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bhcb |
Activity |
bhcb |
Description |
Erythro-3-hydroxy-D-aspartate ammonia-lyase (4.3.1.-) |
Notes |
Bacterial sequences, very similar to eukaryotic serine racemases (family 5.1.1.18) and to bacterial Threo-3-hydroxy-L-aspartate ammonia-lyases (family 4.3.1.16).
At least one enzyme in family 4.3.1.16 (from Pseudomonas sp. 99) also appears to catalyze quite efficiently the bhcB reaction. |
PLP Fold Type |
II |
PLP-dependent Domain |
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Number of sequences |
11 |
Sequences in seed alignment |
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Reference sequence |
WP_041530430 |
Domain interval |
20-308 |
Catalytic site |
57 K |
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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 |
last changed |
2019/11/20 17:34 |
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