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1-methyl-DL-histidine
1-methylhistamine + CO2
1-Methylhistidine
1-Methylhistamine
-
very poor substrate
-
-
?
2-Thiolhistidine
1-Thiolhistamine
-
very poor substrate
-
-
?
3,4-Dihydroxyphenylalanine
Dopamine + CO2
no substrate for wild-type. Mutant S354G acquires the ability to decarboxylate 3,4-dihydroxyphenylalanine
-
-
?
3-Methylhistidine
2-Methylhistamine
-
very poor substrate
-
-
?
beta-(1,2,4-Triazole-3)-Ala
?
-
very poor substrate
-
-
?
beta-(Thiazole-2)-Ala
?
-
very poor substrate
-
-
?
L-histidin
histamine + CO2
-
-
-
?
L-histidine
histamine + CO2
additional information
?
-
1-methyl-DL-histidine
1-methylhistamine + CO2
-
-
-
-
?
1-methyl-DL-histidine
1-methylhistamine + CO2
-
-
-
-
?
beta-(Pyridyl-2)-Ala
?
-
very poor substrate
-
-
?
beta-(Pyridyl-2)-Ala
?
-
-
-
-
?
beta-(Pyridyl-2)-Ala
?
-
-
-
-
?
L-His
Histamine + CO2
-
-
-
?
L-His
Histamine + CO2
-
-
-
?
L-His
Histamine + CO2
-
-
-
?
L-His
Histamine + CO2
-
-
-
?
L-His
Histamine + CO2
-
-
-
?
L-His
Histamine + CO2
-
-
-
?
L-His
Histamine + CO2
-
-
-
?
L-His
Histamine + CO2
-
-
-
?
L-His
Histamine + CO2
-
-
-
?
L-His
Histamine + CO2
-
-
-
?
L-His
Histamine + CO2
-
-
-
?
L-His
Histamine + CO2
-
-
-
?
L-His
Histamine + CO2
-
-
-
?
L-His
Histamine + CO2
-
-
-
?
L-His
Histamine + CO2
-
-
-
?
L-His
Histamine + CO2
-
-
-
?
L-His
Histamine + CO2
-
-
-
?
L-His
Histamine + CO2
-
-
-
?
L-His
Histamine + CO2
-
-
-
?
L-His
Histamine + CO2
-
-
-
?
L-His
Histamine + CO2
-
-
-
?
L-His
Histamine + CO2
-
-
-
?
L-His
Histamine + CO2
-
-
-
?
L-His
Histamine + CO2
-
-
-
?
L-His
Histamine + CO2
-
-
-
?
L-His
Histamine + CO2
-
-
-
?
L-His
Histamine + CO2
-
-
-
?
L-His
Histamine + CO2
-
-
-
?
L-His
Histamine + CO2
-
-
-
?
L-His
Histamine + CO2
-
-
-
?
L-His
Histamine + CO2
-
-
-
?
L-His
Histamine + CO2
-
-
-
?
L-His
Histamine + CO2
-
-
-
?
L-His
Histamine + CO2
-
-
-
?
L-His
Histamine + CO2
-
-
-
?
L-His
Histamine + CO2
-
-
-
?
L-His
Histamine + CO2
-
-
-
?
L-His
Histamine + CO2
-
-
-
?
L-His
Histamine + CO2
-
-
-
?
L-His
Histamine + CO2
-
-
-
?
L-His
Histamine + CO2
-
-
-
?
L-His
Histamine + CO2
-
-
-
?
L-His
Histamine + CO2
-
-
-
?
L-His
Histamine + CO2
-
-
-
?
L-His
Histamine + CO2
-
-
-
?
L-His
Histamine + CO2
-
strictly specific for L-His
-
?
L-histidine
histamine + CO2
-
-
-
?
L-histidine
histamine + CO2
structure-function relationship, molecular modeling, overview
-
-
?
L-histidine
histamine + CO2
-
-
-
?
L-histidine
histamine + CO2
structure-function relationship, molecular modeling, overview
-
-
?
L-histidine
histamine + CO2
-
-
-
?
L-histidine
histamine + CO2
structure-function relationship, molecular modeling, overview
-
-
?
L-histidine
histamine + CO2
-
-
-
-
?
L-histidine
histamine + CO2
-
-
-
?
L-histidine
histamine + CO2
structure-function relationship, molecular modeling, overview
-
-
?
L-histidine
histamine + CO2
-
-
?
L-histidine
histamine + CO2
-
-
?
L-histidine
histamine + CO2
-
-
-
?
L-histidine
histamine + CO2
-
-
-
?
L-histidine
histamine + CO2
structure-function relationship, molecular modeling, overview
-
-
?
L-histidine
histamine + CO2
-
-
-
-
?
L-histidine
histamine + CO2
-
-
-
?
L-histidine
histamine + CO2
-
-
-
-
?
L-histidine
histamine + CO2
-
-
-
?
L-histidine
histamine + CO2
-
-
-
-
?
L-histidine
histamine + CO2
-
-
-
?
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
-
-
?
L-histidine
histamine + CO2
structure-function relationship, molecular modeling, overview
-
-
?
L-histidine
histamine + CO2
-
substrate-specific
-
-
?
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
-
-
-
-
?
L-histidine
histamine + CO2
-
-
-
?
L-histidine
histamine + CO2
-
-
-
-
?
L-histidine
histamine + CO2
structure-function relationship, molecular modeling, overview
-
-
?
L-histidine
histamine + CO2
-
-
-
-
?
L-histidine
histamine + CO2
-
-
-
?
L-histidine
histamine + CO2
-
-
?
L-histidine
histamine + CO2
-
-
-
?
L-histidine
histamine + CO2
-
-
-
?
L-histidine
histamine + CO2
-
-
-
-
?
L-histidine
histamine + CO2
-
-
-
?
L-histidine
histamine + CO2
-
expression of hdc is also mediated by the bacterial growth phase, overview
-
-
?
L-histidine
histamine + CO2
-
-
-
-
?
L-histidine
histamine + CO2
-
expression of hdc is also mediated by the bacterial growth phase, overview
-
-
?
L-histidine
histamine + CO2
-
-
-
?
L-histidine
histamine + CO2
-
-
-
?
L-histidine
histamine + CO2
structure-function relationship, molecular modeling, overview
-
-
?
L-histidine
histamine + CO2
-
-
?
L-histidine
histamine + CO2
-
-
-
?
L-histidine
histamine + CO2
-
-
-
-
?
L-histidine
histamine + CO2
-
-
-
?
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
-
-
-
?
L-histidine
histamine + CO2
-
-
-
?
L-histidine
histamine + CO2
-
-
-
?
L-histidine
histamine + CO2
-
-
-
?
L-histidine
histamine + CO2
-
-
677857, 680148, 680165, 680763, 690778, 692084, 692606, 693426, 693469, 716351, 716876 -
-
?
L-histidine
histamine + CO2
-
-
-
?
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
-
-
-
?
L-histidine
histamine + CO2
-
-
-
-
?
L-histidine
histamine + CO2
-
HDC is the rate-limiting enzyme for histamine synthesis
-
-
?
L-histidine
histamine + CO2
-
-
-
-
?
L-histidine
histamine + CO2
-
-
-
?
L-histidine
histamine + CO2
-
expression of hdc is also mediated by the bacterial growth phase, overview
-
-
?
L-histidine
histamine + CO2
-
-
-
-
?
L-histidine
histamine + CO2
-
expression of hdc is also mediated by the bacterial growth phase, overview
-
-
?
L-histidine
histamine + CO2
-
-
-
?
L-histidine
histamine + CO2
-
-
-
?
L-histidine
histamine + CO2
structure-function relationship, molecular modeling, overview
-
-
?
L-histidine
histamine + CO2
-
-
-
-
?
L-histidine
histamine + CO2
-
expression of hdc is also mediated by the bacterial growth phase, overview
-
-
?
L-histidine
histamine + CO2
-
-
-
-
?
L-histidine
histamine + CO2
-
expression of hdc is also mediated by the bacterial growth phase, overview
-
-
?
L-histidine
histamine + CO2
-
-
?
L-histidine
histamine + CO2
-
-
-
?
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
-
-
-
?
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
-
-
-
?
L-histidine
histamine + CO2
-
-
?
L-histidine
histamine + CO2
-
-
-
?
L-histidine
histamine + CO2
-
-
-
?
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
-
-
?
L-histidine
histamine + CO2
-
-
-
?
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
-
-
-
?
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
-
-
?
L-histidine
histamine + CO2
-
-
?
L-histidine
histamine + CO2
-
-
-
?
L-histidine
histamine + CO2
structure-function relationship, molecular modeling, overview
-
-
?
L-histidine
histamine + CO2
-
-
-
-
?
L-histidine
histamine + CO2
-
-
?
L-histidine
histamine + CO2
-
-
-
?
L-histidine
histamine + CO2
-
-
-
-
?
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 5-phosphate-dependent L-amino acid decarboxylase, L-aaDCII
-
-
?
L-histidine
histamine + CO2
-
-
?
L-histidine
histamine + CO2
-
-
-
?
L-histidine
histamine + CO2
-
-
-
?
L-histidine
histamine + CO2
-
-
-
?
L-histidine
histamine + CO2
-
-
-
?
L-histidine
histamine + CO2
-
-
-
?
L-histidine
histamine + CO2
-
-
-
?
L-histidine
histamine + CO2
-
-
690319, 691549, 691707, 692565, 693044, 693822, 693827, 693829, 694385, 694402, 715728, 716351 -
-
?
L-histidine
histamine + CO2
-
-
-
?
L-histidine
histamine + CO2
structure-function relationship, molecular modeling, overview
-
-
?
L-histidine
histamine + CO2
-
-
-
?
L-histidine
histamine + CO2
-
-
-
?
L-histidine
histamine + CO2
structure-function relationship, molecular modeling, overview
-
-
?
L-histidine
histamine + CO2
-
-
-
?
L-histidine
histamine + CO2
-
-
-
?
L-histidine
histamine + CO2
-
-
-
?
L-histidine
histamine + CO2
-
-
-
?
L-histidine
histamine + CO2
-
-
-
-
?
L-histidine
histamine + CO2
-
-
-
?
L-histidine
histamine + CO2
-
-
-
?
L-histidine
histamine + CO2
-
-
-
?
L-histidine
histamine + CO2
-
-
-
?
L-histidine
histamine + CO2
-
-
-
?
L-histidine
histamine + CO2
-
-
-
?
L-histidine
histamine + CO2
-
-
-
?
L-histidine
histamine + CO2
structure-function relationship, molecular modeling, overview
-
-
?
Npi-Methylhistidine
?
-
-
-
-
?
Npi-Methylhistidine
?
-
-
-
-
?
additional information
?
-
-
induction by phorbol myristate acetate
-
-
?
additional information
?
-
enzyme immunoassay for detection of histamine production
-
-
?
additional information
?
-
-
enzyme immunoassay for detection of histamine production
-
-
?
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
-
-
?
additional information
?
-
no substrates: lysine, arginine, tyrosine, tryptophan or ornithine
-
-
?
additional information
?
-
no substrates: lysine, arginine, tyrosine, tryptophan or ornithine
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
L-histidin
histamine + CO2
-
-
-
?
L-histidine
histamine + CO2
additional information
?
-
L-histidine
histamine + CO2
-
-
-
?
L-histidine
histamine + CO2
-
-
-
?
L-histidine
histamine + CO2
-
-
-
?
L-histidine
histamine + CO2
-
-
-
?
L-histidine
histamine + CO2
-
-
?
L-histidine
histamine + CO2
-
-
?
L-histidine
histamine + CO2
-
-
-
?
L-histidine
histamine + CO2
-
-
-
?
L-histidine
histamine + CO2
-
-
-
-
?
L-histidine
histamine + CO2
-
-
-
?
L-histidine
histamine + CO2
-
-
-
-
?
L-histidine
histamine + CO2
-
-
-
?
L-histidine
histamine + CO2
-
-
-
-
?
L-histidine
histamine + CO2
-
-
-
?
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
-
-
?
L-histidine
histamine + CO2
-
-
-
-
?
L-histidine
histamine + CO2
-
-
-
?
L-histidine
histamine + CO2
-
-
-
-
?
L-histidine
histamine + CO2
-
-
-
-
?
L-histidine
histamine + CO2
-
-
-
?
L-histidine
histamine + CO2
-
-
?
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
-
-
-
?
L-histidine
histamine + CO2
-
-
?
L-histidine
histamine + CO2
-
-
-
?
L-histidine
histamine + CO2
-
-
-
-
?
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
-
-
?
L-histidine
histamine + CO2
-
-
-
?
L-histidine
histamine + CO2
-
-
-
?
L-histidine
histamine + CO2
-
-
-
?
L-histidine
histamine + CO2
-
-
-
?
L-histidine
histamine + CO2
-
-
-
-
?
L-histidine
histamine + CO2
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
?
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
-
-
-
?
L-histidine
histamine + CO2
-
-
?
L-histidine
histamine + CO2
-
-
-
?
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
-
-
?
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
-
-
?
L-histidine
histamine + CO2
-
-
?
L-histidine
histamine + CO2
-
-
-
?
L-histidine
histamine + CO2
-
-
?
L-histidine
histamine + CO2
-
-
-
?
L-histidine
histamine + CO2
-
-
-
-
?
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
-
-
?
L-histidine
histamine + CO2
-
-
-
?
L-histidine
histamine + CO2
-
-
-
?
L-histidine
histamine + CO2
-
-
-
?
L-histidine
histamine + CO2
-
-
-
?
L-histidine
histamine + CO2
-
-
-
?
L-histidine
histamine + CO2
-
-
-
?
L-histidine
histamine + CO2
-
-
-
?
L-histidine
histamine + CO2
-
-
-
?
L-histidine
histamine + CO2
-
-
-
?
L-histidine
histamine + CO2
-
-
-
?
L-histidine
histamine + CO2
-
-
-
?
L-histidine
histamine + CO2
-
-
-
?
additional information
?
-
-
induction by phorbol myristate acetate
-
-
?
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Pyruvoyl group
-
dependent on
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
650807, 651162, 690319, 691549, 692565, 693044, 693822, 693829, 694385, 694402, 715728
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
required
pyridoxal 5'-phosphate
-
required
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
-
dependent on
pyridoxal 5'-phosphate
-
dependent on
pyridoxal 5'-phosphate
dependent on
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
-
additional information
-
pyruvoyl-residue at the NH2-terminus
-
additional information
pyruvoyl-residue at the NH2-terminus
-
additional information
-
pyruvoyl-residue at the NH2-terminus
-
additional information
pyruvoyl-residue at the NH2-terminus
-
additional information
pyruvoyl-residue at the NH2-terminus
-
additional information
-
pyruvoyl-residue at the NH2-terminus
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ca2+
-
activates by 17.20%
CaCl2
-
maximal activity is observed only in the presence of high concentrations of various salts: KCl, NaCl, NaBr, K2SO4, CaCl2 or MgCl2
Fe3+
-
0.1 mM, enhances activity by 7-8%
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
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
Mn2+
-
activates by 23.42%
Mn2+
-
0.1 mM, enhances activity by 7-8%
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(-)-epigallocatechin 3-gallate
-
-
(S)-alpha-fluoromethylhistidine
-
0.001 mM, complete inhibition
2-Hydrazino-3-(4-imidazolyl)propionic acid
-
-
2-Hydroxy-5-nitrobenzylbromide
-
-
4(5)-aminooxymethylimidazole
O-IMHA, a substrate analogue
4-coumaric acid
-
slight inhibition
5,5'-dithiobis(2-nitrobenzoate)
-
-
alpha-Fluoromethylhistidine
caffeic acid
-
slight inhibition
Co2+
-
0.1 mM, 20% decrease of activity
Cu2+
-
0.1 mM, strong inhibition
curcumin
-
slight inhibition
epicatechin gallate
-
competitive versus L-histidine
epigallocatechin gallate
-
time-dependent inhibition, only under aerobic conditions
epigallocatechin-3-gallate
epsilon-N-Pyridoxyllysine
-
-
gallic acid
-
slight inhibition
Hg2+
-
0.1 mM, strong inhibition
kaempferol
-
slight inhibition
KCl
-
50% inhibition at 1.5 M
L-Citric acid
-
19% hdc gene expression at 0.8 g/l
L-Fructose
-
46% hdc gene expression at 50 g/l
L-Glucose
-
22% hdc gene expression at 50 g/l
L-Histidine ethyl ester
-
-
L-histidine methyl ester
-
-
L-Malic acid
-
26% hdc gene expression at 4 g/l
methyl L-histidinate
the compound is able to block the reaction at the Michaelis complex step in HDC
methylgallate
-
slight inhibition
N-pyridoxyl-L-histidine methyl ester
-
60% inhibition at 0.2 mM
Ni2+
-
0.1 mM, 15% decrease of activity
p-hydroxymercuribenzoate
-
-
phlorizin
-
slight inhibition
pyridoxal 5'-phosphate
-
non-competitive inhibition with respect to His, at high concentrations
pyridoxyl-histidine methyl ester conjugate
structure-based inhibitor, binding structure
quercetin
-
slight inhibition
rugosin A
compound isolated from Filipendula ulmaria, non-competitive
rugosin A methyl ester
compound isolated from Filipendula ulmaria, non-competitive
rugosin D
compound isolated from Filipendula ulmaria, non-competitive
Sinapic acid
-
slight inhibition
tellimagrandin II
compound isolated from Filipendula ulmaria, non-competitive
alpha-Fluoromethylhistidine
-
-
alpha-Fluoromethylhistidine
-
alpha-FMH, specific inhibitor of HDC
alpha-Fluoromethylhistidine
-
-
alpha-Fluoromethylhistidine
-
alpha-Fluoromethylhistidine
-
-
alpha-Fluoromethylhistidine
-
irreversible
alpha-Fluoromethylhistidine
-
-
alpha-Fluoromethylhistidine
-
-
alpha-Fluoromethylhistidine
-
-
alpha-Fluoromethylhistidine
-
-
alpha-Fluoromethylhistidine
-
the (S)-isomer is a suicide substrate inhibitor, the (R)-isomer is an at least 10times less potent inhibitor
alpha-Fluoromethylhistidine
-
-
alpha-Fluoromethylhistidine
-
irreversible inhibitor
alpha-Methylhistidine
-
-
alpha-Methylhistidine
-
-
alpha-Methylhistidine
-
-
carnosine
-
-
Citric acid
-
diminishes hdc gene expression
Citric acid
-
diminishes hdc gene expression
CoCl2
-
-
Cyanoborohydride
-
NaCNBH3
D-fructose
-
diminishes hdc gene expression
D-fructose
-
diminishes hdc gene expression
D-glucose
-
diminishes hdc gene expression
D-glucose
-
diminishes hdc gene expression
dithiothreitol
-
-
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
histamine
-
-
histamine
-
at high concentrations
Histidine methyl ester
mixed-type inhibition
Histidine methyl ester
-
-
Histidine methyl ester
-
-
Histidine methyl ester
-
-
Hydrazine sulfate
-
-
imidazole
-
-
imidazole
-
competitively inhibited
malic acid
-
diminishes hdc gene expression
malic acid
-
diminishes hdc gene expression
NaCl
-
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
NaCl
-
50% inhibition at 1.5 M
NiCl2
-
-
Shoyuflavones
-
isolated from soy sauce
Shoyuflavones
-
isolated from soy sauce
Urocanic acid
-
-
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
-
additional information
not inhibitory: NaCl up to 5%
-
additional information
-
not inhibitory: NaCl up to 5%
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Butyrate
-
highly activating for the wild-type enzyme
C/EBPbeta
-
essential for the HDC induction
-
gastrin
-
increase of steady-state levels of 6 HDC isoforms
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
-
contains a pyruvoyl group at the active centre
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
-
12-O-tetradecanoylphorbol-13-acetate induces the enzyme
-
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
-
additional information
-
intraperitoneal or oral administration of aspirin, dexamethasone or indomethacin elevates histidine decarboxylase activity in the stomach
-
additional information
-
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
-
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
-
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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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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-
TREMBL
brenda
-
TREMBL
brenda
33% of the tested strains are positive for histidine decarboxylase
-
-
brenda
-
-
-
brenda
-
TREMBL
brenda
-
-
-
brenda
-
SwissProt
brenda
-
SwissProt
brenda
-
SwissProt
brenda
-
UniProt
brenda
-
TREMBL
brenda
-
-
-
brenda
fragment
UniProt
brenda
fragment
UniProt
brenda
-
-
-
brenda
strain 0006
UniProt
brenda
-
-
-
brenda
i.e. Mesorhizobium loti
SwissProt
brenda
-
-
-
brenda
-
-
-
brenda
strain JCM1672T
SwissProt
brenda
-
UniProt
brenda
BDF1 mice
-
-
brenda
no activity in Buttiauxella sp.
-
-
-
brenda
no activity in Cedecea sp.
-
-
-
brenda
no activity in Citrobacter amalonaticus
-
-
-
brenda
no activity in Citrobacter farmeri
-
-
-
brenda
no activity in Citrobacter koseri
-
-
-
brenda
no activity in Citrobacter sedlakii
-
-
-
brenda
no activity in Edwardsiella tarda
-
-
-
brenda
no activity in Enterobacter cloacae
-
-
-
brenda
no activity in Escherichia coli
-
-
-
brenda
no activity in Ewingella americana
-
-
-
brenda
no activity in Hafnia alvei
-
-
-
brenda
no activity in Klebsiella oxytoca
-
-
-
brenda
no activity in Klebsiella pneumoniae
-
-
-
brenda
no activity in Kluyvera sp.
-
-
-
brenda
no activity in Leclercia adecarboxylata
-
-
-
brenda
no activity in Leminorella sp.
-
-
-
brenda
no activity in Moellerella wisconsensis
-
-
-
brenda
no activity in Pantoea sp.
-
-
-
brenda
no activity in Proteus mirabilis
-
-
-
brenda
no activity in Proteus penneri
-
-
-
brenda
no activity in Proteus vulgaris
-
-
-
brenda
no activity in Providencia sp.
-
-
-
brenda
no activity in Rahnella aquatilis
-
-
-
brenda
no activity in Raoultella terrigena
-
-
-
brenda
no activity in Salmonella sp.
-
-
-
brenda
no activity in Serratia marcescens
-
-
-
brenda
no activity in Shigella sp.
-
-
-
brenda
no activity in Yersinia enterocolitica
-
-
-
brenda
no activity in Yersinia pseudotuberculosis
-
-
-
brenda
-
-
-
brenda
ssp. japonica
TREMBL
brenda
gene hdc
UniProt
brenda
i.e. Listonella damsela
UniProt
brenda
-
SwissProt
brenda
gene hdc
UniProt
brenda
gene hdc
UniProt
brenda
-
SwissProt
brenda
-
SwissProt
brenda
-
SwissProt
brenda
-
-
-
brenda
-
SwissProt
brenda
-
TREMBL
brenda
-
SwissProt
brenda
-
UniProt
brenda
-
UniProt
brenda
-
UniProt
brenda
-
UniProt
brenda
-
UniProt
brenda
-
UniProt
brenda
-
UniProt
brenda
strain JCM10006
UniProt
brenda
JCM 10006T
-
-
brenda
-
-
-
brenda
-
SwissProt
brenda
-
-
-
brenda
-
SwissProt
brenda
-
-
-
brenda
-
SwissProt
brenda
-
-
-
brenda
-
SwissProt
brenda
-
-
-
brenda
all strains are positive for histidine decarboxylase
-
-
brenda
i.e. Aerobacter aerogenes
SwissProt
brenda
i.e. Klebsiella aerogenes
SwissProt
brenda
-
-
-
brenda
30a
Uniprot
brenda
30a
-
-
brenda
wild-type and and mutant enzyme
-
-
brenda
wilde-type and mutant enzyme
-
-
brenda
-
-
-
brenda
isolated from wine, gene hdc
-
-
brenda
strain 0006
UniProt
brenda
-
-
-
brenda
isolated from wine, gene hdc
-
-
brenda
-
-
-
brenda
all strains examined are positive
-
-
brenda
i.e. Proteus morganii
SwissProt
brenda
i.e. Proteus morganii, strain JCM 1672
UniProt
brenda
strain JCM1672T
SwissProt
brenda
-
4142, 4151, 4155, 4156, 4158, 4163, 651193, 651196, 651498, 652237, 664842, 665186, 680148 -
-
brenda
-
TREMBL
brenda
-
UniProt
brenda
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UniProt
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BDF1 mice
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male BALB/c mice
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strain C57BL/6 resistant to infection by Leishmania major, and strain BALB/c susceptible to infection with Leishmania major
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virgin female
UniProt
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
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brenda
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UniProt
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isolated from wine, gene hdc
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isolated from wine, gene hdc
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-
brenda
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brenda
-
UniProt
brenda
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brenda
isolated from wine, gene hdc
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isolated from wine, gene hdc
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-
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gene hdc
UniProt
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strain ATCC 33539T
SwissProt
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-
SwissProt
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TREMBL
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gene hdc
UniProt
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two histidine decarboxylases: a constitutive and an inducible enzyme
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brenda
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SwissProt
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-
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14% of the strains are positive for histidine decarboxylase
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-
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i.e. Klebsiella planticola
SwissProt
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i.e. Raoultella planticola
SwissProt
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strain ATCC 43176
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brenda
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4142, 4144, 4145, 4149, 4160, 4161, 4162, 649295, 650807, 651162, 651497, 652502, 653860, 653861, 663930, 663937, 665184, 666896 -
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brenda
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TREMBL
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-
690319, 691549, 691707, 692565, 693044, 693822, 693827, 693829, 694385, 694402, 715728, 716351, 726888, 728029 -
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brenda
-
TREMBL
brenda
3 enzyme forms: 1, 2, and 3
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-
brenda
-
UniProt
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CHCC1524
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-
brenda
JCM 10006T
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-
brenda
strain JCM10006
UniProt
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gene JM31; i.e. Listonella anguillarum, gene JM31
TREMBL
brenda
i.e. Listonella anguillarum
SwissProt
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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brenda
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-
brenda
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the posterodorsal medial amygdala has high levels of histidine decarboxylase
brenda
-
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brenda
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brenda
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-
brenda
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brenda
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brenda
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in basophilic leukemia
brenda
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-
brenda
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HDC expression is significantly increased in carcinoma cells
brenda
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brenda
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brenda
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brenda
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brenda
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brenda
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brenda
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brenda
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CD34+
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-
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terminal
brenda
-
-
brenda
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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
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brenda
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immature, low expression level in basophilic leukemia
brenda
-
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brenda
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brenda
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brenda
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brenda
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brenda
human oxyntic mucosa contains four major types of neuroendocrine cells: ECL, ghrelin, serotonin and somatostatin cells
brenda
-
-
brenda
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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
-
-
brenda
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brenda
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brenda
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brenda
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brenda
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from patients with mastocytosis
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-
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in the tuberomammillary nucleus of the posterior hypothalamus
brenda
substancia nigra and hypothalamus
brenda
-
-
brenda
-
-
brenda
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brenda
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the enzyme is not expressed after ischemic infarct
brenda
-
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brenda
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brenda
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-
brenda
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brenda
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brenda
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of osteoarthritic cartilage
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
sigmoid and transverse
brenda
-
-
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
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brenda
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ear skin
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brenda
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brenda
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brenda
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brenda
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brenda
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brenda
the tumours are classified based on clinico-pathological criteria
brenda
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brenda
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brenda
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brenda
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brenda
highly expressed in the hypothalamic infundibulum, the cells containing HDC mRNA are localized in the medial mammillary nucleus of the hypothalamic infundibulum
brenda
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brenda
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HDC mRNA is highly expressed in the posterior hypothalamus
brenda
-
brenda
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tuberomammillary nucleus of the hypothalamus
brenda
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HDC mRNA is highly expressed in the posterior hypothalamus
brenda
-
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brenda
epidermal, three-dimensional keratinocyte culture
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two-dimensional culture
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cortex
brenda
-
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brenda
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hypertrophic and hyperplastic, Increase in histidine decarboxylase activity in regenerative growth of renal epithelium can result from activation of translation or increased half-life, i.e. slower degradation of the enzyme protein, or both
brenda
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-
brenda
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brenda
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fetal
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brenda
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brenda
pregnancy associated elevation of histidine decarboxylase activity is successfully affected by enzyme antisense oligonucleotide treatment, inducing short-term histamine deficiency
brenda
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brenda
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brenda
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brenda
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neoplastic mast cells in patients with systemic mastocytosis, including MC leukemia and MC sarcoma, expression in mast cells of different maturation stage, immunohistochemic detection and quantitative expression analysis
brenda
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during the chronic phase of infection elevated levels of histidine decarboxylase, possibly of mast cell origin, are associated with Th2-dominated responses and serious disease development
brenda
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brenda
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P-815 cells
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histaminergic
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neurons of the tuberomammillary nucleus of the posterior hypothalamus
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neurons of the tuberomammillary nucleus of the posterior hypothalamus
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peritoneal cavity
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peritoneal cavity
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brenda
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brenda
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brenda
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-
brenda
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differential activity of HDC in normal and pre-eclamptic placentae, overview
brenda
quadriceps femoris
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quadriceps femoris
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masseter, pectoralis, and quadriceps femoris, in cells in the endomysium and around blood vessels, and also in some muscle fibers
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masseter, pectoralis, and quadriceps femoris, in cells in the endomysium and around blood vessels, and also in some muscle fibers
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atopic
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ear skin
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HDC expression regulation in histamine producing gastric cells
brenda
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in enterochromaffin-like cell, not in G cells
brenda
additional information
histidine decarboxylase (HDC) expression in healthy and neoplastic gastric neuroendocrine cells in relationship to the main histamine metabolite, immunoreactive localization study, overview
brenda
additional information
-
histidine decarboxylase (HDC) expression in healthy and neoplastic gastric neuroendocrine cells in relationship to the main histamine metabolite, immunoreactive localization study, overview
brenda
additional information
human HDC expression is mainly detected in hypothalamus, lung and stomach in comparison with the rest of the tissues
brenda
additional information
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human HDC expression is mainly detected in hypothalamus, lung and stomach in comparison with the rest of the tissues
brenda
additional information
keratinocytes express abundant HDC protein, and the levels increase in atopic skin
brenda
additional information
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keratinocytes express abundant HDC protein, and the levels increase in atopic skin
brenda
additional information
immunostaining of HDC in murine skeletal muscle tissues, overview
brenda
additional information
-
immunostaining of HDC in murine skeletal muscle tissues, overview
-
brenda
additional information
immunolocalization of histamine, with rabbit anti-L-histidine decarboxylase (HDC) antiserum, within the tuberomammillary nucleus is validated using carbodiimide. Rapid eye movement sleep deprivation (REM-SD) increases immunoreactive L-histidine decarboxylase by day 5, and it remains elevated in both dorsal and ventral aspects of the tuberomammillary complex
brenda
additional information
-
immunolocalization of histamine, with rabbit anti-L-histidine decarboxylase (HDC) antiserum, within the tuberomammillary nucleus is validated using carbodiimide. Rapid eye movement sleep deprivation (REM-SD) increases immunoreactive L-histidine decarboxylase by day 5, and it remains elevated in both dorsal and ventral aspects of the tuberomammillary complex
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brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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evolution
the enzyme belongs to the family of pyridoxal 5'-phosphate-dependent decarboxylases
malfunction
filaggrin expression in cultured keratinocytes increased following histamine depletion. Histidine decarboxylase expression is increased in the epidermis of patients with eczema
malfunction
truncated forms of the enzyme are related to the Gilles de la Tourette syndrome, phenotype MIM number 137580. Single nucleotide polymorphisms are related to nicotine dependence and other additive behaviors. Gene-disease associations and common pathologies, detailed overview
metabolism
L-histidine decarboxylase is the rate-limiting enzyme for histamine biosynthesis
metabolism
-
L-histidine decarboxylase is the rate-limiting enzyme for histamine biosynthesis
-
physiological function
-
the enzyme and its product, histamine, are involved in multiple inflammatory diseases, atherosclerosis, some neurological and neuroendocrine diseases, osteroporosis, fertility, and several types of neoplasia
physiological function
human oxyntic mucosa contains four major types of neuroendocrine cells (ECL, ghrelin, serotonin and somatostatin cells). ECL cells are the most abundant type, and they produce histamine. The histamine-synthesizing ability of ECL cells is based on cytosolic HDC. Histamine might be transported by VMAT-2 into the secretory vesicles
physiological function
L-histidine decarboxylase (HDC) is the enzyme responsible for histamine biosynthesis in tuberomammillary nucleus (TMN) neurons of the posterior hypothalamus, the rate-limiting enzyme for histamine biosynthesis might be upregulated during chronic rapid eye movement sleep deprivation (REM-SD) because histamine plays a major role in maintaining wakefulness. Upregulation of L-HDC within the tuberomammillary complex during chronic REM-SD is responsible for maintaining wakefulness. Chronic loss of sleep causes the rat to manifest a number of pathologies or syndromes
physiological function
lipopolysaccharide, house dust mite (HDM) extract, and cytokines, which are implicated in allergic inflammation, promote the expression of the enzyme and upregulate histamine levels in keratinocytes. Actively produced histamine influences keratinocyte differentiation, suggesting functional relevance of the axis to atopic dermatitis. HDC expression in keratinocytes is increased in atopic dermatitis
physiological function
neuronal histamine exerts anorexigenic effects in chicks
physiological function
the enzyme is responsible for the biosynthesis of histamine. It is involved in common physiological functions, such as neurotransmission, gastrointestinal track function, immunity, cell growth and cell differentiation. Tissue-specific and time-specific transcriptional HDC regulation must exist, as it behaves as an inducible gene expressed in a very reduced set of cell types. The complexity of HDC expression regulatory mechanisms is also increased by the fact that the enzyme needs to be activated by proteolytic processing and posttranscriptional regulatory mechanisms at the level the enzyme turnover level cannot be discarded. Memory seems to be an important physiological function involving histamine, dopamine, and serotonin
physiological function
-
L-histidine decarboxylase (HDC) is the enzyme responsible for histamine biosynthesis in tuberomammillary nucleus (TMN) neurons of the posterior hypothalamus, the rate-limiting enzyme for histamine biosynthesis might be upregulated during chronic rapid eye movement sleep deprivation (REM-SD) because histamine plays a major role in maintaining wakefulness. Upregulation of L-HDC within the tuberomammillary complex during chronic REM-SD is responsible for maintaining wakefulness. Chronic loss of sleep causes the rat to manifest a number of pathologies or syndromes
-
additional information
active site residues of the dimeric enzyme are Tyr334B, Asp273A, Lys305A, and Ser354B, which are involved in catalysis
additional information
structural and functional analogies and differences between histidine decarboxylase and aromatic L-amino acid decarboxylase (EC 4.1.1.28) molecular networks, overview. Human histidine decarboxylase (HDC) and dopa decarboxylase (DDC) are highly homologous enzymes responsible for the synthesis of biogenic amines (BA) like histamine, and serotonin and dopamine, respectively
additional information
-
structural and functional analogies and differences between histidine decarboxylase and aromatic L-amino acid decarboxylase (EC 4.1.1.28) molecular networks, overview. Human histidine decarboxylase (HDC) and dopa decarboxylase (DDC) are highly homologous enzymes responsible for the synthesis of biogenic amines (BA) like histamine, and serotonin and dopamine, respectively
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12000
-
1 * 24000 + 1 * 12000, mature enzyme, SDS-PAGE
13400
-
alpha6beta6, 6 * 28800 + 6 * 13400, SDS-PAGE
145000
-
1 * 145000, alpha, + 1 * 66000, beta, SDS-PAGE
208000
-
equilibrium sedimentation
24000
-
1 * 24000 + 1 * 12000, mature enzyme, SDS-PAGE
24892
-
6 * 24892, alpha, + 6 * 8856, beta, calculation from amino acid sequence
25380
-
6 * 25380, alpha, + 6 * 8840, beta, synthesized as a precursor proHDC pi6 of MW 205000. A cleavage between Ser81 and Ser82 generates the alpha and beta chains, calculation from nucleotide sequence
27000
-
6 * 27000, alpha, + 6 * 9000, beta, SDS-PAGE
28000
-
6 * 28000, alpha, + 6 * 8000, beta, SDS-PAGE
28800
-
alpha6beta6, 6 * 28800 + 6 * 13400, SDS-PAGE
29700
-
x * 9000 + x * 29700, the larger subunit contains a pyruvate residue
37000
-
x * 37000, uncleaved proenzyme, SDS-PAGE
43000
-
4 * 43000, SDS-PAGE
50000
-
2 * 50000, SDS-PAGE
53000 - 55000
active enzyme form
66000
-
1 * 145000, alpha, + 1 * 66000, beta, SDS-PAGE
8000
-
6 * 28000, alpha, + 6 * 8000, beta, SDS-PAGE
8840
-
6 * 25380, alpha, + 6 * 8840, beta, synthesized as a precursor proHDC pi6 of MW 205000. A cleavage between Ser81 and Ser82 generates the alpha and beta chains, calculation from nucleotide sequence
8856
-
6 * 24892, alpha, + 6 * 8856, beta, calculation from amino acid sequence
95000
-
enzyme form 1, 2 and 3, gel filtration
110000
-
gel filtration
42500
-
2 * and 4 * 42500, SDS-PAGE
42500
-
4 * and 2 * 42500, SDS-PAGE
53000
-
2 * 53000, SDS-PAGE
53000
-
2 * 53000, SDS-PAGE, 2 * 74000, recombinant 5-3fold FLAG-tagged and 3-HA-tagged enzyme, SDS-PAGE
54000
-
2 * 54000, SDS-PAGE
54000
-
2 * 54000, SDS-PAGE
54000
-
1 * 54000, enzyme from soluble fraction, SDS-PAGE in absence of 2-mercaptoethanol
54000
-
x * 54000, processed HDC protein, SDS-PAGE
54000
-
x * 54000, processed HDC protein, SDS-PAGE
55000
-
2 * 55000, SDS-PAGE
55000
-
x * 55000, SDS-PAGE
74000
-
x * 74000, enzyme from particulate fraction, SDS-PAGE in absence of 2-mercaptoethanol
74000
-
2 * 53000, SDS-PAGE, 2 * 74000, recombinant 5-3fold FLAG-tagged and 3-HA-tagged enzyme, SDS-PAGE
9000
-
x * 9000 + x * 29700, the larger subunit contains a pyruvate residue
9000
-
6 * 27000, alpha, + 6 * 9000, beta, SDS-PAGE
additional information
processing intermediates of about 63 kDa with potential residual activity are observed in some cell types
additional information
-
processing intermediates of about 63 kDa with potential residual activity are observed in some cell types
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heterodimer
-
1 * 24000 + 1 * 12000, mature enzyme, SDS-PAGE
monomer
-
1 * 54000, enzyme from soluble fraction, SDS-PAGE in absence of 2-mercaptoethanol
?
-
x * 74000, enzyme from particulate fraction, SDS-PAGE in absence of 2-mercaptoethanol
?
-
x * 52400, SDS-PAGE
-
?
-
x * 9000 + x * 29700, the larger subunit contains a pyruvate residue
?
-
x * 54000, processed HDC protein, SDS-PAGE
?
-
x * 54000, processed HDC protein, SDS-PAGE
?
-
x * 37000, uncleaved proenzyme, SDS-PAGE
dimer
-
-
dimer
structure analysis, overview
dimer
-
2 * 50000, SDS-PAGE
dimer
-
2 * 55000, SDS-PAGE
dimer
-
2 * 53000, SDS-PAGE
dimer
-
2 * 54000, SDS-PAGE
dimer
-
2 * 53000, SDS-PAGE, 2 * 74000, recombinant 5'-3fold FLAG-tagged and 3'-HA-tagged enzyme, SDS-PAGE
dimer
-
2 * 53000, SDS-PAGE, 2 * 74000, recombinant 5'-3fold FLAG-tagged and 3'-HA-tagged enzyme, SDS-PAGE
-
dimer
-
2 * and 4 * 42500, SDS-PAGE
dimer
-
2 * 54000, SDS-PAGE
dimer
-
1 * 145000, alpha, + 1 * 66000, beta, SDS-PAGE
dimer
-
2 * 53000-58000, SDS-PAGE, the exact sequence of each monomer is not known
dodecamer
-
6 * 27000, alpha, + 6 * 9000, beta, SDS-PAGE
dodecamer
-
6 * 24892, alpha, + 6 * 8856, beta, calculation from amino acid sequence
dodecamer
-
6 * 28000, alpha, + 6 * 8000, beta, SDS-PAGE
dodecamer
-
alpha6beta6, 6 * 28800 + 6 * 13400, SDS-PAGE
dodecamer
-
alpha6beta6, 6 * 28800 + 6 * 13400, SDS-PAGE
-
hexamer
-
6 * 25380, alpha, + 6 * 8840, beta, synthesized as a precursor proHDC pi6 of MW 205000. A cleavage between Ser81 and Ser82 generates the alpha and beta chains, calculation from nucleotide sequence
hexamer
-
6 * 25380, alpha, + 6 * 8840, beta, synthesized as a precursor proHDC pi6 of MW 205000. A cleavage between Ser81 and Ser82 generates the alpha and beta chains, calculation from nucleotide sequence
-
multimer
putative alpha-chain of 27-30 kDa, beta-chain of 7-9 kDa, and a third 35-37 kDa band, SDS-PAGE
multimer
-
putative alpha-chain of 27-30 kDa, beta-chain of 7-9 kDa, and a third 35-37 kDa band, SDS-PAGE
-
tetramer
-
-
tetramer
-
4 * 43000, SDS-PAGE
tetramer
-
4 * 43000, SDS-PAGE
-
tetramer
-
4 * and 2 * 42500, SDS-PAGE
additional information
structure-function relationship, molecular modeling, overview
additional information
structure-function relationship, molecular modeling, overview
additional information
structure-function relationship, molecular modeling, overview
additional information
structure-function relationship, molecular modeling, overview
additional information
structure-function relationship, molecular modeling, overview
additional information
structure molecular modeling
additional information
-
structure molecular modeling
additional information
structure-function relationship, molecular modeling, overview
additional information
the 150 amino acid long C-terminal region present in mammalian HDC but absent in homologous Gram-negative bacteria HDC and all mammalian DDCs. The C-terminus has not got a well-defined secondary structure and it must be removed to reach the active conformation of mammalian HDC. The C-terminus is probably required for sorting the enzyme to the endoplasmic reticulum (ER), after which it can be removed to render the active form of the enzyme located in ER lumen
additional information
-
the 150 amino acid long C-terminal region present in mammalian HDC but absent in homologous Gram-negative bacteria HDC and all mammalian DDCs. The C-terminus has not got a well-defined secondary structure and it must be removed to reach the active conformation of mammalian HDC. The C-terminus is probably required for sorting the enzyme to the endoplasmic reticulum (ER), after which it can be removed to render the active form of the enzyme located in ER lumen
additional information
structure-function relationship, molecular modeling, overview
additional information
-
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
additional information
structure-function relationship, molecular modeling, overview
additional information
structure-function relationship, molecular modeling, overview
additional information
structure-function relationship, molecular modeling, overview
additional information
structure-function relationship, molecular modeling, overview
additional information
structure-function relationship, molecular modeling, overview
additional information
structure-function relationship, molecular modeling, overview
additional information
-
monomeric structure modeling
additional information
structure-function relationship, molecular modeling, overview
additional information
-
five HDC isoforms of 63000 Da, 54000 Da, 48000 Da, 40000 Da and 36000 Da, that derive from the 74000 Da full-length primary translation isoform
additional information
structure-function relationship, molecular modeling, overview
additional information
structure-function relationship, molecular modeling, overview
additional information
structure-function relationship, molecular modeling, overview
additional information
structure-function relationship, molecular modeling, overview
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proteolytic modification
-
enzyme undergoes processing with a major processed band of 59 kDa being observed in addition to a number of minor bands. Processing to the 59 kDa band is caspase-6 dependent
proteolytic modification
the processing to the active form of mammalian HDC relies on the proteinase activity of caspase 9 and the tandem aspartate residues Asp517-Asp518, Asp550-Asp551
proteolytic modification
-
the 74000 Da precursor form is converted into the mature 53000 Da form
proteolytic modification
-
post-translational cleavage by caspase-9 in a mouse mastocytoma P-815, residues D547-D551 and D517-K527 are important, overview
proteolytic modification
-
post-translational cleavage by caspase-9 in a mouse mastocytoma P-815, residues D547-D551 and D517-K527 are important, overview
-
proteolytic modification
-
74000 Da precursor is most probably processed to a carboxy truncated form of 53000-58000 Da
proteolytic modification
-
at least three isoforms with molecular masses of 74000 Da, 63000 Da and 53000 Da, the latter two forms derive from the 74000 Da form by carboxyl-terminal truncation, 63000 Da isoform is probably the active form
proteolytic modification
-
post-translational processing of 74000 Da HDC is required for activity, carboxyl-terminal processing generates an active 55000 Da isoform and additional isoforms with molecular weights higher than 55000 Da
proteolytic modification
-
C-terminal processing of the about 74 kDa full-length protein occurs naturally in vivo, with the production of multiple truncated isoforms. The 74 kDa full-length isoform is deficient in substrate binding, the C-terminally truncated isoforms with molecular masses between 70 kDa and 58 kDa have gradually increasing specific activities
proteolytic modification
-
the protein is processed into major 63, 54 and 58/59 kDa doublet bands. Processing at the HDC SKD 501/502/503 site is likely to be caspase-dependent
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C179S/C417S
double mutation prevents nonspecific polymerization and improves the homogeneity of purified enzyme
C180S/C418S
mutation facilitates the purification and crystallization of enzyme. Mutant shows Km and kcat values similar to wild-type
D551A/D552A
-
mutation in conserved di-aspartate motif. Mutation does not lead to a loss in levels of any of the processed isoforms
DD513A/D514A
-
mutation in conserved di-aspartate motif. Mutation does not lead to a loss in levels of any of the processed isoforms
K305G
complete loss of activity
S354G
mutation at the active site, enlarges the size of the substrate-binding pocket and results in a decreased affinity for histidine, but an acquired ability to bind and act on L-DOPA as a substrate. Mutant exhibits similar absorption spectra as wild-type with two absorption bands at 335 and 425 nm
Y334F
complete loss of activity
D53N/D54N
-
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
H231F
-
mutant enzymes His231Phe and His231Arg are inactive
H231N
-
mutant enzyme His231Asn is 0.2% as active as the wild-type enzyme
H231Q
-
mutant His231Gln is 12% as active as the wild-type enzyme
H231R
-
mutant enzymes His231Phe and His231Arg are inactive
K232A
-
mutant enzyme Lys232Ala is inactive but retains ability to bind both pyridoxal 5'-phosphate and His efficiently
S229A
-
mutant Ser229Ala or Ser229Cys are about 7% as active as the wild-type enzyme
S229C
-
mutant Ser229Ala or Ser229Cys are about 7% as active as the wild-type enzyme
H231N
-
mutant enzyme His231Asn is 0.2% as active as the wild-type enzyme
-
H231Q
-
mutant His231Gln is 12% as active as the wild-type enzyme
-
S229A
-
mutant Ser229Ala or Ser229Cys are about 7% as active as the wild-type enzyme
-
S229C
-
mutant Ser229Ala or Ser229Cys are about 7% as active as the wild-type enzyme
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C552A
-
site-directed mutagenesis, the mutant shows similar cleavage by caspase-9 as the wild-type enzyme
D517A
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site-directed mutagenesis, the mutant shows reduced cleavage by caspase-9 compared to the wild-type enzyme
D518A
-
site-directed mutagenesis, the mutant shows reduced cleavage by caspase-9 compared to the wild-type enzyme
D518A/D550A/D551A
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site-directed mutagenesis, the mutant shows highly reduced activation by butyrate compared to the wild-type enzyme
D547A
-
site-directed mutagenesis, the mutant shows reduced cleavage by caspase-9 compared to the wild-type enzyme
D547A/P548A/F549A
-
site-directed mutagenesis, the mutant shows highly reduced cleavage by caspase-9 compared to the wild-type enzyme
D550A
-
site-directed mutagenesis, the mutant shows reduced cleavage by caspase-9 compared to the wild-type enzyme
D550A/D551A
-
site-directed mutagenesis, the mutant shows highly reduced cleavage by caspase-9 compared to the wild-type enzyme
D550A/D551A/C552A
-
site-directed mutagenesis, the mutant shows highly reduced cleavage by caspase-9 compared to the wild-type enzyme
D551A
-
site-directed mutagenesis, the mutant shows reduced cleavage by caspase-9 compared to the wild-type enzyme
F549A
-
site-directed mutagenesis, the mutant shows reduced cleavage by caspase-9 compared to the wild-type enzyme
I525A
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site-directed mutagenesis, the mutant shows reduced cleavage by caspase-9 compared to the wild-type enzyme
K524A
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site-directed mutagenesis, the mutant shows reduced cleavage by caspase-9 compared to the wild-type enzyme
K527A
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site-directed mutagenesis, the mutant shows reduced cleavage by caspase-9 compared to the wild-type enzyme
P519A
-
site-directed mutagenesis, the mutant shows reduced cleavage by caspase-9 compared to the wild-type enzyme
P548A
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site-directed mutagenesis, the mutant shows reduced cleavage by caspase-9 compared to the wild-type enzyme
Q521A
-
site-directed mutagenesis, the mutant shows similar cleavage by caspase-9 as the wild-type enzyme
R523A
-
site-directed mutagenesis, the mutant shows reduced cleavage by caspase-9 compared to the wild-type enzyme
T544A/M545A/P546A
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site-directed mutagenesis, the mutant shows highly reduced cleavage by caspase-9 compared to the wild-type enzyme
D517A
-
site-directed mutagenesis, the mutant shows reduced cleavage by caspase-9 compared to the wild-type enzyme
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D518A
-
site-directed mutagenesis, the mutant shows reduced cleavage by caspase-9 compared to the wild-type enzyme
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D547A/P548A/F549A
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site-directed mutagenesis, the mutant shows highly reduced cleavage by caspase-9 compared to the wild-type enzyme
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T544A/M545A/P546A
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site-directed mutagenesis, the mutant shows highly reduced cleavage by caspase-9 compared to the wild-type enzyme
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C316V
-
the mutant shows 34% activity compared to the wild type enzyme
D271E
-
mutant conserves 2% of the wild type HDC activity
D315N
-
no enzymatic activity
D315V
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no enzymatic activity
D543A/D544A
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mutation in conserved di-aspartate motif. Mutation does not lead to a loss in levels of any of the processed isoforms
DD519A/D520A
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mutation in conserved di-aspartate motif. Mutation does not lead to a loss in levels of any of the processed isoforms
DELTA517-656
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C-terminall truncated enzyme is fully active
DELTA517-656/C104S
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activity is significantly decreased relative to wild-type enzyme
DELTA517-656/C115S
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activity is significantly decreased relative to wild-type enzyme
DELTA517-656/C254S
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activity is significantly decreased relative to wild-type enzyme
DELTA517-656/C316S
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activity is significantly decreased relative to wild-type enzyme
DELTA517-656/D276G
-
no activity detectable
DELTA517-656/H197G
-
activity is 11.8fold lower than wild-type activity
DELTA517-656/K308G
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no activity detectable
DELTA517-656/Q343G344ins
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no activity detectable
DELTA517-656/Q343ins
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activity is 2.3fold lower than wild-type activity
DELTA517-656/S307G
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activity is 13.4fold lower than wild-type activity
H197G
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mutant retains 10% of the wild type HDC activity
S82A
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the HdcA mutant mimics the proenzyme
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
G58N
the amino acid change can be responsible for the slow autoactivation and the appearance of HDC in the pi chain form
G58N
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the amino acid change can be responsible for the slow autoactivation and the appearance of HDC in the pi chain form
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additional information
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mutation of an EEAPD motif at amino acids 556-560 of the human hHDC protein leads to a decrease in the 59 kDa processed band
additional information
the mutation of a stop codon after W317 in gene hdc leads to a truncated enzyme and the Tourette syndrome
additional information
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the mutation of a stop codon after W317 in gene hdc leads to a truncated enzyme and the Tourette syndrome
additional information
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none of the four residues Met233, Cys230, Cys239 and Ser322 are essential for activity, altough all replacements reduce the activity of the enzyme significantly
additional information
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none of the four residues Met233, Cys230, Cys239 and Ser322 are essential for activity, altough all replacements reduce the activity of the enzyme significantly
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additional information
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construction of deletion mutants with altered activation by butyrate and cleavage by caspase-9, overview
additional information
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construction of deletion mutants with altered activation by butyrate and cleavage by caspase-9, overview
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45
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stable for at least 30 min, without pyridoxal 5'-phosphate
50
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40% loss of activity after 30 min, 5fold increase of half-life in presence of saturating concentrations of pyridoxal 5'-phosphate
57
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50% loss of activity in 4 min, 5fold increase of half-life in presence of saturating concentrations of pyridoxal 5'-phosphate
64
-
50% loss of activity in 30 s, 5fold increase of half-life in presence of saturating concentrations of pyridoxal 5'-phosphate
65
20 min, 20% residual activity
70
-
85% loss of activity after 20 min
80
-
complete loss of activity after 20 min
4 - 50
-
purified native enzyme, highly stable at
4 - 50
low activity at 50°C
40
-
not stable beyond 40°C
40
-
2% loss of activity after 20 min
50 - 60
heat resistance analysis of the enzyme at 50-100°C, and determination of D-value 1.6-6.3 and z-value 18.0 for the Enterobacter aerogenes strain, isolated from tuna, at 50-65°C. The enzyme is inactivated at 60°C
50 - 60
heat resistance analysis of the enzyme at 50-100°C, and determination of D-value 1.6-4.1 and z-value 19.2 for the Morganella morganii strain, isolated from tuna, at 50-65°C. The enzyme is inactivated at 60°C
50 - 60
heat resistance analysis of the enzyme at 50-100°C, and determination of D-value 1.6-2.9 and z-value 13.3 for the Photobacterium damselae strain, isolated from tuna, at 50-65°C. The enzyme is inactivated at 60°C
50 - 60
heat resistance analysis of the enzyme at 50-100°C, and determination of D-value 1.9-4.3 and z-value 22.0 for the Raoultella planticola strain, isolated from tuna, at 50-65°C. The enzyme is inactivated at 60°C
55
-
denaturation of enzyme activity
55
-
50% loss of activity in 13 min, 5fold increase of half-life in presence of saturating concentrations of pyridoxal 5'-phosphate
55
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denaturation of enzyme activity
60
-
50% loss of activity in 2 min, 5fold increase of half-life in presence of saturating concentrations of pyridoxal 5'-phosphate
60
20 min, 72% residual activity
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-20°C, 50 mM potassium phosphate buffer, pH 6.8, 0.01 mM pyridoxal 5'-phosphate, enzyme form 1 and 2 are stable for at least 6 weeks, activity of enzyme form 3 declines steadily
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-20°C, 50 mM potassium phosphate, pH 6.8, 0.2 mM dithiothreitol, 0.01 mM pyridoxal 5'-phosphate, 2% polyethylene glycol, stable for at least 3 months, even at a low protein concentration, 0.01 mg/ml
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-20C, purified recombinant enzyme, 3 months
-20°C, purified recombinant enzyme, 3 months, complete loss of activity
-70°C, 94% of the original activity in the fresh preparation
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-70°C, no loss of activity for at least 6 months
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0°C, 50 mM potassium phosphate, pH 6.8, 0.2 mM dithiothreitol, 0.01 mM pyridoxal 5'-phosphate, 2% polyethylene glycol No. 300, withoout significant loss of enzyme activity after 2 weeks
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4°C, stable for about 1 week
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-20C, purified recombinant enzyme, 3 months
-
-20C, purified recombinant enzyme, 3 months
-20C, purified recombinant enzyme, 3 months
-20C, purified recombinant enzyme, 3 months
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2 enzyme forms: 74000 Da and 74000 Da, expression in Escherichia coli
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cDNA encodes a protein of about 74000 Da, expression in Sf9 cells
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cDNA encoding for residues 1-512 of HDC
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cDNA expression in AGS-B cells
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DNA and amino acid sequence analysis and comparison, intron-exon relationships, phylogenetic analysis, overview
DNA and amino acid sequence analysis, phylogenetic tree, 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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enzyme expression analysis
expressed in Escherichia coli DH5alpha cells
expressed in Escherichia coli JM109 (DE3) cells
expressed in Lactococcus lactis strain NZ9000 and Escherichia coli DH5alpha cells
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expression in COS-7 cells
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expression in COS-7 cells as Myc- or EGFP-tagged constructs, targeting of the endoplasmic reticulum membranes, subcellular distribution pattern, overview
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expression in Escherichia coli
expression in Sf9 insect cells
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expression of 5'-3fold FLAG-tagged and 3'-HA-tagged enzyme in 293FT and P-815 cells using a lentiviral expression system
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expression of cDNA in COS-7 cells
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gene hdc, cDNA is cloned from chicken hypothalamic mRNA, sequence comparisons, quantitative real-time PCR enzyme expression analysis, DNA and amino acid sequence determination and anlysis, recombinant expression, the expressed protein shows high enzymatic activity
gene hdc, DNA and amino acid sequence determination and analysis
gene hdc, located on chromosome 15q21.2, different splicing products, sequence comparisons, regulatory cis elements in the human HDC promoter (TATA, GC, CACC, Sp1 and GATA boxes): two cis-elements are located between the positions -855 and -821 with respect to the transcription start point that regulates the transcription of the HDC in human basophilic cells. Other regulatory elements are located in position -500 and between positions -532 and -497. The HDC promoter also contains a CpG island involved in epigenetic regulation of its expression during the differentiation of histamine-producing cells
gene hdc, recombinant expression of His-tagged enzyme in Escherichia coli
mutant enzymes expressed in Escherichia coli
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quantitative expression analysis in mast cells of different maturation stage of patients with systemic mastocytosis, overview
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quantitative PCR enzyme expression analysis
-
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DNA and amino acid sequence analysis and comparison, intron-exon relationships, phylogenetic analysis, overview
DNA and amino acid sequence analysis and comparison, intron-exon relationships, phylogenetic analysis, overview
DNA and amino acid sequence analysis and comparison, intron-exon relationships, phylogenetic analysis, overview
DNA and amino acid sequence analysis and comparison, intron-exon relationships, phylogenetic analysis, overview
DNA and amino acid sequence analysis and comparison, intron-exon relationships, phylogenetic analysis, overview
DNA and amino acid sequence analysis and comparison, intron-exon relationships, phylogenetic analysis, overview
DNA and amino acid sequence analysis and comparison, intron-exon relationships, phylogenetic analysis, overview
DNA and amino acid sequence analysis and comparison, intron-exon relationships, phylogenetic analysis, overview
DNA and amino acid sequence analysis and comparison, intron-exon relationships, phylogenetic analysis, overview
DNA and amino acid sequence analysis and comparison, intron-exon relationships, phylogenetic analysis, overview
DNA and amino acid sequence analysis and comparison, intron-exon relationships, phylogenetic analysis, overview
DNA and amino acid sequence analysis and comparison, intron-exon relationships, phylogenetic analysis, overview
DNA and amino acid sequence analysis and comparison, intron-exon relationships, phylogenetic analysis, overview
DNA and amino acid sequence analysis and comparison, intron-exon relationships, phylogenetic analysis, overview
DNA and amino acid sequence analysis and comparison, intron-exon relationships, phylogenetic analysis, overview
DNA and amino acid sequence analysis and comparison, intron-exon relationships, phylogenetic analysis, overview
DNA and amino acid sequence analysis and comparison, intron-exon relationships, phylogenetic analysis, overview
expressed in Escherichia coli DH5alpha cells
expressed in Escherichia coli DH5alpha cells
expressed in Escherichia coli DH5alpha cells
expressed in Escherichia coli DH5alpha cells
expressed in Escherichia coli DH5alpha cells
expression in COS7 cell
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expression in COS7 cell
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expression in Escherichia coli
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expression in Escherichia coli
-
expression in Escherichia coli
-
expression in Escherichia coli
-
expression in Escherichia coli
expression in Escherichia coli
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gene hdc, DNA and amino acid sequence determination and analysis
gene hdc, DNA and amino acid sequence determination and analysis
gene hdc, DNA and amino acid sequence determination and analysis
gene hdc, recombinant expression of His-tagged enzyme in Escherichia coli
gene hdc, recombinant expression of His-tagged enzyme in Escherichia coli
gene hdc, recombinant expression of His-tagged enzyme in Escherichia coli
gene hdc, recombinant expression of His-tagged enzyme in Escherichia coli
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12-O-tetradecanoylphorbol-13-acetate induces HDC in mast cells
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both flower buds of Lonicera japonica and chlorogenic acid have inhibitory activities against the expression of 53-kDa HDC and histamine production in human epidermal keratinocytes. Chlorogenic acid shows a weaker effect on histamine production than that of flower buds of Lonicera japonica suggesting that other chemical constituents besides chlorogenic acid might contribute to the inhibitory activities. Chlorogenic acid might have an effect on the histamine production in other cells as well such as mast cells in addition to keratinocytes in the epidermis
HDC transcription is repressed by Kruppel-like factor 4 (KLF4) interacting at the level of Sp1 binding site, and by the nuclear factors Ying-yang 1 and SREBP-1a that interact with the GC box. The histone acetyl transferases KAT5 (also named as TIP60) and HDAC7 seem to be involved in this mechanisms of KLF4-mediated HDC repression acting as corepressors
histidine decarboxylase expression is 2fold higher in the B16F10 melanoma cells as compared to non-cancerous Melan-A cells
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in histamine producing immune cells, HDC expression is modulated by a long list of different stimulus, including lipopolysaccharydes, polypeptides (for instance, neuropeptide P, cytokines), inflammation regulators (for instance, phorbolesters plus dexamethasone), or other compounds (for instance, the intracelular levels of polyamines). Helicobacter pylori infection promotes HDC expression through a signaling pathway involving the trans-elements Rap1 and beta-ra
induction of the histamine-forming enzyme histidine decarboxylase in skeletal muscles by prolonged muscular work, interleukin-1beta (IL-1beta) and TNF-alpha may cooperatively mediate this induction. IL-1beta increases HDC activity in all the muscles tested (masseter, pectoralis, and quadriceps femoris). HDC activity in these tissues peaks at around 5 h after the injection of IL-1beta (10 ng/g), injection of TNF-alpha (100 ng/g) also increases HDC activity in all of these muscles
intravenous injection of Toll-like receptor (TLR)-4-agonistic synthetic lipid A definitely induces HDC activity in the liver, spleen, and lungs, especially the lungs, in mice (maximum activity is induced after about 3 h). The TLR2/6 agonistic synthetic diacyl-type lipopeptide FSL-1 and TLR3-agonistic poly I:C are also effective in inducing HDC, while the NOD2-agonistic synthetic muramyldipeptide (5 mg/kg) and NOD1-agonistic synthetic FK156 (D-lactyl-L-Ala-gamma-D-Glu-meso-DAP-Gly, 0.01-0.1 mg/kg), and FK565 (heptanoyl-g-D-Glu-meso-DAP-D-Ala, 0.5 mg/kg) exhibit only weak activities in this respect. Mice primed with intravenous injection of NOD1 or NOD2 agonists produce higher HDC activity following the 4-6 h later intravenous challenge with the above TLR agonists
-
rapid eye movement sleep deprivation (REM-SD) increases immunoreactive L-histidine decarboxylase by day 5, and it remains elevated in both dorsal and ventral aspects of the tuberomammillary complex
ultraviolet B and surfactant exposure induce the expression of histamine-synthesizing enzyme histidine decarboxylase in keratinocytes. Lipopolysaccharide, house dust mite (HDM) extract, and cytokines, which are implicated in allergic inflammation, promote the expression of the enzyme and upregulate histamine levels in keratinocytes
when the cultures are supplemented with L-histidine, a 4fold increase in the HDC concentration is observed compared to the control conditions. When L-arginine is present in the medium together with histidine, the HDC concentration is only 2fold higher than the basal level
induction of the histamine-forming enzyme histidine decarboxylase in skeletal muscles by prolonged muscular work, interleukin-1beta (IL-1beta) and TNF-alpha may cooperatively mediate this induction. IL-1beta increases HDC activity in all the muscles tested (masseter, pectoralis, and quadriceps femoris). HDC activity in these tissues peaks at around 5 h after the injection of IL-1beta (10 ng/g), injection of TNF-alpha (100 ng/g) also increases HDC activity in all of these muscles
induction of the histamine-forming enzyme histidine decarboxylase in skeletal muscles by prolonged muscular work, interleukin-1beta (IL-1beta) and TNF-alpha may cooperatively mediate this induction. IL-1beta increases HDC activity in all the muscles tested (masseter, pectoralis, and quadriceps femoris). HDC activity in these tissues peaks at around 5 h after the injection of IL-1beta (10 ng/g), injection of TNF-alpha (100 ng/g) also increases HDC activity in all of these muscles
-
-
rapid eye movement sleep deprivation (REM-SD) increases immunoreactive L-histidine decarboxylase by day 5, and it remains elevated in both dorsal and ventral aspects of the tuberomammillary complex
rapid eye movement sleep deprivation (REM-SD) increases immunoreactive L-histidine decarboxylase by day 5, and it remains elevated in both dorsal and ventral aspects of the tuberomammillary complex
-
-
when the cultures are supplemented with L-histidine, a 4fold increase in the HDC concentration is observed compared to the control conditions. When L-arginine is present in the medium together with histidine, the HDC concentration is only 2fold higher than the basal level
-
when the cultures are supplemented with L-histidine, a 4fold increase in the HDC concentration is observed compared to the control conditions. When L-arginine is present in the medium together with histidine, the HDC concentration is only 2fold higher than the basal level
-
-
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diagnostics
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HDC can be used as an immunohistochemical marker for the detection of immature neoplastic mast cells in patients with mast cell-proliferative disorders
drug development
HDC is a potential target to attenuate histamine production in certain pathological states using structure-based inhibitors, 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, overview
medicine
-
confirmatory test for identification of Enterobacter aerogenes
medicine
-
histamine-mediated signaling contributes to malaria pathogenesis, histidine decarboxylase-deficient mice are highly resistant to severe malaria and display resistance to Plasmodium berghei strains ANKA and NK65
medicine
-
histidine decarboxylase-deficient mice present a numerical and functional deficit in invariant NK T cells as evidenced by a drastic decrease of IL-4 and IFN-gamma production
medicine
-
loss of HDC is a marker of malignant transformation and dedifferentiation of B-cells infiltrating the skin
medicine
-
suppression of histamine signaling by inhibition of HDC may be a novel target of probiotics in preventing allergic diseases
nutrition
dairy products must be dedicated to a thorough risk analysis and development of strategies to contrast the presence of histaminogenic Streptococcus thermophilus strains in products from raw or mildly heat-treated milk. The HdcA enzyme in crude cell-free extracts is mostly active at acidic pH values common in dairy products. NaCl concentrations lower than 5% do not affect its activity. The enzyme is quite resistant to heat treatments resembling low pasteurization, but is inactivated at 75°C for 2 min
nutrition
-
dairy products must be dedicated to a thorough risk analysis and development of strategies to contrast the presence of histaminogenic Streptococcus thermophilus strains in products from raw or mildly heat-treated milk. The HdcA enzyme in crude cell-free extracts is mostly active at acidic pH values common in dairy products. NaCl concentrations lower than 5% do not affect its activity. The enzyme is quite resistant to heat treatments resembling low pasteurization, but is inactivated at 75°C for 2 min
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