D-threonine aldolase

D-threonine aldolase (EC 4.1.2.42, D-TA, DTA, low specificity D-TA, low specificity D-threonine aldolase) is an enzyme with systematic name D-threonine acetaldehyde-lyase (glycine-forming).^[1]^[2]^[3]^[4]^[5]^[6] This enzyme catalyses the following chemical reaction

(1) D-threonine

\rightleftharpoons

glycine + acetaldehyde

(2) D-allothreonine

\rightleftharpoons

glycine + acetaldehyde

This pyridoxal-phosphate protein is activated by divalent metal cations (e.g. Co²⁺, Ni²⁺, Mn²⁺ or Mg²⁺).

References

↑ Kataoka, M., Ikemi, M., Morikawa, T., Miyoshi, T., Nishi, K., Wada, M., Yamada, H. and Shimizu, S. (1997). "Isolation and characterization of D-threonine aldolase, a pyridoxal-5′-phosphate-dependent enzyme from Arthrobacter sp. DK-38". Eur. J. Biochem. 248: 385–393. doi:10.1111/j.1432-1033.1997.00385.x. PMID 9346293.
↑ Liu, J.Q., Dairi, T., Itoh, N., Kataoka, M., Shimizu, S. and Yamada, H. (1998). "A novel metal-activated pyridoxal enzyme with a unique primary structure, low specificity D-threonine aldolase from Arthrobacter sp. Strain DK-38. Molecular cloning and cofactor characterization". J. Biol. Chem. 273: 16678–16685. doi:10.1074/jbc.273.27.16678. PMID 9642221.
↑ Liu, J.Q., Odani, M., Dairi, T., Itoh, N., Shimizu, S. and Yamada, H. (1999). "A new route to L-threo-3-[4-(methylthio)phenylserine], a key intermediate for the synthesis of antibiotics: recombinant low-specificity D-threonine aldolase-catalyzed stereospecific resolution". Appl. Microbiol. Biotechnol. 51: 586–591. doi:10.1007/s002530051436. PMID 10390816.
↑ Liu, J.Q., Odani, M., Yasuoka, T., Dairi, T., Itoh, N., Kataoka, M., Shimizu, S. and Yamada, H. (2000). "Gene cloning and overproduction of low-specificity D-threonine aldolase from Alcaligenes xylosoxidans and its application for production of a key intermediate for parkinsonism drug". Appl. Microbiol. Biotechnol. 54: 44–51. doi:10.1007/s002539900301. PMID 10952004.
↑ Liu, J.Q., Dairi, T., Itoh, N., Kataoka, M., Shimizu, S. and Yamada, H. (2000). "Diversity of microbial threonine aldolases and their application". J. Mol. Catal. B 10: 107–115. doi:10.1016/s1381-1177(00)00118-1.
↑ Paiardini, A., Contestabile, R., D'Aguanno, S., Pascarella, S. and Bossa, F. (2003). "Threonine aldolase and alanine racemase: novel examples of convergent evolution in the superfamily of vitamin B₆-dependent enzymes". Biochim. Biophys. Acta 1647: 214–219. doi:10.1016/s1570-9639(03)00050-5. PMID 12686135.

External links

D-threonine aldolase at the US National Library of Medicine Medical Subject Headings (MeSH)

Carbon-carbon lyases (EC 4.1)

4.1.1: Carboxy-lyases	Acetoacetate decarboxylase Adenosylmethionine decarboxylase Aromatic L-amino acid decarboxylase Glutamate decarboxylase Histidine decarboxylase Lysine decarboxylase Malonyl-CoA decarboxylase Ornithine decarboxylase Oxaloacetate decarboxylase Phosphoenolpyruvate carboxykinase Phosphoenolpyruvate carboxylase Phosphoribosylaminoimidazole carboxylase Pyrophosphomevalonate decarboxylase Pyruvate decarboxylase RuBisCO Uridine monophosphate synthetase/Orotidine 5'-phosphate decarboxylase Uroporphyrinogen III decarboxylase

4.1.2: Aldehyde-lyases	Fructose-bisphosphate aldolase Aldolase A Aldolase B Aldolase C 2-hydroxyphytanoyl-CoA lyase Threonine aldolase

4.1.3: Oxo-acid-lyases	Isocitrate lyase 3-hydroxy-3-methylglutaryl-CoA lyase

4.1.99: Other	Tryptophanase

Enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases(list) EC2 Transferases(list) EC3 Hydrolases(list) EC4 Lyases(list) EC5 Isomerases(list) EC6 Ligases(list)

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