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Synonyms
DCHS, Decarboxylase, histidine, HDC, HdcA, HisDCase, histamine-forming enzyme, L-Histidine decarboxylase, pyruvoyl-dependent decarboxylase, pyruvoyl-dependent histidine decarboxylase, TOM92,
more
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L-histidine = histamine + CO2
L-histidine = histamine + CO2

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L-histidine = histamine + CO2
structure-activity relationship, active site structure, molecular modeling, the imidazole ring is located in a pocket composed of residues Tyr-81B, Asn-302B, Ser-304B, Lys-305B, Leu-102A, Phe-104A, and Ser-354A
L-histidine = histamine + CO2
catalytic mechanism, quantum mechanics-molecular mechanics study and molecular dynamics simulations using the enzyme's crystal structure, PDB ID 4E1O, overview. The reaction involves two sequential steps: the decarboxylation of L-histidine and the protonation of the generated intermediate from which results histamine. The rate-limiting step is the first one with an activation barrier of 17.9 kcal/mol. In contrast, the second step is very fast and exergonic. When the substrate L-histidine is available in the active site of HDC, it binds to the pyridoxal 5'-phosphate cofactor. In this process, the imine bond formed between pyridoxal 5'-phosphate and Lys305A is cleaved and a new external aldimine intermediate is created between the pyridoxal 5'-phosphate cofactor and the amino group of the substrate
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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1-methyl-DL-histidine
1-methylhistamine + CO2
1-Methylhistidine
1-Methylhistamine
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very poor substrate
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?
2-Thiolhistidine
1-Thiolhistamine
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very poor substrate
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?
3,4-Dihydroxyphenylalanine
Dopamine + CO2
no substate for wild-type. Mutant S354G acquires the ability to decarboxylate 3,4-dihydroxyphenylalanine
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?
3-Methylhistidine
2-Methylhistamine
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very poor substrate
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?
beta-(1,2,4-Triazole-3)-Ala
?
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very poor substrate
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?
beta-(Thiazole-2)-Ala
?
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very poor substrate
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?
L-histidin
histamine + CO2
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L-histidine
histamine + CO2
additional information
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1-methyl-DL-histidine

1-methylhistamine + CO2
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?
1-methyl-DL-histidine
1-methylhistamine + CO2
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?
beta-(Pyridyl-2)-Ala

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very poor substrate
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?
beta-(Pyridyl-2)-Ala
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beta-(Pyridyl-2)-Ala
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?
L-His

Histamine + CO2
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L-His
Histamine + CO2
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L-His
Histamine + CO2
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L-His
Histamine + CO2
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L-His
Histamine + CO2
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L-His
Histamine + CO2
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?
L-His
Histamine + CO2
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?
L-His
Histamine + CO2
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?
L-His
Histamine + CO2
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L-His
Histamine + CO2
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?
L-His
Histamine + CO2
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?
L-His
Histamine + CO2
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L-His
Histamine + CO2
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?
L-His
Histamine + CO2
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?
L-His
Histamine + CO2
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?
L-His
Histamine + CO2
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L-His
Histamine + CO2
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?
L-His
Histamine + CO2
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?
L-His
Histamine + CO2
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?
L-His
Histamine + CO2
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?
L-His
Histamine + CO2
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?
L-His
Histamine + CO2
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?
L-His
Histamine + CO2
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?
L-His
Histamine + CO2
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?
L-His
Histamine + CO2
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?
L-His
Histamine + CO2
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?
L-His
Histamine + CO2
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?
L-His
Histamine + CO2
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?
L-His
Histamine + CO2
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?
L-His
Histamine + CO2
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?
L-His
Histamine + CO2
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?
L-His
Histamine + CO2
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?
L-His
Histamine + CO2
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?
L-His
Histamine + CO2
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?
L-His
Histamine + CO2
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?
L-His
Histamine + CO2
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?
L-His
Histamine + CO2
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?
L-His
Histamine + CO2
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?
L-His
Histamine + CO2
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?
L-His
Histamine + CO2
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?
L-His
Histamine + CO2
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?
L-His
Histamine + CO2
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?
L-His
Histamine + CO2
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?
L-His
Histamine + CO2
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?
L-His
Histamine + CO2
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?
L-His
Histamine + CO2
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strictly specific for L-His
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?
L-histidine

histamine + CO2
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?
L-histidine
histamine + CO2
structure-function relationship, molecular modeling, overview
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?
L-histidine
histamine + CO2
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?
L-histidine
histamine + CO2
structure-function relationship, molecular modeling, overview
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?
L-histidine
histamine + CO2
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?
L-histidine
histamine + CO2
structure-function relationship, molecular modeling, overview
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?
L-histidine
histamine + CO2
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?
L-histidine
histamine + CO2
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?
L-histidine
histamine + CO2
structure-function relationship, molecular modeling, overview
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?
L-histidine
histamine + CO2
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?
L-histidine
histamine + CO2
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?
L-histidine
histamine + CO2
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?
L-histidine
histamine + CO2
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?
L-histidine
histamine + CO2
structure-function relationship, molecular modeling, overview
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?
L-histidine
histamine + CO2
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?
L-histidine
histamine + CO2
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?
L-histidine
histamine + CO2
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?
L-histidine
histamine + CO2
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?
L-histidine
histamine + CO2
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?
L-histidine
histamine + CO2
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?
L-histidine
histamine + CO2
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?
L-histidine
histamine + CO2
-
HDC is the key enzyme involved in histamine production
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?
L-histidine
histamine + CO2
-
histamine is a bioactive amine acting as a neurotransmitter as well as a chemical mediator
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?
L-histidine
histamine + CO2
-
rate-limiting step in histamine biosynthesis, enzyme activity is increased in pre-eclampsia, a complex of disorder of pregnancy involving a systemic inflammatory response and endothelial activation within the maternal vascular system, overview
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?
L-histidine
histamine + CO2
structure-function relationship, molecular modeling, overview
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?
L-histidine
histamine + CO2
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substrate-specific
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?
L-histidine
histamine + CO2
the binding site of HDC does not tolerate groups other than the imidazole side chain of histidine
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L-histidine
histamine + CO2
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?
L-histidine
histamine + CO2
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L-histidine
histamine + CO2
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L-histidine
histamine + CO2
structure-function relationship, molecular modeling, overview
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?
L-histidine
histamine + CO2
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?
L-histidine
histamine + CO2
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?
L-histidine
histamine + CO2
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?
L-histidine
histamine + CO2
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?
L-histidine
histamine + CO2
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?
L-histidine
histamine + CO2
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?
L-histidine
histamine + CO2
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?
L-histidine
histamine + CO2
-
expression of hdc is also mediated by the bacterial growth phase, overview
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?
L-histidine
histamine + CO2
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?
L-histidine
histamine + CO2
-
expression of hdc is also mediated by the bacterial growth phase, overview
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?
L-histidine
histamine + CO2
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?
L-histidine
histamine + CO2
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?
L-histidine
histamine + CO2
structure-function relationship, molecular modeling, overview
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?
L-histidine
histamine + CO2
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?
L-histidine
histamine + CO2
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?
L-histidine
histamine + CO2
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?
L-histidine
histamine + CO2
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?
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
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?
L-histidine
histamine + CO2
structure-function relationship, molecular modeling, overview
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L-histidine
histamine + CO2
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?
L-histidine
histamine + CO2
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?
L-histidine
histamine + CO2
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?
L-histidine
histamine + CO2
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?
L-histidine
histamine + CO2
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?
L-histidine
histamine + CO2
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677857, 680148, 680165, 680763, 690778, 692084, 692606, 693426, 693469, 716351, 716876 -
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?
L-histidine
histamine + CO2
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L-histidine
histamine + CO2
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?
L-histidine
histamine + CO2
-
HDC induction may contribute to the replenishment of the reduced pool of mast cell histamine in the anaphylactic period
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?
L-histidine
histamine + CO2
-
HDC is the rate-limiting enzyme for histamine synthesis
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L-histidine
histamine + CO2
structure-function relationship, molecular modeling, overview
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?
L-histidine
histamine + CO2
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?
L-histidine
histamine + CO2
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?
L-histidine
histamine + CO2
-
HDC is the rate-limiting enzyme for histamine synthesis
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?
L-histidine
histamine + CO2
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?
L-histidine
histamine + CO2
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?
L-histidine
histamine + CO2
-
expression of hdc is also mediated by the bacterial growth phase, overview
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?
L-histidine
histamine + CO2
-
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?
L-histidine
histamine + CO2
-
expression of hdc is also mediated by the bacterial growth phase, overview
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?
L-histidine
histamine + CO2
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?
L-histidine
histamine + CO2
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?
L-histidine
histamine + CO2
structure-function relationship, molecular modeling, overview
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?
L-histidine
histamine + CO2
-
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?
L-histidine
histamine + CO2
-
expression of hdc is also mediated by the bacterial growth phase, overview
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?
L-histidine
histamine + CO2
-
-
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?
L-histidine
histamine + CO2
-
expression of hdc is also mediated by the bacterial growth phase, overview
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?
L-histidine
histamine + CO2
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?
L-histidine
histamine + CO2
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?
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
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L-histidine
histamine + CO2
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?
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
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?
L-histidine
histamine + CO2
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L-histidine
histamine + CO2
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?
L-histidine
histamine + CO2
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?
L-histidine
histamine + CO2
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?
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
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?
L-histidine
histamine + CO2
structure-function relationship, molecular modeling, overview
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?
L-histidine
histamine + CO2
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?
L-histidine
histamine + CO2
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?
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
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?
L-histidine
histamine + CO2
-
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?
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
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?
L-histidine
histamine + CO2
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?
L-histidine
histamine + CO2
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L-histidine
histamine + CO2
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L-histidine
histamine + CO2
structure-function relationship, molecular modeling, overview
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L-histidine
histamine + CO2
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L-histidine
histamine + CO2
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L-histidine
histamine + CO2
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L-histidine
histamine + CO2
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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
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?
L-histidine
histamine + CO2
-
the enzyme has roles in inflammatory and neurological diseases, and in progression of several cancer types
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L-histidine
histamine + CO2
structure-function relationship, molecular modeling, overview
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L-histidine
histamine + CO2
-
the enzyme is a group II pyridoxal 5Ć¢ĀĀ-phosphate-dependent L-amino acid decarboxylase, L-aaDCII
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L-histidine
histamine + CO2
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L-histidine
histamine + CO2
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L-histidine
histamine + CO2
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?
L-histidine
histamine + CO2
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?
L-histidine
histamine + CO2
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?
L-histidine
histamine + CO2
-
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?
L-histidine
histamine + CO2
-
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?
L-histidine
histamine + CO2
-
-
690319, 691549, 691707, 692565, 693044, 693822, 693827, 693829, 694385, 694402, 715728, 716351 -
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L-histidine
histamine + CO2
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L-histidine
histamine + CO2
structure-function relationship, molecular modeling, overview
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L-histidine
histamine + CO2
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L-histidine
histamine + CO2
-
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?
L-histidine
histamine + CO2
structure-function relationship, molecular modeling, overview
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L-histidine
histamine + CO2
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?
L-histidine
histamine + CO2
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?
L-histidine
histamine + CO2
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?
L-histidine
histamine + CO2
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?
L-histidine
histamine + CO2
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?
L-histidine
histamine + CO2
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?
L-histidine
histamine + CO2
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?
L-histidine
histamine + CO2
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?
L-histidine
histamine + CO2
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?
L-histidine
histamine + CO2
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L-histidine
histamine + CO2
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L-histidine
histamine + CO2
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L-histidine
histamine + CO2
structure-function relationship, molecular modeling, overview
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?
Npi-Methylhistidine

?
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Npi-Methylhistidine
?
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additional information

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induction by phorbol myristate acetate
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?
additional information
?
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enzyme immunoassay for detection of histamine production
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additional information
?
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enzyme immunoassay for detection of histamine production
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?
additional information
?
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mast cells are known to produce histamine through a difference mechanism than HDC induction
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additional information
?
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biocomputational analysis of the evolutionary specificity-determinants in decreasing order: Y279, D315, P85, M97, S77, L132, R361, Y83, D348, S112, Q150, G40, L377, R415, A82, W75, P70, R286, L285, and I430, overview
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?
additional information
?
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HDC is the key enzyme for histamine biosynthesis
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additional information
?
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no substrates: lysine, arginine, tyrosine, tryptophan or ornithine
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?
additional information
?
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no substrates: lysine, arginine, tyrosine, tryptophan or ornithine
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?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
L-histidin
histamine + CO2
-
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?
L-histidine
histamine + CO2
additional information
?
-
L-histidine

histamine + CO2
-
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?
L-histidine
histamine + CO2
-
-
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?
L-histidine
histamine + CO2
-
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?
L-histidine
histamine + CO2
-
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?
L-histidine
histamine + CO2
-
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?
L-histidine
histamine + CO2
-
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?
L-histidine
histamine + CO2
-
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?
L-histidine
histamine + CO2
-
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?
L-histidine
histamine + CO2
-
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?
L-histidine
histamine + CO2
-
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?
L-histidine
histamine + CO2
-
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?
L-histidine
histamine + CO2
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?
L-histidine
histamine + CO2
-
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?
L-histidine
histamine + CO2
-
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?
L-histidine
histamine + CO2
-
-
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?
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
-
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?
L-histidine
histamine + CO2
-
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?
L-histidine
histamine + CO2
-
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?
L-histidine
histamine + CO2
-
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?
L-histidine
histamine + CO2
-
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?
L-histidine
histamine + CO2
-
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?
L-histidine
histamine + CO2
-
expression of hdc is also mediated by the bacterial growth phase, overview
-
-
?
L-histidine
histamine + CO2
-
expression of hdc is also mediated by the bacterial growth phase, overview
-
-
?
L-histidine
histamine + CO2
-
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?
L-histidine
histamine + CO2
-
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?
L-histidine
histamine + CO2
-
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?
L-histidine
histamine + CO2
-
-
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?
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
-
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?
L-histidine
histamine + CO2
-
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?
L-histidine
histamine + CO2
-
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?
L-histidine
histamine + CO2
-
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?
L-histidine
histamine + CO2
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?
L-histidine
histamine + CO2
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?
L-histidine
histamine + CO2
-
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?
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
-
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.
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
-
-
-
brenda
-
UniProt
brenda
BDF1 mice
-
-
brenda
male BALB/c mice
-
-
brenda
strain C57BL/6 resistant to infection by Leishmania major, and strain BALB/c susceptible to infection with Leishmania major
-
-
brenda
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
-
-
brenda
-
-
-
brenda
-
UniProt
brenda
-
-
-
brenda
isolated from wine, gene hdc
-
-
brenda
-
-
-
brenda
isolated from wine, gene hdc
-
-
brenda
-
-
-
brenda
-
UniProt
brenda
-
-
-
brenda
isolated from wine, gene hdc
-
-
brenda
-
-
-
brenda
isolated from wine, gene hdc
-
-
brenda
gene hdc
UniProt
brenda
strain ATCC 33539T
SwissProt
brenda
-
SwissProt
brenda
-
TREMBL
brenda
gene hdc
UniProt
brenda
two histidine decarboxylases: a constitutive and an inducible enzyme
-
-
brenda
-
-
-
brenda
-
SwissProt
brenda
-
-
-
brenda
14% of the strains are positive for histidine decarboxylase
-
-
brenda
i.e. Klebsiella planticola
SwissProt
brenda
i.e. Raoultella planticola
SwissProt
brenda
strain ATCC 43176
-
-
brenda
-
4142, 4144, 4145, 4149, 4160, 4161, 4162, 649295, 650807, 651162, 651497, 652502, 653860, 653861, 663930, 663937, 665184, 666896 -
-
brenda
-
TREMBL
brenda
-
690319, 691549, 691707, 692565, 693044, 693822, 693827, 693829, 694385, 694402, 715728, 716351, 726888, 728029 -
-
brenda
-
TREMBL
brenda
3 enzyme forms: 1, 2, and 3
-
-
brenda
-
UniProt
brenda
CHCC1524
-
-
brenda
JCM 10006T
-
-
brenda
strain JCM10006
UniProt
brenda
gene JM31; i.e. Listonella anguillarum, gene JM31
TREMBL
brenda
i.e. Listonella anguillarum
SwissProt
brenda
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