Y variant, however, did not show any additional specificity for neutral or basic d-amino acids and its activity against acidic d-amino acids was greatly reduced. The kinetic properties of these variants indicated that the Arg-216 residue is important for the catalytic activity and substrate specificity of mouse DDO. However, Arg-237 is, apparently, only marginally involved in substrate recognition, but is important for catalytic activity. Notably, the substrate specificity of the R216L-R237Y variant differed significantly from that of the R216L variant, suggesting that Arg-237 has subsidiary effects on substrate specificity. Additional experiments using several DDO and DAO inhibitors also suggested the involvement of Arg-216 in the substrate specificity and catalytic activity of mouse DDO and that Arg-237 is possibly involved in substrate recognition by this enzyme. Collectively, these results indicate that Arg-216 and Arg-237 play crucial and subsidiary role(s), respectively, in the substrate specificity of mouse DDO.

The role of residues Arg169 and Arg220 in intersubunit interactions of yeast D-Amino acid oxidase

Cherskova,Khoronenkova,Tishkov

, p. 269 - 275 (2010)

D-Amino acid oxidase from the yeast Trigonopsis variabilis (EC 1.4.3.3, TvDAAO) exists as a dimer consisting of two identical subunits. The dimeric structure of the enzyme is stabilized by 12 (six pairs) hydrogen bonds, the residues Arg169 and Arg220 of each subunit being involved in eight hydrogen bonds. The Arg169Glu and Arg(169,220)Ala mutants of TvDAAO were prepared. Both mutant enzymes were expressed in E. coli cells as insoluble but catalytically active inclusion bodies. The introduction of amino acid substitutions at the intersubunit interface resulted in a change in the substrate specificity profile and a strong decrease in thermal stability.

Electrooxidation of glycerol on nickel and nickel alloy (Ni-Cu and Ni-Co) nanoparticles in alkaline media

Habibi, Biuck,Delnavaz, Nasrin

, p. 31797 - 31806 (2016)

In the present study, nickel (Ni) and Ni alloy (Ni-Cu and Ni-Co) nanoparticles modified carbon-ceramic electrodes (Ni/CCE, Ni-Cu/CCE and Ni-Co/CCE) were prepared by an electrochemical process for the oxidation of glycerol. In order to obtain the surface and physicochemical information, the Ni/CCE, Ni-Cu/CCE and Ni-Co/CCE were investigated by scanning electron microscopy, energy dispersive X-ray spectroscopy, X-ray diffraction and electrochemical techniques. Then, cyclic voltammetry and chronoamperometry were employed to characterize the electrocatalytic activity of the modified electrodes, Ni/CCE, Ni-Cu/CCE and Ni-Co/CCE, toward the oxidation of glycerol in 1.0 M NaOH solution. It was found that the Ni alloy nanoparticle modified electrodes are catalytically more active than the Ni/CCE, therefore, the alloying of the Ni with Cu and Co in the form of nanoparticles on the carbon-ceramic electrode, as a homemade substrate, greatly enhances the catalytic activity of the Ni-based electrocatalysts (as the non-platinum electrocatalysts) in glycerol oxidation.

SiO2-, Cu-, and Ni-supported Au nanoparticles for selective glycerol oxidation in the liquid phase

Kapkowski, Maciej,Bartczak, Piotr,Korzec, Mateusz,Sitko, Rafal,Szade, Jacek,Balin, Katarzyna,Lel?tko, Józef,Polanski, Jaroslaw

, p. 110 - 118 (2014)

We tested for the first time the efficiency of SiO2-, Cu-, and Ni-supported Au in deep glycerol oxidation in a diluted and viscous H2O2/H2O liquid phase. Acetic acid (AA), the C2 oxidate, was preferentially formed in such a system. High conversion (100%) and AA yields (90%) were observed for the sol-gel SiO2-supported Au in diluted solutions. Although with the increase of glycerol concentration in the viscous liquid phase these values decreased to ca. 40% (conversion) and 20% (AA yield), the addition of acetonitrile improved the AA yield to ca. 40%, while the surfactants were found to be capable of a many-fold enhancement of the catalyst activity at the room temperature highly viscous liquid phase. High performances were also observed for the bimetallic Au/Cu and Au/Ni catalysts obtained by nano-Au transfer; however, these catalysts were destroyed during the reaction by the Cu or Ni leaching effect.

Highly selective transformation of glycerol to dihydroxyacetone without using oxidants by a PtSb/C-catalyzed electrooxidation process

Lee, Seonhwa,Kim, Hyung Ju,Lim, Eun Ja,Kim, Youngmin,Noh, Yuseong,Huber, George W.,Kim, Won Bae

, p. 2877 - 2887 (2016)

We demonstrate an electrocatalytic reactor system for the partial oxidation of glycerol in an acidic solution to produce value-added chemicals, such as dihydroxyacetone (DHA), glyceraldehyde (GAD), glyceric acid (GLA), and glycolic acid (GCA). Under optimized conditions, the carbon-supported bimetallic PtSb (PtSb/C) catalyst was identified as a highly active catalyst for the selective oxidation of glycerol in the electrocatalytic reactor. The product selectivity can be strongly controlled as a function of the applied electrode potential and the catalyst surface composition. The main product from the electrocatalytic oxidation of glycerol was DHA, with a yield of 61.4% of DHA at a glycerol conversion of 90.3%, which can be achieved even without using any oxidants over the PtSb/C catalyst at 0.797 V (vs. SHE, standard hydrogen electrode). The electrocatalytic oxidation of biomass-derived glycerol represents a promising method of chemical transformation to produce value-added molecules.

Enzymatic synthesis of 'natural-labeled' 6-deoxy-L-sorbose precursor of an important food flavor

Hecquet,Bolte,Demuynck

, p. 8223 - 8232 (1996)

A biological route to natural 6-deoxy-L-sorbose is described. This method is based on the production of natural hydroxypyruvate and 4-deoxy-L-threose and their conversion into 6-deoxy-L-sorbose: hydroxypyruvate is obtained from L-serine by serine: glyoxylate aminotransferase catalysis, 4-deoxy-L-threose is obtained by microbial isomerization of 4-deoxy-L-erythrulose, this last being obtained from acetaldehyde (a naturally-available compound) and hydroxypyruvate by transketolase catalysis.

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