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Ligands
Code Name Style Show Link
PUT 1,4-diaminobutane
TRS 2-amino-2-hydroxymethyl-propane-1,3-diol
Non-standard Residues
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Glycosylation
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Code : 1JL0   PDBj   RCSB PDB   PDBe
Header : LYASE
Title : Structure of a Human S-Adenosylmethionine Decarboxylase Self-processing Ester Intermediate and Mechanism of Putrescine Stimulation of Processing as Revealed by the H243A Mutant
Release Data : 2001-08-22
Compound :
mol_id molecule chains synonym
1 S-ADENOSYLMETHIONINE DECARBOXYLASE PROENZYME A,B ADOMETDC
ec: 4.1.1.50
mutation: H243A
Source :
mol_id organism_scientific organism_common expression_system
1 Homo sapiens  (taxid:9606) Human Escherichia coli  (taxid:562)
Authors : Ekstrom, J.L., Tolbert, W.D., Xiong, H., Pegg, A.E., Ealick, S.E.
Keywords : SPERMIDINE BIOSYNTHESIS, LYASE, DECARBOXYLASE, PYRUVATE, S-ADENOSYLMETHIONINE, SANDWICH, ALLOSTERIC ENZYME, PYRUVOYL, ESTER INTERMEDIATE, HYDROXYALANINE
Exp. method : X-RAY DIFFRACTION ( 1.50 Å )
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.  et al.
(2001)  Biochemistry  40 : 9495 - 9504

PubMed: 11583148
DOI: 10.1021/bi010736o

The Crystal Structure of Human S-adenosylmethionine Decarboxylase at 2.25 A Resolution Reveals a Novel Fold

Ekstrom, J.L.,Mathews, I.I.,Stanley, B.A.  et al.
(1999)  Structure  7 : 583 - 595

DOI: 10.1016/S0969-2126(99)80074-4

Chain : A, B
UniProt : P17707 (DCAM_HUMAN)
Reaction: EC: Evidence:
Physiological Direction:
H(+) + S-adenosyl-L-methionine = CO2 + S-adenosyl 3- (methylsulfanyl)propylamine 4.1.1.50 PubMed:10029540, PubMed:10574985, PubMed:11583147, PubMed:1917972, PubMed:2460457, PubMed:2687270
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