EzCatDB: D00252

DB codeD00252
CATH domainDomain 14.10.510.10Catalytic domain
Domain 23.50.20.10Catalytic domain
E.C.4.1.1.22
CSA1pya
MACiEM0049


Enzyme Name
Swiss-protKEGG

P00862
Protein nameHistidine decarboxylase proenzymehistidine decarboxylase
L-histidine decarboxylase
L-histidine carboxy-lyase
SynonymsEC 4.1.1.22
Pi chain
ContainsHistidine decarboxylase beta chain
Histidine decarboxylase alpha chain

KEGG pathways
MAP codePathways
MAP00340Histidine metabolism

Swiss-prot:Accession NumberP00862
Entry nameDCHS_LACS3
ActivityL-histidine = histamine + CO(2).
SubunitThe proenzyme is a hexamer of identical pi chains, each pi chain monomer is cleaved to form a small (or beta) chain and a large (or alpha) chain by non-hydrolytic self-catalysis.
Subcellular location
CofactorPyruvoyl group.


CofactorsSubstratesProducts
KEGG-idC00022C00135C00388C00011
CompoundPyruvateL-HistidineHistamineCO2
Typecarbohydrate,carboxyl groupamino acids,aromatic ring (with nitrogen atoms)amine group,aromatic ring (with nitrogen atoms)others
1hq6AUnboundUnboundUnboundUnbound
1hq6CUnboundUnboundUnboundUnbound
1pyaAUnboundUnboundUnboundUnbound
1pyaCUnboundUnboundUnboundUnbound
1pyaEUnboundUnboundUnboundUnbound
1hq6BBound:PYR 82UnboundUnboundUnbound
1hq6DBound:PYR 82UnboundUnboundUnbound
1pyaBUnboundUnboundUnboundUnbound
1pyaDUnboundUnboundUnboundUnbound
1pyaFUnboundUnboundUnboundUnbound

Active-site residues
resource
Swiss-prot;P00862 & literature [4] & [8]
pdbCatalytic residuesModified residuesMain-chain involved in catalysiscomment
1hq6ASER 81



1hq6CSER 81



1pyaASER 81



1pyaCSER 81



1pyaESER 81



1hq6BLYS 155;GLU 197
PYR 82(Pyruvoyl group)
PHE 195

1hq6DLYS 155;GLU 197
PYR 82(Pyruvoyl group)
PHE 195

1pyaBLYS 155;GLU 197
                      
PHE 195
invisible PYR82(Pyruvoyl group)
1pyaDLYS 155;GLU 197
                      
PHE 195
invisible PYR82(Pyruvoyl group)
1pyaFLYS 155;GLU 197
                      
PHE 195
invisible PYR82(Pyruvoyl group)

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[4]Fig.28
[5]Fig.4, Fig.5, Fig. 64
[8]Fig.23

references
[1]
PubMed ID199715
JournalJ Pharm Sci
Year1977
Volume66
Pages1660-2
AuthorsJohnson HL, Thomas DW, Ellis M, Cary L, DeGraw JI
TitleApplication of 13C-NMR spectroscopy to in vitro analysis of enzyme kinetics.
[2]
PubMed ID7451468
JournalJ Biol Chem
Year1981
Volume256
Pages687-90
AuthorsHackert ML, Meador WE, Oliver RM, Salmon JB, Recsei PA, Snell EE
TitleCrystallization and subunit structure of histidine decarboxylase from Lactobacillus 30a.
[3]
CommentsX-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
Medline ID85237485
PubMed ID4009714
JournalJ Mol Biol
Year1985
Volume182
Pages455-65
AuthorsParks EH, Ernst SR, Hamlin R, Xuong NH, Hackert ML
TitleStructure determination of histidine decarboxylase from Lactobacillus 30a at 3.0 A resolution.
Related Swiss-protP00862
[4]
CommentsX-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
Medline ID89308713
PubMed ID2745463
JournalJ Biol Chem
Year1989
Volume264
Pages12737-43
AuthorsGallagher T, Snell EE, Hackert ML
TitlePyruvoyl-dependent histidine decarboxylase. Active site structure and mechanistic analysis.
Related Swiss-protP00862
[5]
PubMed ID2813341
JournalProtein Eng
Year1989
Volume3
Pages43-8
AuthorsMcElroy HE, Robertus JD
TitleSite-directed alteration of Glu197 and Glu66 in a pyruvoyl-dependent histidine decarboxylase.
[6]
PubMed ID2197977
JournalAnnu Rev Biochem
Year1990
Volume59
Pages29-59
Authorsvan Poelje PD, Snell EE
TitlePyruvoyl-dependent enzymes.
[7]
PubMed ID2261482
JournalBiochemistry
Year1990
Volume29
Pages10413-8
Authorsvan Poelje PD, Kamath AV, Snell EE
TitleSite-directed alteration of the active-site residues of histidine decarboxylase from Clostridium perfringens.
[8]
PubMed ID1989676
JournalBiochemistry
Year1991
Volume30
Pages1057-62
AuthorsGelfman CM, Copeland WC, Robertus JD
TitleSite-directed alteration of four active-site residues of a pyruvoyl-dependent histidine decarboxylase.
[9]
CommentsX-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
Medline ID93217991
PubMed ID8464063
JournalJ Mol Biol
Year1993
Volume230
Pages516-28
AuthorsGallagher T, Rozwarski DA, Ernst SR, Hackert ML
TitleRefined structure of the pyruvoyl-dependent histidine decarboxylase from Lactobacillus 30a.
Related PDB1pya
Related Swiss-protP00862
[10]
CommentsX-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
Medline ID21140141
PubMed ID11243783
JournalJ Mol Biol
Year2001
Volume306
Pages727-32
AuthorsSchelp E, Worley S, Monzingo AF, Ernst S, Robertus JD
TitlepH-induced structural changes regulate histidine decarboxylase activity in Lactobacillus 30a.
Related PDB1hq6
Related Swiss-protP00862


createdupdated
2004-05-202009-02-26


Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2010)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)

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