Protein Family Models

It is clear from the structures of bacterial members of MaoC dehydratase, Pfam:PF01575, that the full-length functional dehydratase enzyme is made up of two structures that dimerise to form a whole. Divergence of the N- and C- monomers in higher eukaryotes has led to two distinct domains, this one and MaoC_dehydratas. However, in order to function as an enzyme both are required together. (from Pfam)

Date:

2024-08-14

The maoC gene is part of a operon with maoA which is involved in the synthesis of monoamine oxidase [1]. The MaoC protein is found to share similarity with a wide variety of enzymes; estradiol 17 beta-dehydrogenase 4, peroxisomal hydratase-dehydrogenase-epimerase, fatty acid synthase beta subunit. Several bacterial proteins that are composed solely of this domain have (R)-specific enoyl-CoA hydratase activity [2]. This domain is also present in the NodN nodulation protein N. [1]. 8647101. A monoamine-regulated Klebsiella aerogenes operon containing the. monoamine oxidase structural gene (maoA) and the maoC gene.. Sugino H, Sasaki M, Azakami H, Yamashita M, Murooka Y. J Bacteriol 1992;174:2485-2492.. [2]. 9457873. Expression and characterization of (R)-specific enoyl coenzyme A. hydratase involved in polyhydroxyalkanoate biosynthesis by. Aeromonas caviae.. Fukui T, Shiomi N, Doi Y;. J Bacteriol. 1998;180:667-673. (from Pfam)

Date:

2024-08-14