Biology:3-Oxo-5,6-dehydrosuberyl-CoA semialdehyde dehydrogenase
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Short description: Enzyme
3-oxo-5,6-dehydrosuberyl-CoA semialdehyde dehydrogenase | |||||||||
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Identifiers | |||||||||
EC number | 1.17.1.7 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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3-oxo-5,6-dehydrosuberyl-CoA semialdehyde dehydrogenase (EC 1.17.1.7, paaZ (gene)) is an enzyme with systematic name 3-oxo-5,6-dehydrosuberyl-CoA semialdehyde:NADP+ oxidoreductase.[1][2][3] This enzyme catalyses the following chemical reaction
- 3-oxo-5,6-dehydrosuberyl-CoA semialdehyde + NADP+ + H2O [math]\displaystyle{ \rightleftharpoons }[/math] 3-oxo-5,6-dehydrosuberyl-CoA + NADPH + H+
The enzyme from Escherichia coli is a bifunctional protein that also acts as EC 3.7.1.16, oxepin-CoA hydrolase.
References
- ↑ "Catabolism of phenylacetic acid in Escherichia coli. Characterization of a new aerobic hybrid pathway". The Journal of Biological Chemistry 273 (40): 25974–86. October 1998. doi:10.1074/jbc.273.40.25974. PMID 9748275.
- ↑ "Functional genomics by NMR spectroscopy. Phenylacetate catabolism in Escherichia coli". European Journal of Biochemistry 270 (14): 3047–54. July 2003. doi:10.1046/j.1432-1033.2003.03683.x. PMID 12846838.
- ↑ "Bacterial phenylalanine and phenylacetate catabolic pathway revealed". Proceedings of the National Academy of Sciences of the United States of America 107 (32): 14390–5. August 2010. doi:10.1073/pnas.1005399107. PMID 20660314. Bibcode: 2010PNAS..10714390T.
External links
- 3-oxo-5,6-dehydrosuberyl-CoA+semialdehyde+dehydrogenase at the US National Library of Medicine Medical Subject Headings (MeSH)
Original source: https://en.wikipedia.org/wiki/3-Oxo-5,6-dehydrosuberyl-CoA semialdehyde dehydrogenase.
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