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Information on EC 4.1.1.22 - histidine decarboxylase
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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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Word Map
- 4.1.1.22
-
high-dose
-
mast
-
autologous
-
histaminergic
- mucosa
- stomach
- gastrin
- marrow
- hypothalamus
-
hematopoietic
- alpha-fluoromethylhistidine
- cyclophosphamide
-
oxyntic
-
enterochromaffin-like
-
allergic
-
relapsed
- etoposide
-
biogenic
-
thiotepa
- melphalan
- decarboxylases
- cimetidine
-
tuberomammillary
- carboplatin
-
basophil
-
chromogranin
- omeprazole
-
stem-cell
-
h1-receptors
- morganii
-
pyrilamine
- thioperamide
-
hypergastrinemia
-
event-free
- morganella
- carmustine
-
mepyramine
- mucositis
-
busulfan
-
cell-deficient
- fundic
- mastocytoma
- tourette
-
sleep-wake
-
standard-dose
- pentagastrin
-
reinfusion
- drug development
- nutrition
-
aminergic
-
snell
-
chlorpheniramine
- diagnostics
- medicine
The enzyme appears in viruses and cellular organisms
Synonyms
DCHS, Decarboxylase, histidine, HDC, HdcA, HisDCase, histamine-forming enzyme, L-Histidine decarboxylase, pyruvoyl-dependent decarboxylase, pyruvoyl-dependent histidine decarboxylase, TOM92, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Decarboxylase, histidine
-
-
-
-
HDC
HdcA
HisDCase
-
-
-
-
L-Histidine decarboxylase
pyruvoyl-dependent decarboxylase
pyruvoyl-dependent histidine decarboxylase
TOM92
-
-
-
-
HDC
-
-
-
-
HDC
-
-
HDC
-
-
L-Histidine decarboxylase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-histidine = histamine + CO2
-
-
-
-
L-histidine = histamine + CO2
structure-activity relationship, active site structure, molecular modeling, the imidazole ring is located in a pocket composed of residues Tyr-81B, Asn-302B, Ser-304B, Lys-305B, Leu-102A, Phe-104A, and Ser-354A
L-histidine = histamine + CO2
catalytic mechanism, quantum mechanics-molecular mechanics study and molecular dynamics simulations using the enzyme's crystal structure, PDB ID 4E1O, overview. The reaction involves two sequential steps: the decarboxylation of L-histidine and the protonation of the generated intermediate from which results histamine. The rate-limiting step is the first one with an activation barrier of 17.9 kcal/mol. In contrast, the second step is very fast and exergonic. When the substrate L-histidine is available in the active site of HDC, it binds to the pyridoxal 5'-phosphate cofactor. In this process, the imine bond formed between pyridoxal 5'-phosphate and Lys305A is cleaved and a new external aldimine intermediate is created between the pyridoxal 5'-phosphate cofactor and the amino group of the substrate
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
decarboxylation
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
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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.
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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
3,4-Dihydroxyphenylalanine
Dopamine + CO2
no substate for wild-type. Mutant S354G acquires the ability to decarboxylate 3,4-dihydroxyphenylalanine
-
-
?
L-histidine
histamine + CO2
structure-function relationship, molecular modeling, overview
-
-
?
L-histidine
histamine + CO2
structure-function relationship, molecular modeling, overview
-
-
?
L-histidine
histamine + CO2
structure-function relationship, molecular modeling, overview
-
-
?
L-histidine
histamine + CO2
structure-function relationship, molecular modeling, overview
-
-
?
L-histidine
histamine + CO2
structure-function relationship, molecular modeling, overview
-
-
?
L-histidine
histamine + CO2
-
-
-
-
?
L-histidine
histamine + CO2
-
HDC is the key enzyme involved in histamine production
-
-
?
L-histidine
histamine + CO2
-
histamine is a bioactive amine acting as a neurotransmitter as well as a chemical mediator
-
-
?
L-histidine
histamine + CO2
-
rate-limiting step in histamine biosynthesis, enzyme activity is increased in pre-eclampsia, a complex of disorder of pregnancy involving a systemic inflammatory response and endothelial activation within the maternal vascular system, overview
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-
?
L-histidine
histamine + CO2
structure-function relationship, molecular modeling, overview
-
-
?
L-histidine
histamine + CO2
the binding site of HDC does not tolerate groups other than the imidazole side chain of histidine
-
-
?
L-histidine
histamine + CO2
structure-function relationship, molecular modeling, overview
-
-
?
L-histidine
histamine + CO2
-
expression of hdc is also mediated by the bacterial growth phase, overview
-
-
?
L-histidine
histamine + CO2
-
expression of hdc is also mediated by the bacterial growth phase, overview
-
-
?
L-histidine
histamine + CO2
structure-function relationship, molecular modeling, overview
-
-
?
L-histidine
histamine + CO2
histamine-producing bacteria, such as Morganella morganii, possess histidine decarboxylase, which is responsible for histamine fish poisoning due to to the ingestion of fish containing high levels of histamine produced by the bacteria
-
-
?
L-histidine
histamine + CO2
structure-function relationship, molecular modeling, overview
-
-
?
L-histidine
histamine + CO2
-
-
-
-
?
L-histidine
histamine + CO2
-
HDC induction may contribute to the replenishment of the reduced pool of mast cell histamine in the anaphylactic period
-
-
?
L-histidine
histamine + CO2
-
HDC is the rate-limiting enzyme for histamine synthesis
-
-
?
L-histidine
histamine + CO2
structure-function relationship, molecular modeling, overview
-
-
?
L-histidine
histamine + CO2
-
HDC is the rate-limiting enzyme for histamine synthesis
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-
?
L-histidine
histamine + CO2
-
expression of hdc is also mediated by the bacterial growth phase, overview
-
-
?
L-histidine
histamine + CO2
-
expression of hdc is also mediated by the bacterial growth phase, overview
-
-
?
L-histidine
histamine + CO2
structure-function relationship, molecular modeling, overview
-
-
?
L-histidine
histamine + CO2
-
expression of hdc is also mediated by the bacterial growth phase, overview
-
-
?
L-histidine
histamine + CO2
-
expression of hdc is also mediated by the bacterial growth phase, overview
-
-
?
L-histidine
histamine + CO2
histamine-producing bacteria, such as Photobacterium damselae, possess histidine decarboxylase, which is responsible for histamine fish poisoning due to to the ingestion of fish containing high levels of histamine produced by the bacteria
-
-
?
L-histidine
histamine + CO2
histamine-producing bacteria, such as Photobacterium damselae, possess histidine decarboxylase, which is responsible for histamine fish poisoning due to to the ingestion of fish containing high levels of histamine produced by the bacteria
-
-
?
L-histidine
histamine + CO2
histamine-producing bacteria, such as Photobacterium phosphoreum, possess histidine decarboxylase, which is responsible for histamine fish poisoning due to to the ingestion of fish containing high levels of histamine produced by the bacteria
-
-
?
L-histidine
histamine + CO2
structure-function relationship, molecular modeling, overview
-
-
?
L-histidine
histamine + CO2
histamine-producing bacteria, such as Photobacterium phosphoreum, possess histidine decarboxylase, which is responsible for histamine fish poisoning due to to the ingestion of fish containing high levels of histamine produced by the bacteria
-
-
?
L-histidine
histamine + CO2
histamine-producing bacteria, such as Photobacterium phosphoreum, possess histidine decarboxylase, which is responsible for histamine fish poisoning due to to the ingestion of fish containing high levels of histamine produced by the bacteria
-
-
?
L-histidine
histamine + CO2
structure-function relationship, molecular modeling, overview
-
-
?
L-histidine
histamine + CO2
-
histamine-producing bacteria, such as Raoultella planticola, possess histidine decarboxylase, which is responsible for histamine fish poisoning due to to the ingestion of fish containing high levels of histamine produced by the bacteria
-
-
?
L-histidine
histamine + CO2
-
the enzyme has roles in inflammatory and neurological diseases, and in progression of several cancer types
-
-
?
L-histidine
histamine + CO2
structure-function relationship, molecular modeling, overview
-
-
?
L-histidine
histamine + CO2
-
the enzyme is a group II pyridoxal 5Ć¢ĀĀ-phosphate-dependent L-amino acid decarboxylase, L-aaDCII
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-
?
L-histidine
histamine + CO2
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-
-
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?
L-histidine
histamine + CO2
structure-function relationship, molecular modeling, overview
-
-
?
L-histidine
histamine + CO2
structure-function relationship, molecular modeling, overview
-
-
?
L-histidine
histamine + CO2
structure-function relationship, molecular modeling, overview
-
-
?
additional information
?
-
enzyme immunoassay for detection of histamine production
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-
?
additional information
?
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-
enzyme immunoassay for detection of histamine production
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-
?
additional information
?
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-
mast cells are known to produce histamine through a difference mechanism than HDC induction
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-
?
additional information
?
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-
biocomputational analysis of the evolutionary specificity-determinants in decreasing order: Y279, D315, P85, M97, S77, L132, R361, Y83, D348, S112, Q150, G40, L377, R415, A82, W75, P70, R286, L285, and I430, overview
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-
?
additional information
?
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-
HDC is the key enzyme for histamine biosynthesis
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-
?
additional information
?
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no substrates: lysine, arginine, tyrosine, tryptophan or ornithine
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-
?
additional information
?
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no substrates: lysine, arginine, tyrosine, tryptophan or ornithine
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-
?
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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
L-histidine
histamine + CO2
-
HDC is the key enzyme involved in histamine production
-
-
?
L-histidine
histamine + CO2
-
histamine is a bioactive amine acting as a neurotransmitter as well as a chemical mediator
-
-
?
L-histidine
histamine + CO2
-
rate-limiting step in histamine biosynthesis, enzyme activity is increased in pre-eclampsia, a complex of disorder of pregnancy involving a systemic inflammatory response and endothelial activation within the maternal vascular system, overview
-
-
?
L-histidine
histamine + CO2
-
expression of hdc is also mediated by the bacterial growth phase, overview
-
-
?
L-histidine
histamine + CO2
-
expression of hdc is also mediated by the bacterial growth phase, overview
-
-
?
L-histidine
histamine + CO2
histamine-producing bacteria, such as Morganella morganii, possess histidine decarboxylase, which is responsible for histamine fish poisoning due to to the ingestion of fish containing high levels of histamine produced by the bacteria
-
-
?
L-histidine
histamine + CO2
-
HDC induction may contribute to the replenishment of the reduced pool of mast cell histamine in the anaphylactic period
-
-
?
L-histidine
histamine + CO2
-
HDC is the rate-limiting enzyme for histamine synthesis
-
-
?
L-histidine
histamine + CO2
-
HDC is the rate-limiting enzyme for histamine synthesis
-
-
?
L-histidine
histamine + CO2
-
expression of hdc is also mediated by the bacterial growth phase, overview
-
-
?
L-histidine
histamine + CO2
-
expression of hdc is also mediated by the bacterial growth phase, overview
-
-
?
L-histidine
histamine + CO2
-
expression of hdc is also mediated by the bacterial growth phase, overview
-
-
?
L-histidine
histamine + CO2
-
expression of hdc is also mediated by the bacterial growth phase, overview
-
-
?
L-histidine
histamine + CO2
histamine-producing bacteria, such as Photobacterium damselae, possess histidine decarboxylase, which is responsible for histamine fish poisoning due to to the ingestion of fish containing high levels of histamine produced by the bacteria
-
-
?
L-histidine
histamine + CO2
histamine-producing bacteria, such as Photobacterium damselae, possess histidine decarboxylase, which is responsible for histamine fish poisoning due to to the ingestion of fish containing high levels of histamine produced by the bacteria
-
-
?
L-histidine
histamine + CO2
histamine-producing bacteria, such as Photobacterium phosphoreum, possess histidine decarboxylase, which is responsible for histamine fish poisoning due to to the ingestion of fish containing high levels of histamine produced by the bacteria
-
-
?
L-histidine
histamine + CO2
histamine-producing bacteria, such as Photobacterium phosphoreum, possess histidine decarboxylase, which is responsible for histamine fish poisoning due to to the ingestion of fish containing high levels of histamine produced by the bacteria
-
-
?
L-histidine
histamine + CO2
histamine-producing bacteria, such as Photobacterium phosphoreum, possess histidine decarboxylase, which is responsible for histamine fish poisoning due to to the ingestion of fish containing high levels of histamine produced by the bacteria
-
-
?
L-histidine
histamine + CO2
-
histamine-producing bacteria, such as Raoultella planticola, possess histidine decarboxylase, which is responsible for histamine fish poisoning due to to the ingestion of fish containing high levels of histamine produced by the bacteria
-
-
?
L-histidine
histamine + CO2
-
the enzyme has roles in inflammatory and neurological diseases, and in progression of several cancer types
-
-
?
additional information
?
-
-
mast cells are known to produce histamine through a difference mechanism than HDC induction
-
-
?
additional information
?
-
-
biocomputational analysis of the evolutionary specificity-determinants in decreasing order: Y279, D315, P85, M97, S77, L132, R361, Y83, D348, S112, Q150, G40, L377, R415, A82, W75, P70, R286, L285, and I430, overview
-
-
?
additional information
?
-
-
HDC is the key enzyme for histamine biosynthesis
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
contains 1 mol of pyridoxal 5'-phosphate per mol of subunit
pyridoxal 5'-phosphate
-
contains 1 mol of pyridoxal 5'-phosphate per mol of subunit
pyridoxal 5'-phosphate
-
the enzyme binds 4 pyridoxal 5'-phosphate per tetramer
pyridoxal 5'-phosphate
-
after dialysis for 48 h against buffer containing 1 mM semicarbazide, about 50% loss of activity, full recovery by adding pyridoxal 5'-phosphate. Km: 0.001 mM
pyridoxal 5'-phosphate
-
tightly bound to the apoenzyme. Non-competitive inhibition at high concentrations
pyridoxal 5'-phosphate
-
Km for pyridoxal 5'-phosphate with soluble enzyme: 0.00243 mM. Km for pyridoxal 5'-phosphate with membrane-bound enzyme: 0.00296 mM. Km for pyridoxal 5'-phosphate with solubilized membrane-bound enzyme: 0.00286 mM
pyridoxal 5'-phosphate
-
activates, but does not influence the enzyme expression level
pyridoxal 5'-phosphate
-
activates, but does not influence the enzyme expression level
pyridoxal 5'-phosphate
-
activates, but does not influence the enzyme expression level
pyridoxal 5'-phosphate
dependent on, binding structure involving a Schiff base, overview
pyridoxal 5'-phosphate
dependent on, binding structure involving a Schiff base, overview
pyridoxal 5'-phosphate
dependent on, binding structure involving a Schiff base, overview
pyridoxal 5'-phosphate
dependent on, binding structure involving a Schiff base, overview
pyridoxal 5'-phosphate
dependent on, binding structure involving a Schiff base, overview
pyridoxal 5'-phosphate
dependent on, binding structure involving a Schiff base, overview
pyridoxal 5'-phosphate
dependent on, binding structure involving a Schiff base, overview
pyridoxal 5'-phosphate
dependent on, binding structure involving a Schiff base, overview
pyridoxal 5'-phosphate
dependent on, binding structure involving a Schiff base, overview
pyridoxal 5'-phosphate
dependent on, binding structure involving a Schiff base, overview
pyridoxal 5'-phosphate
dependent on, binding structure involving a Schiff base, overview
pyridoxal 5'-phosphate
dependent on, binding structure involving a Schiff base, overview
pyridoxal 5'-phosphate
dependent on, binding structure involving a Schiff base, overview
pyridoxal 5'-phosphate
dependent on, binding structure involving a Schiff base, overview
pyridoxal 5'-phosphate
dependent on, binding structure involving a Schiff base, overview
pyridoxal 5'-phosphate
dependent on, binding structure involving a Schiff base, overview
pyridoxal 5'-phosphate
dependent on, binding structure involving a Schiff base, overview
pyridoxal 5'-phosphate
cofactor is located in the large domain. The pyridine ring of pyridoxal 5'-phosphate is sandwiched between the methyl group of Ala275 and the imidazole ring of His194
additional information
-
HDC uses a covalently bound pyruvoyl moiety as cofactor
-
additional information
pyruvoyl-residue at the NH2-terminus
-
additional information
pyruvoyl-residue at the NH2-terminus
-
additional information
pyruvoyl-residue at the NH2-terminus
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CaCl2
-
maximal activity is observed only in the presence of high concentrations of various salts: KCl, NaCl, NaBr, K2SO4, CaCl2 or MgCl2
K2SO4
-
maximal activity is observed only in the presence of high concentrations of various salts: KCl, NaCl, NaBr, K2SO4, CaCl2 or MgCl2
KCl
-
maximal activity is observed only in the presence of high concentrations of various salts: KCl, NaCl, NaBr, K2SO4, CaCl2 or MgCl2
MgCl2
-
maximal activity is observed only in the presence of high concentrations of various salts: KCl, NaCl, NaBr, K2SO4, CaCl2 or MgCl2
Mn2+
NaBr
-
maximal activity is observed only in the presence of high concentrations of various salts: KCl, NaCl, NaBr, K2SO4, CaCl2 or MgCl2
NaCl
-
maximal activity is observed only in the presence of high concentrations of various salts: KCl, NaCl, NaBr, K2SO4, CaCl2 or MgCl2
additional information
-
constitutive and inducible enzyme show optimal activity in absence of NaCl
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
epigallocatechin gallate
-
time-dependent inhibition, only under aerobic conditions
methyl L-histidinate
the compound is able to block the reaction at the Michaelis complex step in HDC
pyridoxal 5'-phosphate
-
non-competitive inhibition with respect to His, at high concentrations
pyridoxyl-histidine methyl ester conjugate
structure-based inhibitor, binding structure
rugosin A methyl ester
compound isolated from Filipendula ulmaria, non-competitive
tellimagrandin II
compound isolated from Filipendula ulmaria, non-competitive
alpha-Fluoromethylhistidine
-
the (S)-isomer is a suicide substrate inhibitor, the (R)-isomer is an at least 10times less potent inhibitor
epigallocatechin-3-gallate
EGCG, the inhibitory effect is mediated by blocking the entrance to the catalytic site, therefore, preventing substrate binding
epigallocatechin-3-gallate
-
antiproliferative and antangiogenic component of green tea, 0.1 mM, 67% and 57% inhibition of recombinant and native HDC, respectively
epigallocatechin-3-gallate
-
direct inhibitory effect on both histidine decarboxylase and DOPA decarboxylase. Modeling of binding to the enzymes. The presence of epigallocatechin-3-gallate contiguous to the active site entrance leads to the movement of several residues in the active site. Epigallocatechin-3-gallate occludes the entrance channel to the enzyme active site and establishes new interactions with residues in the active site. These residues turn outward when the active site collapses. After docking of epigallocatechin-3-gallate, neither histidine nor the inhibitors histidine methyl ester and alpha-fluoromethyl histidine are able to bind to the enzyme
NaCl
2 M, 50% residual activity, 4.3 M, residual activity is 80%, 69%, and 38% of that of the enzyme in NaCl-free conditions at pH 5.0, 5.5, 6.0, respectively
additional information
design, synthesis, and test of potentially membrane-permeable pyridoxyl-substrate conjugates as inhibitors for human HDC and modeling of an active site for hHDC, which is compatible with the experimental data, structure-activity relationship, overview
-
additional information
-
design, synthesis, and test of potentially membrane-permeable pyridoxyl-substrate conjugates as inhibitors for human HDC and modeling of an active site for hHDC, which is compatible with the experimental data, structure-activity relationship, overview
-
additional information
-
treatment of mast cells in systemic mastocytosis with pharmacologic inhibitors prednisone, IFNalpha, and 2CdA only slightly inhibit expression of HDC, overview
-
additional information
-
poor inhibition by procatechiuc acid, ferulic acid, chlorogenic acid, and ellagic acid, no inhibition by luteorin, apigenin and rutin
-
additional information
-
1-metylhistidine, L-phenylalanine, L-tryptophan, tert-butyloxycarbonyl-modified ornithine, and tert-butyloxycarbonyl-modified alpha,gamma-diaminobutyric acid do not inhibit human HDC in mast cells and cell extracts significantly
-
additional information
successful strategies to inhibit the decarboxylase have included the synthesis of fluoro-derivatives, which act as competitive and/or suicide inhibitors, as it is the case of alpha-fluoromethylhistidine
-
additional information
-
successful strategies to inhibit the decarboxylase have included the synthesis of fluoro-derivatives, which act as competitive and/or suicide inhibitors, as it is the case of alpha-fluoromethylhistidine
-
additional information
-
histamine causes a decrease in the expression of gene hdc
-
additional information
-
knockdown of the transcription factor C/EBPbeta by dehydroxymethylepoxyquinomicin reduces the HDC expression in lipopolysaccharide-treated cells
-
additional information
-
histamine causes a decrease in the expression of gene hdc
-
additional information
-
histamine causes a decrease in the expression of gene hdc
-
additional information
-
Lac-B (a mixture of freeze-dried Bifidobacterium infantis and Bifidobacterium longum) shows significant anti-allergic effect through suppression of both H1R and HDC gene expression followed by decrease in H1R, HDC protein level, and histamine content, oral administration of the Lac-B suspension significantly suppresses the toluene 2,4-diisocyanate-induced HDC mRNA up-regulation
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
HdcB
-
HdcB catalyses the maturation of pyruvoyl-dependent histidine decarboxylase by cleavage of the proenzyme which results in the formation of the pyruvoyl prosthetic group
-
lipopolysaccharide
-
excreted from Escherichia coli after oral infection, stimulates the enzyme in dental pulp and gingiva, tissue-specific effects, oveview
monosodium urate
monosodium urate crystals injected into the air pouch lead to a highly upregulated mRNA level of HDC
-
SH-groups
-
wild type and mutant enzyme each contain two SH groups per alpha-chain
ethanol
-
does not increase hdc gene expression or activity in cells, but increases HDC activity, 122% activity at 10% ethanol
ethanol
-
does not increase hdc gene expression or activity in cells, but increases HDC activity
ethanol
-
does not increase hdc gene expression or activity in cells, but increases HDC activity
pyridoxal 5'-phosphate
-
activates, but does not influence the enzyme expression level
pyridoxal 5'-phosphate
-
activates, but does not influence the enzyme expression level
pyridoxal 5'-phosphate
-
activates, but does not influence the enzyme expression level
pyruvate
-
pyruvoyl-group is covalently bound to the alpha-subunit and undergoes Schiff base formation with histamine
pyruvate
-
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
pyruvate
-
pyruvoyl-group is covalently bound to the alpha-subunit and undergoes Schiff base formation with histamine
toluene 2,4-diisocyanate
-
toluene 2,4-diisocyanate provocation causes acute allergy-like behaviors along with significant up-regulation of HDC mRNA expression and increased HDC activity
toluene 2,4-diisocyanate
-
toluene 2,4-diisocyanate provocation shows a significant up-regulation of histidine decarboxylase gene expression in rats, prolonged pre-treatment of Sho-seiryu-to significantly suppresses the mRNA level of HDC upregulated by toluene 2,4-diisocyanate
additional information
12-O-tetradecanoylphorbol-13-acetate induces the enzyme
-
additional information
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12-O-tetradecanoylphorbol-13-acetate induces the enzyme
-
additional information
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L-histidine induces the expression of the histidine decarboxylase gene hdc
-
additional information
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tartaric acid, L-lactic acid, and sulfur dioxide have no effect on enzyme synthesis and activity
-
additional information
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intraperitoneal or oral administration of aspirin, dexamethasone or indomethacin elevates histidine decarboxylase activity in the stomach
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additional information
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antigen challenge induces HDC in both mast cell-dependent and mast cell-independent ways at a postanaphylactic time in the liver, lung, spleen, and ears, enzyme activity is increased in atissue-dependent manner after sensitization of wild-type mice by ovalbumin, overview
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additional information
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L-histidine induces the expression of the histidine decarboxylase gene hdc
-
additional information
-
tartaric acid, L-lactic acid, and sulfur dioxide have no effect on enzyme synthesis and activity
-
additional information
-
L-histidine induces the expression of the histidine decarboxylase gene hdc
-
additional information
-
tartaric acid, L-lactic acid, and sulfur dioxide have no effect on enzyme synthesis and activity
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
between pH 6 and pH 9 the Km-value for L-His declines from 1 mM to about 0.01 mM
-
additional information
additional information
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Lineweaver-Burk kinetics
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.01
epicatechin gallate
-
pH 6.8, 37ĆĀ°C, recombinant enzyme, versus L-histidine
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.00000014
-
HDC activity in cultured brain microvascular endothelial cells
147
additional information
additional information
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tissue-specific activity induced by lipopolysaccharide, overview
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5
4.8
6.2
6.5
6.6
6.8
7.2 - 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
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5 - 8.5
5.5 - 8
6 - 7.6
-
pH 6.0: about 50% of maximal activity, pH 7.6: about 40% of maximal activity
7 - 9
5.5 - 8
-
pH 5.5: about 35% of maximal activity, pH 8.0: about 10% of maximal activity, membrane-bound enzyme
5.5 - 8
-
pH 5.5: about 50% of maximal activity, pH 8.0: about 40% of maximal activity, soluble enzyme
7 - 9
-
pH 7.0: about 85% of maximal activity, pH 9.0: about 70% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
28
30
37
40
45
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 50
47 - 60
-
47ĆĀ°C: about 50% of maximal activity, 60ĆĀ°C: about 75% of maximal activity, no activity detectable at 65ĆĀ°C
4 - 50
50% of maximal activity at 50ĆĀ°C, no activity at 60ĆĀ°C
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
33% of the tested strains are positive for histidine decarboxylase
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-
brenda
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-
-
brenda
strain C57BL/6 resistant to infection by Leishmania major, and strain BALB/c susceptible to infection with Leishmania major
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-
brenda
wild-type BALB/c mice, mast cell-deficient W/W v mice, and IL-1-KO BALB/c mice, deficient in both Iinterleukin-1alpha and interleukin-1beta
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-
brenda
two histidine decarboxylases: a constitutive and an inducible enzyme
-
-
brenda
-
4142, 4144, 4145, 4149, 4160, 4161, 4162, 649295, 650807, 651162, 651497, 652502, 653860, 653861, 663930, 663937, 665184, 666896
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
the posterodorsal medial amygdala has high levels of histidine decarboxylase
brenda
-
HDC expression is significantly increased in carcinoma cells
brenda
-
in the acute phase of infection of mice infected with Leishmania major, detected in both strains the resistant C57BL/6 and the susceptible BALB/c. Only susceptible mice known to be unable to control parasite dissemination show induction of histidine decarboxylase in their distant periaortic lymph nodes as well. During the chronic phase of infection only the heavily parasitized organs of BALB/c mice show high expression of histidine decarboxylase gene
brenda
human oxyntic mucosa contains four major types of neuroendocrine cells: ECL, ghrelin, serotonin and somatostatin cells
brenda
-
histidine decarboxylase is induced upon infiltration of polymorphonuclear leukocytes into mouse peritoneal cavity. Histamine is synthesized by the enzyme attached to the granule membrane of polymorphonuclear leukocytes
brenda
additional information
in the tuberomammillary nucleus of the posterior hypothalamus
brenda
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of osteoarthritic cartilage. Histidine decarboxylase is localized within chondrocytes of the superficial layer of nearly all the osteoarthritis specimen examined, with little or no immunostaining in the intermediate or deep zones. Production of histamine and histidine decarboxylase in specimen of osteoarthritic cartilage respresents three grades of clinical severity
brenda
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high levels of HDC protein are also found in the striatum
brenda
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high levels of HDC protein are also found in the striatum
brenda
the tumours are classified based on clinico-pathological criteria
brenda
highly expressed in the hypothalamic infundibulum, the cells containing HDC mRNA are localized in the medial mammillary nucleus of the hypothalamic infundibulum
brenda