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B6db activities: 4.1.3.41

4.1.3.41
Description 3-hydroxy-D-aspartate aldolase
Alternative names D-3-hydroxyaspartate aldolase;
3-hydroxy-D-aspartate glyoxylate-lyase (glycine-forming);
bhcC (gene name);
Catalyzed reaction threo-3-hydroxy-D-aspartate = glycine + glyoxylate
D-erythro-3-hydroxyaspartate = glycine + glyoxylate
Cofactor Pyridoxal-phosphate and Mn(II).
Comments A pyridoxal-phosphate protein. The enzyme, purified from the bacterium Paracoccus denitrificans IFO 13301, is strictly D-specific as to the α-position of the substrate, but accepts both the threo and erythro forms at the β-position. The erythro form is a far better substrate (about 100 fold). The enzyme can also accept D-allothreonine, D-threonine, erythro-3-phenyl-D-serine and threo-3-phenyl-D-serine.

Different from EC 4.1.3.14, erythro-3-hydroxy-L-aspartate aldolase.

Requires a divalent cation, such as Mg2+, Mn2+ or Co2+.

Organisms -Eubacteria
 

Family 

4.1.3.41 (18)
 
Links Enzyme (activities) 4.1.3.41
BRENDA (activities) 4.1.3.41
KEGG (pathways) 4.1.3.41
PLPMDB (PLP mutants) 4.1.3.41
 
References
 Schada von Borzyskowski L, Severi F, Krüger K, Hermann L, Gilardet A, Sippel F, Pommerenke B, Claus P, Cortina NS, Glatter T, Zauner S, Zarzycki J, Fuchs BM, Bremer E, Maier UG, Amann RI, Erb TJ (2019) Marine Proteobacteria metabolize glycolate via the β-hydroxyaspartate cycle Nature 575 500-504.

 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.

Articles on 4.1.3.41
 
last changed 2019/11/19 11:19

B6db activities