Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
twitter

Escherichia coli K-12 substr. MG1655 Reaction: 4.1.2.48/4.1.2.49

Superclasses: Reactions Classified By Conversion Type Simple Reactions Chemical Reactions
Reactions Classified By Substrate Small-Molecule Reactions

EC Number: 4.1.2.48 , 4.1.2.49

Enzymes and Genes:
low-specificity L-threonine aldolase Inferred from experiment : ltaE
serine hydroxymethyltransferase : glyA

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

Mass balance status: Balanced.

Direct generic reaction:
DL-allothreonine ↔ acetaldehyde + glycine (4.1.2.-)

Enzyme Commission Primary Name for 4.1.2.48: low-specificity L-threonine aldolase

Enzyme Commission Synonyms for 4.1.2.48: LtaE

Enzyme Commission Primary Name for 4.1.2.49: L-allo-threonine aldolase

Enzyme Commission Summary for 4.1.2.48:
Requires pyridoxal phosphate. The low-specificity L-threonine aldolase can act on both L-threonine and L-allo-threonine [Yamada70, Kumagai72]. The enzyme from Escherichia coli can also act on L-threo-phenylserine and L-erythro-phenylserine [Liu98a]. The enzyme can also catalyse the aldol condensation of glycolaldehyde and glycine to form 4-hydroxy-L-threonine, an intermediate of pyridoxal phosphate biosynthesis [Liu97]. Different from EC 4.1.2.5, L-threonine aldolase, and EC 4.1.2.49, L-allo-threonine aldolase.

Enzyme Commission Summary for 4.1.2.49:
Requires pyridoxal phosphate. This enzyme, characterized from the bacterium Aeromonas jandaei, is specific for L-allo-threonine and can not act on either L-threonine or L-serine. Different from EC 4.1.2.5, L-threonine aldolase, and EC 4.1.2.48, low-specificity L-threonine aldolase. A previously listed enzyme with this name, EC 4.1.2.6, was deleted in 1971 after it was found to be identical to EC 2.1.2.1, glycine hydroxymethyltransferase.

Citations: [Kim10a, Kataoka97]

Gene-Reaction Schematic: ?

Instance reaction of [DL-allothreonine ↔ acetaldehyde + glycine] (4.1.2.-):
i1: L-allo-threonine ↔ glycine + acetaldehyde (4.1.2.48/4.1.2.49)

Relationship Links: BRENDA:EC:4.1.2.48 , BRENDA:EC:4.1.2.49 , ENZYME:EC:4.1.2.48 , ENZYME:EC:4.1.2.49 , IUBMB-ExplorEnz:EC:4.1.2.48 , IUBMB-ExplorEnz:EC:4.1.2.49


References

Kataoka97: Kataoka M, Wada M, Nishi K, Yamada H, Shimizu S (1997). "Purification and characterization of L-allo-threonine aldolase from Aeromonas jandaei DK-39." FEMS Microbiol Lett 151(2);245-8. PMID: 9228760

Kim10a: Kim J, Kershner JP, Novikov Y, Shoemaker RK, Copley SD (2010). "Three serendipitous pathways in E. coli can bypass a block in pyridoxal-5'-phosphate synthesis." Mol Syst Biol 6;436. PMID: 21119630

Kumagai72: Kumagai H, Nagate T, Yoshida H, Yamada H (1972). "Threonine aldolase from Candida humicola. II. Purification, crystallization and properties." Biochim Biophys Acta 258(3);779-90. PMID: 5017702

Liu97: Liu JQ, Nagata S, Dairi T, Misono H, Shimizu S, Yamada H (1997). "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." Eur J Biochem 245(2);289-93. PMID: 9151955

Liu98a: Liu JQ, Dairi T, Itoh N, Kataoka M, Shimizu S, Yamada H (1998). "Gene cloning, biochemical characterization and physiological role of a thermostable low-specificity L-threonine aldolase from Escherichia coli." Eur J Biochem 1998;255(1);220-6. PMID: 9692922

Yamada70: Yamada H, Kumagai H, Nagate T, Yoshida H (1970). "Crystalline threonine aldolase from Candida humicola." Biochem Biophys Res Commun 39(1);53-8. PMID: 5438301


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
Page generated by SRI International Pathway Tools version 18.5 on Sat Nov 22, 2014, BIOCYC14B.