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.
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