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PROSITE documentation PDOC000653-hydroxyacyl-CoA dehydrogenase signature
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PURL: https://purl.expasy.org/prosite/documentation/PDOC00065
3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35) (HCDH) [1] is an enzyme involved in fatty acid metabolism, it catalyzes the reduction of 3-hydroxyacyl-CoA to 3-oxoacyl-CoA. Most eukaryotic cells have 2 fatty-acid β-oxidation systems, one located in mitochondria and the other in peroxisomes. In peroxisomes 3-hydroxyacyl-CoA dehydrogenase forms, with enoyl-CoA hydratase (ECH) and 3,2-trans-enoyl-CoA isomerase (ECI) a multifunctional enzyme where the N-terminal domain bears the hydratase/isomerase activities and the C-terminal domain the dehydrogenase activity. There are two mitochondrial enzymes: one which is monofunctional and the other which is, like its peroxisomal counterpart, multifunctional.
In Escherichia coli (gene fadB) and Pseudomonas fragi (gene faoA) HCDH is part of a multifunctional enzyme which also contains an ECH/ECI domain as well as a 3-hydroxybutyryl-CoA epimerase domain [2].
The other proteins structurally related to HCDH are:
- Bacterial 3-hydroxybutyryl-CoA dehydrogenase (EC 1.1.1.157) which reduces 3-hydroxybutanoyl-CoA to acetoacetyl-CoA [3].
- Eye lens protein lambda-crystallin [4], which is specific to lagomorphes (such as rabbit).
There are two major region of similarities in the sequences of proteins of the HCDH family, the first one located in the N-terminal, corresponds to the NAD-binding site, the second one is located in the center of the sequence. We have chosen to derive a signature pattern from this central region.
Last update:December 2004 / Pattern and text revised.
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PROSITE method (with tools and information) covered by this documentation:
| 1 | Authors | Birktoff J.J. Holden H.M. Hamlin R. Xuong N.-H. Banaszak L.J. |
| Source | Proc. Natl. Acad. Sci. U.S.A. 84:8262-8266(1987). |
| 2 | Authors | Nakahigashi K. Inokuchi H. |
| Title | Nucleotide sequence of the fadA and fadB genes from Escherichia coli. | |
| Source | Nucleic Acids Res. 18:4937-4937(1990). | |
| PubMed ID | 2204034 |
| 3 | Authors | Mullany P. Clayton C.L. Pallen M.J. Slone R. al-Saleh A. Tabaqchali S. |
| Title | Genes encoding homologues of three consecutive enzymes in the butyrate/butanol-producing pathway of Clostridium acetobutylicum are clustered on the Clostridium difficile chromosome. | |
| Source | FEMS Microbiol. Lett. 124:61-67(1994). | |
| PubMed ID | 8001771 |
| 4 | Authors | Mulders J.W.M. Hendriks W. Blankesteijn W.M. Bloemendal H. de Jong W.W. |
| Title | Lambda-crystallin, a major rabbit lens protein, is related to hydroxyacyl-coenzyme A dehydrogenases. | |
| Source | J. Biol. Chem. 263:15462-15466(1988). | |
| PubMed ID | 3170592 |
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