PROSITE documentation PDOC00166
Thiamine pyrophosphate enzymes signature


A number of enzymes require thiamine pyrophosphate (TPP) (vitamin B1) as a cofactor. It has been shown [1] that some of these enzymes are structurally related. These related TPP enzymes are:

  • Pyruvate oxidase (POX) (EC Reaction catalyzed: pyruvate + orthophosphate + O(2) + H(2)O = acetyl phosphate + CO(2) + H(2)O(2).
  • Pyruvate decarboxylase (PDC) (EC Reaction catalyzed: pyruvate = acetaldehyde + CO(2).
  • Indolepyruvate decarboxylase (EC [2] Reaction catalyzed: indole-3-pyruvate = indole-3-acetaldehyde + CO(2).
  • Acetolactate synthase (ALS) (EC Reaction catalyzed: 2 pyruvate = acetolactate + CO(2).
  • Benzoylformate decarboxylase (BFD) (EC [3] Reaction catalyzed: benzoylformate = benzaldehyde + CO(2).

As a signature pattern for these enzymes we have selected a conserved region which is located in their C-terminal section.


Other TPP enzymes such as the E1 component of pyruvate dehydrogenase complex, 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase, and transketolase do not seem to be related to the above enzymes.

Last update:

November 1995 / Pattern and text revised.


Technical section

PROSITE method (with tools and information) covered by this documentation:

TPP_ENZYMES, PS00187; Thiamine pyrophosphate enzymes signature  (PATTERN)


1AuthorsGreen J.B.A.
TitlePyruvate decarboxylase is like acetolactate synthase (ILV2) and not like the pyruvate dehydrogenase E1 subunit.
SourceFEBS Lett. 246:1-5(1989).
PubMed ID2651151

2AuthorsKoga J. Adachi T. Hidaka H.
TitleMolecular cloning of the gene for indolepyruvate decarboxylase from Enterobacter cloacae.
SourceMol. Gen. Genet. 226:10-16(1991).
PubMed ID2034209

3AuthorsTsou A.Y. Ransom S.C. Gerlt J.A. Buechter D.D. Babbitt P.C. Kenyon G.L.
TitleMandelate pathway of Pseudomonas putida: sequence relationships involving mandelate racemase, (S)-mandelate dehydrogenase, and benzoylformate decarboxylase and expression of benzoylformate decarboxylase in Escherichia coli.
SourceBiochemistry 29:9856-9862(1990).
PubMed ID2271624

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