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bhcb |
Description |
Erythro-3-hydroxy-D-aspartate ammonia-lyase (4.3.1.-) |
Alternative names |
erythro-β-Hydroxy-D-aspartic acid dehydratase; erythro-β-Hydroxy-D-aspartate ammonia-lyase (oxaloacetate-forming);
(2R, 3S)-β-hydroxyaspartate dehydratase;
bhcB (gene name);
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Catalyzed reaction |
erythro-3-hydroxy-D-aspartate = oxaloacetate + NH3 |
Cofactor |
Pyridoxal-phosphate and probably Mg2+. |
Comments |
The enzyme activity was assayed in the presence of 1 mM Mg2+ |
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The same reaction is catalyzed (inefficiently) by Threo-3-hydroxy-D-aspartate ammonia-lyases (4.3.1.27), which are Fold-type III enzymes, whereas the functionally validated bhcB belongs to the Fold-Type II group. |
Organisms |
-Eubacteria |
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Family |
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Links |
Enzyme (activities) bhcb
BRENDA (activities) bhcb
KEGG (pathways) bhcb
PLPMDB (PLP mutants) bhcb
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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. Nagano, H.; Shibano, K.; Matsumoto, Y.; Yokota, A.; Wada, M.
(2017) Isolation and amino acid sequence of a dehydratase acting on d-erythro-3-hydroxyaspartate from Pseudomonas sp. N99, and its application in the production of optically active 3-hydroxyaspartate Biosci Biotechnol Biochem 81 1156-1164. Articles on bhcb |
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last changed |
2019/11/20 09:32 |
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