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4.1.2.42 |
Description |
D-threonine aldolase, low specificity |
Alternative names |
D-TA; DTA; low specificity D-TA; low specificity D-threonine aldolase.
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Catalyzed reaction |
(1) D-threonine = glycine + acetaldehyde
(2) D-allothreonine = glycine + acetaldehyde |
Cofactor |
Pyridoxal-phosphate and Mn(II) |
Comments |
A pyridoxal-phosphate protein that is activated by divalent metal cations (e.g. Co2+, Ni2+, Mn2+ or Mg2+). The reaction is reversible, which can lead to the interconversion of D-threonine and D-allothreonine. Several other D-β-hydroxy-α-amino acids, such as D-β-phenylserine, D-β-hydroxy-α-aminovaleric acid and D-β-3,4-dihydroxyphenylserine, can also act as substrate. |
PDB |
4V15; |
Organisms |
-Eubacteria |
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Family |
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Links |
Enzyme (activities) 4.1.2.42
BRENDA (activities) 4.1.2.42
KEGG (pathways) 4.1.2.42
PLPMDB (PLP mutants) 4.1.2.42
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References |
Hirato, Y; Tokuhisa, M; Tanigawa, M; Ashida, H; Tanaka, H; Nishimura, K. (2017) Cloning and characterization of d-threonine aldolase from the green alga Chlamydomonas reinhardtii Phytochemistry 135 18-23. Qijia, C.; Xi, C.; Yunfeng, C.: Jie, R.; Wei, L.; Jinhui, F.; Qiaqing, W.; Dunming, Z. (2017) A new D-threonine aldolase as a promising biocatalyst for highly stereoselective preparation of chiral aromatic β-hydroxy-α-amino acids Catal. Sci. Technol. 7 5964-5973. Uhl MK, Oberdorfer G, Steinkellner G, Riegler-Berket L, Mink D, van Assema F, Schürmann M, Gruber K (2015) The crystal structure of D-threonine aldolase from Alcaligenes xylosoxidans provides insight into a metal ion assisted PLP-dependent mechanism PLoS One 10 e0124056. Liu, J. Q.; Odani, M.; Yasuoka, T.; Dairi, T.; Itoh, N.; Kataoka, M.; Shimizu, S.; 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. Liu, J. Q.; Dairi, T.; Itoh, N.; Kataoka, M.; Shimizu, S.; 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 16678-85. Articles on 4.1.2.42 |
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last changed |
2017/08/04 12:36 |
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