Family

Methylmalonate-semialdehyde dehydrogenase (IPR010061)

Short name: MeMal-semiAld_DH

Family relationships

Description

Methylmalonate-semialdehyde dehydrogenase (MMSDH, EC=1.2.1.27) catalyses the irreversible NAD+- and CoA-dependent oxidative decarboxylation of methylmalonate semialdehyde to propionyl-CoA. Methylmalonate-semialdehyde dehydrogenase has been characterised in both prokaryotes [PMID: 1339433, PMID: 8550471] and eukaryotes [PMID: 1527093], functioning as a mammalian tetramer and a bacterial homodimer. Although similar in monomeric molecular mass and enzymatic activity, the N-terminal sequence in Pseudomonas aeruginosa does not correspond with the N-terminal sequence predicted for rat liver. Sequence homology to a variety of prokaryotic and eukaryotic aldehyde dehydrogenases places MMSDH in the aldehyde dehydrogenase (NAD+) superfamily making MMSDH's CoA requirement unique among known ALDHs. Methylmalonate semialdehyde dehydrogenase is closely related to betaine aldehyde dehydrogenase, 2-hydroxymuconic semialdehyde dehydrogenase, and class 1 and 2 aldehyde dehydrogenase [PMID: 1527093].

In most cases these enzymes are involved in valine metabolism, but Gram-positive bacteria, such as Bacillus, contain a distinct subset. This subset of enzymes is encoded in an iol operon and is apparently involved in myo-inositol catabolism, converting malonic semialdehyde to acetyl CoA ad CO2 [PMID: 9226270].

GO terms

Biological Process

GO:0055114 oxidation-reduction process

Molecular Function

GO:0004491 methylmalonate-semialdehyde dehydrogenase (acylating) activity

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
PANTHER
TIGRFAMs
CDD
PANTHER