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B6db families: 4.1.2.42

4.1.2.42
Activity 4.1.2.42
Description D-threonine aldolase, low specificity
Notes Rather diverse family of enzymes, most strictly related to 3-hydroxy-D-aspartate aldolases (family 4.1.3.41), which catalyze a similar reaction.
PDB 4V15;
PLP Fold Type III
PLP-dependent Domain
Domain alignment
Domain hmm
Fold type III

Reference sequence BAA86032
Domain interval 17-320
Catalytic site 59 K
 
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
last changed 2018/01/08 10:47

B6db families