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 1JL0
External Links
Method X-RAY DIFFRACTION
Organism Escherichia
Primary Citation
Structure of a human S-adenosylmethionine decarboxylase self-processing ester intermediate and mechanism of putrescine stimulation of processing as revealed by the H243A mutant.
Ekstrom, J.L., Tolbert, W.D., Xiong, H., Pegg, A.E., Ealick, S.E.
Biochemistry