v5.1.0.3
Glycine data from LIS
Type | Domain |
Description | In general, the Gfo/Idh/MocA protein family members are enzymes that catalyse various different chemical reactions such as oxidation and reduction of carbohydrates, oxidation of trans-dihydrodiols, reduction of biliverdin, and hydrolysation of glycosidic bonds. All the enzymes in this family utilise NAD(P) as a hydride donor or acceptor. However, despite the structural similarities, some member such as the transcriptional repressor Gal80p, does not have enzymatic activity [ ]. The Gfo/Idh/MocA protein family members consists of two main domains: an N-terminal dinucleotide-binding domain containing a typical Rossmann fold3 and a C-terminal alpha/beta-domain participating in substrate binding and oligomerisation. This entry represents the C-terminal domain [ ]. |
Short Name | Gfo/Idh/MocA-like_OxRdtase_C |