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Information on EC 4.1.1.22 - histidine decarboxylase and Organism(s) Lactobacillus sp. and UniProt Accession P00862
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4.1.1.22 histidine decarboxylaseIUBMB Comments
A pyridoxal-phosphate protein (in animal tissues). The bacterial enzyme has a pyruvoyl residue as prosthetic group.
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- 4.1.1.22
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high-dose
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mast
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autologous
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histaminergic
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h1-receptors
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standard-dose
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cell-deficient
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chlorpheniramine
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snell
The taxonomic range for the selected organisms is: Lactobacillus sp.
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
hdc, histidine decarboxylase, l-histidine decarboxylase, histamine-forming enzyme, hisdcase, pyruvoyl-dependent histidine decarboxylase, pyruvoyl-dependent decarboxylase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Decarboxylase, histidine
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HDC
HisDCase
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L-Histidine decarboxylase
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-
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TOM92
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-
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HDC
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
decarboxylation
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-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
L-histidine carboxy-lyase (histamine-forming)
A pyridoxal-phosphate protein (in animal tissues). The bacterial enzyme has a pyruvoyl residue as prosthetic group.
CAS REGISTRY NUMBER
COMMENTARY
9024-61-7
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
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HDC uses a covalently bound pyruvoyl moiety as cofactor
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SH-groups
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wild type and mutant enzyme each contain two SH groups per alpha-chain
pyruvate
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contains several functionally essential pyruvate residues, covalently bound through an amide linkage to a Phe residue of the peptide chain. The free carbonyl group of these pyruvate residues undergoes Schiff base formation with His as part of the catalytic process
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.8
4.8
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HDC is essentially inactive at neutral and alkaline pH and active at low pH, low pH shifts HDC from the inactive, i.e. T-state, to the active, i.e. R-state
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
24892
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6 * 24892, alpha, + 6 * 8856, beta, calculation from amino acid sequence
8856
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6 * 24892, alpha, + 6 * 8856, beta, calculation from amino acid sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dodecamer
additional information
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a pyruvate-free proenzyme pi-chain, MW: 37000, is converted during activation to a beta-chain, MW 9000, with a carboxy-terminal Ser residue and an alpha-chain, MW: 28000, with a pyruvoyl group blocking the amino-terminus
dodecamer
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6 * 24892, alpha, + 6 * 8856, beta, calculation from amino acid sequence
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of active HDC at pH 4.8 at 2.5 A resolution, crystal structure of less active HDC at pH 8.0 at 2.7 A resolution, crystals are grown at room temperatur by hanging-drop vapor diffusion, drops contain 0.004 ml HDC at 12.5 mg/ml, 0.001 ml n-dodecyl-beta-D-maltoside and 0.005 ml precipitant solution from the well containing 25% polyethylene glycol 400, 8% polyethylene glycol 400, 100 mM Tris pH 8.0, and 100 mM sodium acetate, enzyme activity is regulated by pH-induced structural changes
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D53N/D54N
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crystal structure of apo-D53N/D54N double mutant and of mutant complexed with the substrate-analog inhibitor histidine methyl ester, crystals are grown at room temperature by hanging-drop vapor diffusion, drops contain 0.005 ml HDC at 12 mg/ml and 0.005 ml of precipitant solution from the well containing 0-15% polyethylene glycol 400, 4-8% polyethylene glycol 4000, 100 mM sodium acetate, pH 4.6, crystals diffract to 3.2 A
S51A/G58D
S51A/G58D
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mutant enzyme 3 has two amino acid replacements, both in the beta chain: Ser51 is replaced by Ala and Gly58 by Asp. In addition, about 15% of the mutant beta chains contain Met-Ser at the NH2-terminus rather than Ser. These replacements decrease stability of the enzyme and change its pH activity profile, but do not decrease its activity at pH 4.8, its optimum
S51A/G58D
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mutant enzyme Ser51Ala/Gly58Asp shows a significantly increased alpha-helical content and a significant decrease in the isoelectric point of the beta chain, consistent with changes in physical and catalytic properties of the mutant enzyme
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
separation of unmodified alpha and beta subunits and for reconstitution of fully active histidine decarboxylase
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Yamagata, S.; Snell, E.E.
Histidine decarboxylase from Lactobacillus 30a: reconstitution from separated subunits
Biochemistry
18
2964-2967
1979
Lactobacillus sp.
Hackert, M.L.; Meador, W.E.; Oliver, R.M.; Salmon, J.B.
Crystallization and subunit structure of histidine decarboxylase from Lactobacillus 30a
J. Biol. Chem.
256
687-690
1981
Lactobacillus sp.
Parks, E.H.; Ernst, S.R.; Hamlin, R.; Xuong, N.H.; Hackert, M.L.
Structure determination of histidine decarboxylase from Lactobacillus 30a at 3.0 A resolution
J. Mol. Biol.
182
455-465
1985
Lactobacillus sp.
Chang, G.W.; Snell, E.E.
Histidine decarboxylase (Lactobacillus 30a)
Methods Enzymol.
17B
663-667
1971
Lactobacillus sp.
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Recsei, P.A.; Snell, E.E.
Histidine decarboxylase from Lactobacillus 30a. Comparative properties of wild type and mutant proenzymes and their derived enzymes
J. Biol. Chem.
257
7196-7202
1982
Lactobacillus sp.
Snell, E.E.
Pyruvoyl-dependent histidine decarboxylase from Lactobacillus 30a: purification and properties
Methods Enzymol.
122
128-135
1986
Lactobacillus sp.
Coton, E.; Rollan, G.C.; Lonvaud-Funel, A.
Histidine carboxylase of Leuconostoc oenos 9204: purification, kinetic properties, cloning and nucleotide sequence of the hdc gene
J. Appl. Microbiol.
84
143-151
1998
Clostridium perfringens, Lentilactobacillus buchneri, Lactobacillus sp., Oenococcus oeni, Micrococcus sp., Oenococcus oeni 9204
Vaaler, G.L.; Recsei, P.A.; Fox, J.L.; Snell, E.E.
Histidine decarboxylase of Lactobacillus 30a. Comparative sequence of the beta chain from wild type and mutant enzymes
J. Biol. Chem.
257
12770-12774
1982
Lactobacillus sp.
Schelp, E.; Worley, S.; Monzingo, A.F.; Ernst, S.; Robertus, J.D.
pH-induced structural changes regulate histidine decarboxylase activity in Lactobacillus 30a
J. Mol. Biol.
306
727-732
2001
Lactobacillus sp. (P00862)
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