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- *********************************************
- * 3-hydroxyacyl-CoA dehydrogenase signature *
- *********************************************
-
- 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 beta-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. The mitochondrial enzyme is monofunctional.
-
- 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 eye lens protein lambda-crystallin [3], which is specific to lagomorphes
- (such as rabbit), has been found to be structurally related to 3-hydroxyacyl-
- CoA dehydrogenase.
-
- 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.
-
- -Consensus pattern: G-F-[LIVMF]-x-N-R-[LIVM]-x(2)-[AP]
- -Sequences known to belong to this class detected by the pattern: ALL.
- -Other sequence(s) detected in SWISS-PROT: NONE.
- -Last update: December 1992 / Text revised.
-
- [ 1] Birktoff J.J., Holden H.M., Hamlin R., Xuong N.H., Banaszak L.J.
- Proc. Natl. Acad. Sci. U.S.A. 84:8262-8266(1987).
- [ 2] Nakahigashi K., Inokuchi H.
- Nucleic Acids Res. 18:4937-4937(1990).
- [ 3] Mulders J.W.M., Hendriks W., Blankesteijn W.M., Bloemendal H.,
- de Jong W.W.
- J. Biol. Chem. 263:15462-15466(1988).
-