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B6db activities: 4.1.2.42

4.1.2.42
Description D-threonine aldolase, low specificity
Alternative names D-TA;
DTA;
low specificity D-TA;
low specificity D-threonine aldolase.
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.

Organisms -Eubacteria
 

Family 

4.1.2.42 (7)
 
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
 
References
 Liu, J. Q.; Dairi, T.; Itoh, N.; Kataoka, M.; Shimizu, S. (2003) A novel enzyme, D-3-hydroxyaspartate aldolase from Paracoccus denitrificans IFO 13301: purification, characterization, and gene cloning Appl Microbiol Biotechnol 62 53-60.

 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 2010/06/07 18:06

B6db activities