DB code: D00252

CATH domain 4.10.510.10 : Pyruvoyl-Dependent Histidine Decarboxylas; Chain A Catalytic domain
3.50.20.10 : Pyruvoyl-Dependent Histidine Decarboxylase; Chain B Catalytic domain
E.C. 4.1.1.22
CSA 1pya
M-CSA 1pya
MACiE M0049

CATH domain Related DB codes (homologues)

Uniprot Enzyme Name
UniprotKB Protein name Synonyms Contains Pfam
P00862 Histidine decarboxylase proenzyme
EC 4.1.1.22
Pi chain
Histidine decarboxylase beta chain
Histidine decarboxylase alpha chain
PF02329 (HDC)
[Graphical View]

KEGG enzyme name
histidine decarboxylase
L-histidine decarboxylase
L-histidine carboxy-lyase

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P00862 DCHS_LACS3 L-histidine = histamine + CO(2). The 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. Pyruvoyl group.

KEGG Pathways
Map code Pathways E.C.
MAP00340 Histidine metabolism

Compound table
Cofactors Substrates Products Intermediates
KEGG-id C00022 C00135 C00388 C00011
E.C.
Compound Pyruvate L-Histidine Histamine CO2
Type carbohydrate,carboxyl group amino acids,aromatic ring (with nitrogen atoms) amine group,aromatic ring (with nitrogen atoms) others
ChEBI 32816
 32816
 		15971
 57595
 15971
 57595
 		18295
 18295
 		16526
 16526
PubChem 1060
 1060
 		6274
 6971009
 6274
 6971009
 		774
 774
 		280
 280
1hq6A Unbound Unbound Unbound Unbound
1hq6C Unbound Unbound Unbound Unbound
1pyaA Unbound Unbound Unbound Unbound
1pyaC Unbound Unbound Unbound Unbound
1pyaE Unbound Unbound Unbound Unbound
1hq6B Bound:PYR_82 Unbound Unbound Unbound
1hq6D Bound:PYR_82 Unbound Unbound Unbound
1pyaB Unbound Unbound Unbound Unbound
1pyaD Unbound Unbound Unbound Unbound
1pyaF Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
Swiss-prot;P00862 & literature [4] & [8]

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1hq6A SER 81
1hq6C SER 81
1pyaA SER 81
1pyaC SER 81
1pyaE SER 81
1hq6B LYS 155;GLU 197 PYR 82(Pyruvoyl group) PHE 195
1hq6D LYS 155;GLU 197 PYR 82(Pyruvoyl group) PHE 195
1pyaB LYS 155;GLU 197 PHE 195 invisible PYR82(Pyruvoyl group)
1pyaD LYS 155;GLU 197 PHE 195 invisible PYR82(Pyruvoyl group)
1pyaF LYS 155;GLU 197 PHE 195 invisible PYR82(Pyruvoyl group)

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[4]
Fig.2 8
[5]
Fig.4, Fig.5, Fig. 6 4
[8]
Fig.2 3

References
[1]
Resource
Comments
Medline ID
PubMed ID 199715
Journal J Pharm Sci
Year 1977
Volume 66
Pages 1660-2
Authors Johnson HL, Thomas DW, Ellis M, Cary L, DeGraw JI
Title Application of 13C-NMR spectroscopy to in vitro analysis of enzyme kinetics.
Related PDB
Related UniProtKB
[2]
Resource
Comments
Medline ID
PubMed ID 7451468
Journal J Biol Chem
Year 1981
Volume 256
Pages 687-90
Authors Hackert ML, Meador WE, Oliver RM, Salmon JB, Recsei PA, Snell EE
Title Crystallization and subunit structure of histidine decarboxylase from Lactobacillus 30a.
Related PDB
Related UniProtKB
[3]
Resource
Comments X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
Medline ID 85237485
PubMed ID 4009714
Journal J Mol Biol
Year 1985
Volume 182
Pages 455-65
Authors Parks EH, Ernst SR, Hamlin R, Xuong NH, Hackert ML
Title Structure determination of histidine decarboxylase from Lactobacillus 30a at 3.0 A resolution.
Related PDB
Related UniProtKB P00862
[4]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
Medline ID 89308713
PubMed ID 2745463
Journal J Biol Chem
Year 1989
Volume 264
Pages 12737-43
Authors Gallagher T, Snell EE, Hackert ML
Title Pyruvoyl-dependent histidine decarboxylase. Active site structure and mechanistic analysis.
Related PDB
Related UniProtKB P00862
[5]
Resource
Comments
Medline ID
PubMed ID 2813341
Journal Protein Eng
Year 1989
Volume 3
Pages 43-8
Authors McElroy HE, Robertus JD
Title Site-directed alteration of Glu197 and Glu66 in a pyruvoyl-dependent histidine decarboxylase.
Related PDB
Related UniProtKB
[6]
Resource
Comments
Medline ID
PubMed ID 2197977
Journal Annu Rev Biochem
Year 1990
Volume 59
Pages 29-59
Authors van Poelje PD, Snell EE
Title Pyruvoyl-dependent enzymes.
Related PDB
Related UniProtKB
[7]
Resource
Comments
Medline ID
PubMed ID 2261482
Journal Biochemistry
Year 1990
Volume 29
Pages 10413-8
Authors van Poelje PD, Kamath AV, Snell EE
Title Site-directed alteration of the active-site residues of histidine decarboxylase from Clostridium perfringens.
Related PDB
Related UniProtKB
[8]
Resource
Comments
Medline ID
PubMed ID 1989676
Journal Biochemistry
Year 1991
Volume 30
Pages 1057-62
Authors Gelfman CM, Copeland WC, Robertus JD
Title Site-directed alteration of four active-site residues of a pyruvoyl-dependent histidine decarboxylase.
Related PDB
Related UniProtKB
[9]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
Medline ID 93217991
PubMed ID 8464063
Journal J Mol Biol
Year 1993
Volume 230
Pages 516-28
Authors Gallagher T, Rozwarski DA, Ernst SR, Hackert ML
Title Refined structure of the pyruvoyl-dependent histidine decarboxylase from Lactobacillus 30a.
Related PDB 1pya
Related UniProtKB P00862
[10]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
Medline ID 21140141
PubMed ID 11243783
Journal J Mol Biol
Year 2001
Volume 306
Pages 727-32
Authors Schelp E, Worley S, Monzingo AF, Ernst S, Robertus JD
Title pH-induced structural changes regulate histidine decarboxylase activity in Lactobacillus 30a.
Related PDB 1hq6
Related UniProtKB P00862

Comments

Created Updated
2004-05-20 2009-02-26