99297-20-8

Basic information

• Product Name: β-(3-amino-1,2,4-triazol-1-yl)-L-alanine
• CAS NO: 99297-20-8
• Molecular Weight: 171.159
• Mol File: 99297-20-8.mol
• Article Data: 4

Chemical Properties

• CAS DataBase Reference: β-(3-amino-1,2,4-triazol-1-yl)-L-alanine(CAS DataBase Reference)
• NIST Chemistry Reference: β-(3-amino-1,2,4-triazol-1-yl)-L-alanine(99297-20-8)
• EPA Substance Registry System: β-(3-amino-1,2,4-triazol-1-yl)-L-alanine(99297-20-8)

Safety Data

• Hazardous Substances Data: 99297-20-8(Hazardous Substances Data)

Upstream product

• 61-82-5 3⁽⁵⁾-amino-1,2,4-triazole 
• 5147-00-2 O-acetyl-L-serine 
• 52-90-4 L-Cysteine 
• 61-82-5 4H-1,2,4-triazol-3-amine 

Relevant articles and documents

ENZYMATIC SYNTHESIS OF THE NEUROEXCITATORY AMINO ACID QUISQUALIC ACID BY CYSTEINE SYNTHASE

Key Word Index - Quisqualis indica var. villosa; Combretaceae; cysteine synthase; isoenzyme; enzyme purification; biosynthesis; heterocyclic β-substituted alanines; quisqualic acid; O-acetyl-L-serine; cysteine.Purification of cysteine synthase from the leaves of Quisqualis indica var. villosa reveals the presence of two forms of this enzyme, separated by chromatography on DEAE-Sephadex A-50.Isoenzyme A was purified 10 000-fold and had a specific activity of 10.8 U/mg protein.Isoenzyme B was purified 460-fold with a specific activity of 0.49 U/mg protein.Both isoenzymes have the same Mrs (58 000) and dissociate into identical subunits (Mr 29 000).The Km value of isoenzyme A is 1.9 mM for O-acetyl-L-serine and 59 μM for sulphide, while that of isoenzyme B is 7.1 mM for O-acetyl-L-serine and 4.0 mM for 3,5-dioxo-1,2,4-oxadiazolidine.Both isoenzymes catalyse the formation of cysteine from O-acetyl-L-serine and hydrogen sulphide, but only isoenzyme B catalyses the formation of L-quisqualic acid.Other significant differences occur in the substrate specificity of the two isoenzymes.Some properties of the purified cysteine synthase isoenzymes are also described.

PURIFICATION AND PROPERTIES OF β-CYANO-L-ALANINE SYNTHASE FROM SPINACIA OLERACEA

β-Cyano-L-alanine synthase was purified ca 6200-fold to homogeneity from the leaves of spinach (Spinacia oleracea).The purified enzyme has an apparent Mr of 60 000 and can be dissociated into identical subunits of Mr 30 000.The subunits each contain one molecule of pyridoxal 5'-phosphate.The Km value is 2.3 mM for L-cysteine and 0.73 mM for cyanide. β-Cyano-L-alanine synthase from S. oleracea also catalyses the formation of some S-substituted L-cysteines and some heterocyclic β-substituted alanines from L-cysteine or O-acetyl-L-serine.The specificity of these additional catalytic activities of the purified enzyme are compared with those of cysteine synthase purified from the same plant, and with those of β-cyano-L-alanine synthase purified from other sources.Some other properties, including the amino acid composition of the purified enzyme, are also described. - Key Word Index: Spinacia oleracea; Chenopodiaceae; spinach; β-cyano-L-alanine synthase; cysteine synthase; enzyme purification; amino acid composition; L-cysteine; O-acetyl-L-serine; β-cyano-L-alanine; heterocyclic β-substituted alanines.