CATH Classification

Domain Context

CATH Clusters

Superfamily S-adenosylmethionine decarboxylase
Functional Family S-adenosylmethionine decarboxylase proenzyme

Enzyme Information

4.1.1.50
Adenosylmethionine decarboxylase.
based on mapping to UniProt P17707
S-adenosyl-L-methionine = S-adenosyl 3-(methylthio)propylamine + CO(2).

UniProtKB Entries (1)

P17707
DCAM_HUMAN
Homo sapiens
S-adenosylmethionine decarboxylase proenzyme

PDB Structure

PDB 1MSV
External Links
Method X-RAY DIFFRACTION
Organism Escherichia
Primary Citation
Mechanism of Human S-Adenosylmethionine Decarboxylase Proenzyme Processing as Revealed by the Structure of the S68A Mutant.
Tolbert, W.D., Zhang, Y., Cottet, S.E., Bennett, E.M., Ekstrom, J.L., Pegg, A.E., Ealick, S.E.
Biochemistry