Conserved Site

TPP-binding enzyme, conserved site (IPR000399)

Short name: TPP-bd_CS

Description

A number of enzymes require thiamine pyrophosphate (TPP) (vitamin B1) as a cofactor. It has been shown [PMID: 8604141] that some of these enzymes are structurally related.

Enzymes with a TPP-binding domain include:

  • Pyruvate oxidase (POX) (EC:1.2.3.3). Reaction catalysed: pyruvate + orthophosphate + O(2) + H(2)O = acetyl phosphate + CO(2) + H(2)O(2).
  • Pyruvate decarboxylase (PDC) (EC:4.1.1.1) [PMID: 8604141]. Reaction catalysed: pyruvate = acetaldehyde + CO(2).
  • Indolepyruvate decarboxylase (EC:4.1.1.74) [PMID: 1639814]. Reaction catalysed: indole-3-pyruvate = indole-3-acetaldehyde + CO(2).
  • Acetolactate synthase (ALS) (EC:4.1.3.18). Reaction catalysed: 2x pyruvate = acetolactate + CO(2).
  • Benzoylformate decarboxylase (BFD) (EC:4.1.1.7) [PMID: 12590569]. Reaction catalysed: benzoylformate = benzaldehyde + CO(2).

GO terms

Biological Process

No terms assigned in this category.

Molecular Function

GO:0000287 magnesium ion binding
GO:0030976 thiamine pyrophosphate binding

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
PROSITE patterns