Glutamate formimidoyltransferase

Glutamate formimidoyltransferase

Formiminotransferase domain, N-terminal subdomain
the crystal structure of the formiminotransferase domain of formiminotransferase-cyclodeaminase.
Identifiers
Symbol FTCD_N
Pfam InterPro IPR012886
SCOP SUPERFAMILY 1qd1
Formiminotransferase domain
the crystal structure of the formiminotransferase domain of formiminotransferase-cyclodeaminase.
Identifiers
Symbol FTCD
Pfam InterPro IPR013802
SCOP SUPERFAMILY 1qd1

In molecular biology, Glutamate formimidoyltransferase is a methyltransferase enzyme which uses tetrahydrofolate as part of histidine catabolism. It catalyses two reactions:

  • 5-formyltetrahydrofolate + L-glutamate <=> tetrahydrofolate + N-formyl-L-glutamate

It is classified under

Structure

The formiminotransferase (FT) domain of formiminotransferase-cyclodeaminase (FTCD) forms a homodimer, with each protomer comprising two subdomains. The formiminotransferase domain has an N-terminal subdomain that is made up of a six-stranded mixed beta-pleated sheet and five alpha helices, which are arranged on the external surface of the beta sheet. This, in turn, faces the beta-sheet of the C-terminal subdomain to form a double beta-sheet layer. The two subdomains are separated by a short linker sequence, which is not thought to be any more flexible than the remainder of the molecule. The substrate is predicted to form a number of contacts with residues found in both the N-terminal and C-terminal subdomains.[2] In humans, deficiency of this enzyme results in a disease phenotype.[3]

References

External links

  • Medical Subject Headings (MeSH)

This article incorporates text from the IPR013802

This article incorporates text from the IPR012886