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13477-53-7

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13477-53-7 Usage

Uses

2-Hydroxy-4-amino Butanoic Acid is a GABA analog.

Check Digit Verification of cas no

The CAS Registry Mumber 13477-53-7 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 1,3,4,7 and 7 respectively; the second part has 2 digits, 5 and 3 respectively.
Calculate Digit Verification of CAS Registry Number 13477-53:
(7*1)+(6*3)+(5*4)+(4*7)+(3*7)+(2*5)+(1*3)=107
107 % 10 = 7
So 13477-53-7 is a valid CAS Registry Number.
InChI:InChI=1/C4H9NO3/c5-2-1-3(6)4(7)8/h3,6H,1-2,5H2,(H,7,8)/t3-/m1/s1

13477-53-7SDS

SAFETY DATA SHEETS

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

Version: 1.0

Creation Date: Aug 18, 2017

Revision Date: Aug 18, 2017

1.Identification

1.1 GHS Product identifier

Product name 4-Amino-2-hydroxybutanoic acid

1.2 Other means of identification

Product number -
Other names 4-Amino-2-hydroxybutyric 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:13477-53-7 SDS

13477-53-7Relevant articles and documents

Synthesis of DL 4 amino 2 hydroxybutyric acid

Yamada,Okada

, p. 1437 - 1438 (1976)

-

Enantioselective Syntheses of (S)- and (R)-3-Hydroxypyrrolidin-2-ones via Lactate Dehydrogenase Catalysed Reductions of 4-Benzyloxycarbonylamino-2-oxobutanoic Acid

Bentley, Jonathan M.,Wadsworth, Harry J.,Willis, Christine L.

, p. 231 - 232 (1995)

The first examples of the BS- and SE-lactate dehydrogenase catalysed reductions of an α-keto acid incorporating a nitrogen containing function in the side chain are described: (S)- and (R)-benzyloxycarbonylamino-2-hydroxybutanoic acids were prepared in good yield and excellent enantioselectivities and were converted to the (S)- and (R)-3-hydroxypyrrolidin-2-ones respectively.

-

Woo,P.W.K. et al.

, p. 2617 - 2620 (1971)

-

Sato et al.

, p. 2815 (1976)

Structural and functional characterization of plant aminoaldehyde dehydrogenase from pisum sativum with a broad specificity for natural and synthetic aminoaldehydes

Tylichova, Martina,Kopecny, David,Morera, Solange,Briozzo, Pierre,Lenobel, Rene,Snegaroff, Jacques,Sebela, Marek

experimental part, p. 870 - 882 (2011/04/24)

Aminoaldehyde dehydrogenases (AMADHs, EC 1.2.1.19) belong to the large aldehyde dehydrogenase (ALDH) superfamily, namely, the ALDH9 family. They oxidize polyamine-derived ω-aminoaldehydes to the corresponding ω-amino acids. Here, we report the first X-ray structures of plant AMADHs: two isoenzymes, PsAMADH1 and PsAMADH2, from Pisum sativum in complex with β-nicotinamide adenine dinucleotide (NAD+) at 2.4 and 2.15 A resolution, respectively. Both recombinant proteins are dimeric and, similarly to other ALDHs, each monomer is composed of an oligomerization domain, a coenzyme binding domain and a catalytic domain. Each subunit binds NAD+ as a coenzyme, contains a solvent-accessible C-terminal peroxisomal targeting signal (type 1) and a cation bound in the cavity close to the NAD+ binding site. While the NAD+ binding mode is classical for PsAMADH2, that for PsAMADH1 is unusual among ALDHs. A glycerol molecule occupies the substrate binding site and mimics a bound substrate. Structural analysis and substrate specificity study of both isoenzymes in combination with data published previously on other ALDH9 family members show that the established categorization of such enzymes into distinct groups based on substrate specificity is no more appropriate, because many of them seem capable of oxidizing a large spectrum of aminoaldehyde substrates. PsAMADH1 and PsAMADH2 can oxidize N,N,N-trimethyl-4-aminobutyraldehyde into γ-butyrobetaine, which is the carnitine precursor in animal cells. This activity highly suggests that in addition to their contribution to the formation of compatible osmolytes such as glycine betaine, β-alanine betaine and γ-aminobutyric acid, AMADHs might participate in carnitine biosynthesis in plants.

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