KEGG   ENZYME: 4.1.2.48Help
Entry
EC 4.1.2.48                 Enzyme                                 

Name
low-specificity L-threonine aldolase;
LtaE
Class
Lyases;
Carbon-carbon lyases;
Aldehyde-lyases
BRITE hierarchy
Sysname
L-threonine/L-allo-threonine acetaldehyde-lyase (glycine-forming)
Reaction(IUBMB)
(1) L-threonine = glycine + acetaldehyde;
(2) L-allo-threonine = glycine + acetaldehyde
Substrate
L-threonine [CPD:C00188];
L-allo-threonine [CPD:C05519]
Product
glycine [CPD:C00037];
acetaldehyde [CPD:C00084]
Comment
Requires pyridoxal phosphate. The low-specificity L-threonine aldolase can act on both L-threonine and L-allo-threonine [1,2]. The enzyme from Escherichia coli can also act on L-threo-phenylserine and L-erythro-phenylserine [4]. The enzyme can also catalyse the aldol condensation of glycolaldehyde and glycine to form 4-hydroxy-L-threonine, an intermediate of pyridoxal phosphate biosynthesis [3]. Different from EC 4.1.2.5, L-threonine aldolase, and EC 4.1.2.49, L-allo-threonine aldolase.
History
EC 4.1.2.48 created 2011
Reference
1  [PMID:5438301]
  Authors
Yamada H, Kumagai H, Nagate T, Yoshida H
  Title
Crystalline threonine aldolase from Candida humicola.
  Journal
Biochem. Biophys. Res. Commun. 39 (1970) 53-8.
Reference
2  [PMID:5017702]
  Authors
Kumagai H, Nagate T, Yoshida H, Yamada H.
  Title
Threonine aldolase from Candida humicola. II. Purification, crystallization and properties.
  Journal
Biochim. Biophys. Acta. 258 (1972) 779-90.
Reference
3  [PMID:9151955]
  Authors
Liu JQ, Nagata S, Dairi T, Misono H, Shimizu S, Yamada H
  Title
The GLY1 gene of Saccharomyces cerevisiae encodes a low-specific L-threonine aldolase that catalyzes cleavage of L-allo-threonine and L-threonine to glycine--expression of the gene in Escherichia coli and purification and characterization of the enzyme.
  Journal
Eur. J. Biochem. 245 (1997) 289-93.
  Sequence
[sce:YEL046C]
Reference
4  [PMID:9692922]
  Authors
Liu JQ, Dairi T, Itoh N, Kataoka M, Shimizu S, Yamada H
  Title
Gene cloning, biochemical characterization and physiological role of a thermostable low-specificity L-threonine aldolase from Escherichia coli.
  Journal
Eur. J. Biochem. 255 (1998) 220-6.
  Sequence
[eco:b0870]
Reference
5  [PMID:21119630]
  Authors
Kim J, Kershner JP, Novikov Y, Shoemaker RK, Copley SD
  Title
Three serendipitous pathways in E. coli can bypass a block in pyridoxal-5'-phosphate synthesis.
  Journal
Mol. Syst. Biol. 6 (2010) 436.
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 

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