Information on EC 4.1.1.22 - Histidine decarboxylase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY
4.1.1.22
-
RECOMMENDED NAME
GeneOntology No.
Histidine decarboxylase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-histidine = histamine + CO2
show the reaction diagram
-
-
-
-
L-histidine = histamine + CO2
show the reaction diagram
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
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
decarboxylation
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of secondary metabolites
-
-
histamine biosynthesis
-
-
Histidine metabolism
-
-
histidine metabolism
-
-
Metabolic pathways
-
-
SYSTEMATIC NAME
IUBMB Comments
L-histidine carboxy-lyase (histamine-forming)
A pyridoxal-phosphate protein (in animal tissues). The bacterial enzyme has a pyruvoyl residue as prosthetic group.
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Decarboxylase, histidine
-
-
-
-
HDC
-
-
-
-
HisDCase
-
-
-
-
L-Histidine decarboxylase
-
-
-
-
TOM92
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9024-61-7
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
33% of the tested strains are positive for histidine decarboxylase
-
-
Manually annotated by BRENDA team
all strains are positive for histidine decarboxylase
-
-
Manually annotated by BRENDA team
i.e. Aerobacter aerogenes
SwissProt
Manually annotated by BRENDA team
strain MB31
SwissProt
Manually annotated by BRENDA team
strain MB31
SwissProt
Manually annotated by BRENDA team
strain 0006
UniProt
Manually annotated by BRENDA team
strain 464, isolated from wine, gene hdc
-
-
Manually annotated by BRENDA team
Lactobacillus hilgardii 464
strain 464
-
-
Manually annotated by BRENDA team
Lactobacillus hilgardii 464
strain 464, isolated from wine, gene hdc
-
-
Manually annotated by BRENDA team
Lactobacillus hilgardii 6
strain 0006
UniProt
Manually annotated by BRENDA team
Lactobacillus hilgardii ISE 5211
-
-
-
Manually annotated by BRENDA team
fragment; strain LTH2076
UniProt
Manually annotated by BRENDA team
Lactobacillus sakei LTH2076
fragment; strain LTH2076
UniProt
Manually annotated by BRENDA team
strain 30a
-
-
Manually annotated by BRENDA team
strain 30a; wilde-type and mutant enzyme
-
-
Manually annotated by BRENDA team
wild-type and and mutant enzyme
-
-
Manually annotated by BRENDA team
i.e. Mesorhizobium loti
SwissProt
Manually annotated by BRENDA team
all strains examined are positive
-
-
Manually annotated by BRENDA team
i.e. Proteus morganii
SwissProt
Manually annotated by BRENDA team
i.e. Proteus morganii, strain JCM 1672
UniProt
Manually annotated by BRENDA team
strain JCM1672T
SwissProt
Manually annotated by BRENDA team
Morganella morganii AM-15
strain AM-15
-
-
Manually annotated by BRENDA team
Morganella morganii JCM1672T
strain JCM1672T
SwissProt
Manually annotated by BRENDA team
BDF1 mice
-
-
Manually annotated by BRENDA team
male BALB/c mice
-
-
Manually annotated by BRENDA team
strain C57BL/6 resistant to infection by Leishmania major, and strain BALB/c susceptible to infection with Leishmania major
-
-
Manually annotated by BRENDA team
virgin female
UniProt
Manually annotated by BRENDA team
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
-
-
Manually annotated by BRENDA team
Mus musculus BDF1
BDF1 mice
-
-
Manually annotated by BRENDA team
no activity in Buttiauxella sp.
-
-
-
Manually annotated by BRENDA team
no activity in Cedecea sp.
-
-
-
Manually annotated by BRENDA team
no activity in Citrobacter amalonaticus
-
-
-
Manually annotated by BRENDA team
no activity in Citrobacter farmeri
-
-
-
Manually annotated by BRENDA team
no activity in Citrobacter koseri
-
-
-
Manually annotated by BRENDA team
no activity in Citrobacter sedlakii
-
-
-
Manually annotated by BRENDA team
no activity in Edwardsiella tarda
-
-
-
Manually annotated by BRENDA team
no activity in Enterobacter cloacae
-
-
-
Manually annotated by BRENDA team
no activity in Escherichia coli
-
-
-
Manually annotated by BRENDA team
no activity in Ewingella americana
-
-
-
Manually annotated by BRENDA team
no activity in Hafnia alvei
-
-
-
Manually annotated by BRENDA team
no activity in Klebsiella oxytoca
-
-
-
Manually annotated by BRENDA team
no activity in Klebsiella pneumoniae
-
-
-
Manually annotated by BRENDA team
no activity in Kluyvera sp.
-
-
-
Manually annotated by BRENDA team
no activity in Leclercia adecarboxylata
-
-
-
Manually annotated by BRENDA team
no activity in Leminorella sp.
-
-
-
Manually annotated by BRENDA team
no activity in Moellerella wisconsensis
-
-
-
Manually annotated by BRENDA team
no activity in Pantoea sp.
-
-
-
Manually annotated by BRENDA team
no activity in Proteus mirabilis
-
-
-
Manually annotated by BRENDA team
no activity in Proteus penneri
-
-
-
Manually annotated by BRENDA team
no activity in Proteus vulgaris
-
-
-
Manually annotated by BRENDA team
no activity in Providencia sp.
-
-
-
Manually annotated by BRENDA team
no activity in Rahnella aquatilis
-
-
-
Manually annotated by BRENDA team
no activity in Raoultella terrigena
-
-
-
Manually annotated by BRENDA team
no activity in Salmonella sp.
-
-
-
Manually annotated by BRENDA team
no activity in Serratia marcescens
-
-
-
Manually annotated by BRENDA team
no activity in Shigella sp.
-
-
-
Manually annotated by BRENDA team
no activity in Yersinia enterocolitica
-
-
-
Manually annotated by BRENDA team
no activity in Yersinia pseudotuberculosis
-
-
-
Manually annotated by BRENDA team
strain 4042
-
-
Manually annotated by BRENDA team
strain 4042, isolated from wine, gene hdc
-
-
Manually annotated by BRENDA team
strain 9204
-
-
Manually annotated by BRENDA team
strain 9204
UniProt
Manually annotated by BRENDA team
Oenococcus oeni 4042
strain 4042
-
-
Manually annotated by BRENDA team
Oenococcus oeni 4042
strain 4042, isolated from wine, gene hdc
-
-
Manually annotated by BRENDA team
Oenococcus oeni 9204
strain 9204
-
-
Manually annotated by BRENDA team
Oenococcus oeni 9204
strain 9204
UniProt
Manually annotated by BRENDA team
ssp. japonica
TREMBL
Manually annotated by BRENDA team
strain P270
-
-
Manually annotated by BRENDA team
strain P270, isolated from wine, gene hdc
-
-
Manually annotated by BRENDA team
Pediococcus parvulus P270
strain P270
-
-
Manually annotated by BRENDA team
Pediococcus parvulus P270
strain P270, isolated from wine, gene hdc
-
-
Manually annotated by BRENDA team
strain ATCC 33539T
SwissProt
Manually annotated by BRENDA team
strain JCM 8968, gene hdc
UniProt
Manually annotated by BRENDA team
Photobacterium damselae JCM 8968
strain JCM 8968, gene hdc
UniProt
Manually annotated by BRENDA team
strain MB36
SwissProt
Manually annotated by BRENDA team
strain NBRC 13896; strain NBRC 13896, gene hdc
UniProt
Manually annotated by BRENDA team
strain YS4-7; strain YS4-7, gene hdc
UniProt
Manually annotated by BRENDA team
two histidine decarboxylases: a constitutive and an inducible enzyme
-
-
Manually annotated by BRENDA team
Photobacterium phosphoreum MB36
strain MB36
SwissProt
Manually annotated by BRENDA team
Photobacterium phosphoreum NBRC 13896
strain NBRC 13896; strain NBRC 13896, gene hdc
UniProt
Manually annotated by BRENDA team
Photobacterium phosphoreum YS4-7
strain YS4-7; strain YS4-7, gene hdc
UniProt
Manually annotated by BRENDA team
strain AU34
SwissProt
Manually annotated by BRENDA team
Proteus vulgaris AU34
strain AU34
SwissProt
Manually annotated by BRENDA team
14% of the strains are positive for histidine decarboxylase
-
-
Manually annotated by BRENDA team
i.e. Raoultella planticola
SwissProt
Manually annotated by BRENDA team
strain 8433
SwissProt
Manually annotated by BRENDA team
strain ATCC 43176
-
-
Manually annotated by BRENDA team
Raoultella planticola 8433
strain 8433
SwissProt
Manually annotated by BRENDA team
3 enzyme forms: 1, 2, and 3
-
-
Manually annotated by BRENDA team
strain IFIJ12
UniProt
Manually annotated by BRENDA team
Staphylococcus capitis IFIJ12
strain IFIJ12
UniProt
Manually annotated by BRENDA team
Staphylococcus epidermidis TYH1
-
UniProt
Manually annotated by BRENDA team
Streptococcus thermophilus PRI60
-
UniProt
Manually annotated by BRENDA team
Tetragenococcus halophilus H
strain H
UniProt
Manually annotated by BRENDA team
strain JCM10006
UniProt
Manually annotated by BRENDA team
Tetragenococcus muriaticus JCM 10006T
JCM 10006T
-
-
Manually annotated by BRENDA team
Tetragenococcus muriaticus JCM10006
strain JCM10006
UniProt
Manually annotated by BRENDA team
gene JM31; i.e. Listonella anguillarum, gene JM31
TREMBL
Manually annotated by BRENDA team
i.e. Listonella anguillarum
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1-Methylhistidine
1-Methylhistamine
show the reaction diagram
-
very poor substrate
-
-
-
2-Thiolhistidine
1-Thiolhistamine
show the reaction diagram
-
very poor substrate
-
-
-
3,4-Dihydroxyphenylalanine
Dopamine + CO2
show the reaction diagram
-
no substate for wild-type. Mutant S354G acquires the ability to decarboxylate 3,4-dihydroxyphenylalanine
-
-
?
3-Methylhistidine
2-Methylhistamine
show the reaction diagram
-
very poor substrate
-
-
-
beta-(1,2,4-Triazole-3)-Ala
?
show the reaction diagram
-
very poor substrate
-
-
-
beta-(Pyridyl-2)-Ala
?
show the reaction diagram
-
-
-
-
-
beta-(Pyridyl-2)-Ala
?
show the reaction diagram
-
very poor substrate
-
-
-
beta-(Pyridyl-2)-Ala
?
show the reaction diagram
Morganella morganii AM-15
-
-
-
-
-
beta-(Thiazole-2)-Ala
?
show the reaction diagram
-
very poor substrate
-
-
-
L-His
Histamine + CO2
show the reaction diagram
-
-
-
-
L-His
Histamine + CO2
show the reaction diagram
-
-
-
-
L-His
Histamine + CO2
show the reaction diagram
-
-
-
-
L-His
Histamine + CO2
show the reaction diagram
-
-
-
-
L-His
Histamine + CO2
show the reaction diagram
-
-
-
-
L-His
Histamine + CO2
show the reaction diagram
-
-
-
-
L-His
Histamine + CO2
show the reaction diagram
-
-
-
-
L-His
Histamine + CO2
show the reaction diagram
-
-
-
-
L-His
Histamine + CO2
show the reaction diagram
-
-
-
-
L-His
Histamine + CO2
show the reaction diagram
-
-
-
-
L-His
Histamine + CO2
show the reaction diagram
-
-
-
-
L-His
Histamine + CO2
show the reaction diagram
-
-
-
-
L-His
Histamine + CO2
show the reaction diagram
-
-
-
-
L-His
Histamine + CO2
show the reaction diagram
-
-
-
-
L-His
Histamine + CO2
show the reaction diagram
-
-
-
-
L-His
Histamine + CO2
show the reaction diagram
-
-
-
-
L-His
Histamine + CO2
show the reaction diagram
-
-
-
-
L-His
Histamine + CO2
show the reaction diagram
-
-
-
-
L-His
Histamine + CO2
show the reaction diagram
-
-
-
-
L-His
Histamine + CO2
show the reaction diagram
-
-
-
-
L-His
Histamine + CO2
show the reaction diagram
-
-
-
-
L-His
Histamine + CO2
show the reaction diagram
-
-
-
-
L-His
Histamine + CO2
show the reaction diagram
-
-
-
-
L-His
Histamine + CO2
show the reaction diagram
-
-
-
-
L-His
Histamine + CO2
show the reaction diagram
-
-
-
-
L-His
Histamine + CO2
show the reaction diagram
-
-
-
-
L-His
Histamine + CO2
show the reaction diagram
-
-
-
-
L-His
Histamine + CO2
show the reaction diagram
-
-
-
-
L-His
Histamine + CO2
show the reaction diagram
-
-
-
-
L-His
Histamine + CO2
show the reaction diagram
-
-
-
-
L-His
Histamine + CO2
show the reaction diagram
-
-
-
-
L-His
Histamine + CO2
show the reaction diagram
-
-
-
-
L-His
Histamine + CO2
show the reaction diagram
-
-
-
-
L-His
Histamine + CO2
show the reaction diagram
-
-
-
-
L-His
Histamine + CO2
show the reaction diagram
-
-
-
-
L-His
Histamine + CO2
show the reaction diagram
-
-
-
-
L-His
Histamine + CO2
show the reaction diagram
-
-
-
-
L-His
Histamine + CO2
show the reaction diagram
-
-
-
-
L-His
Histamine + CO2
show the reaction diagram
-
-
-
-
L-His
Histamine + CO2
show the reaction diagram
-
-
-
-
L-His
Histamine + CO2
show the reaction diagram
-
strictly specific for L-His
-
-
L-His
Histamine + CO2
show the reaction diagram
Morganella morganii AM-15
-
-
-
-
L-His
Histamine + CO2
show the reaction diagram
Morganella morganii AM-15
-
-
-
-
L-His
Histamine + CO2
show the reaction diagram
Morganella morganii AM-15
-
-
-
-
L-His
Histamine + CO2
show the reaction diagram
Morganella morganii AM-15
-
-
-
-
L-His
Histamine + CO2
show the reaction diagram
Oenococcus oeni 9204
-
-
-
-
L-histidin
histamine + CO2
show the reaction diagram
-
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
-
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
-
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
-
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
-
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
-
-
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
-
-
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
-
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
-
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
-
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
-
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
-
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
-
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
-
-
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
-
-
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
P00862
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
-
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
-
-
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
-
-
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
-
-
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
-
-
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
Q83VD4
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
Q83VD3
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
Q83VD2
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
-
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
Q83VD9
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
Q83UY1
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
Q83VD5
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
Q86BW8
-
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
Q98A07
-
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
P16453
-
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
P95477
-
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
P05034
-
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
P54772
-
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
P28578
-
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
P19113
-
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
-
-
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
P28577
-
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
Q05733
-
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
Q7TMW5
-
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
-
-
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
Q56581, Q79JY8
-
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
Q1JU61, Q1JU62
-
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
Q1JU59
-
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
Q1JU60
-
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
Q894Q7
-
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
Q7NIG4
-
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
Q846V2
-
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
Q8RV06
-
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
Q9MA74
-
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
B1B5I3
-
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
Q5DLT9
-
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
Q32UL2
-
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
O66000
-
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
Q75UV3
-
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
A9IZZ1
-
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
P23738
-
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
B3Y006
-
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
-
expression of hdc is also mediated by the bacterial growth phase, overview
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
-
HDC induction may contribute to the replenishment of the reduced pool of mast cell histamine in the anaphylactic period
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
-
HDC is the key enzyme involved in histamine production
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
-
HDC is the rate-limiting enzyme for histamine synthesis
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
-
histamine is a bioactive amine acting as a neurotransmitter as well as a chemical mediator
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
Q1JU59
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
show the reaction diagram
Q1JU60
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
show the reaction diagram
Q1JU61, Q1JU62
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
the enzyme has roles in inflammatory and neurological diseases, and in progression of several cancer types
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
Q86BW8
structure-function relationship, molecular modeling, overview
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
Q98A07
structure-function relationship, molecular modeling, overview
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
P16453
structure-function relationship, molecular modeling, overview
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
P95477
structure-function relationship, molecular modeling, overview
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
P05034
structure-function relationship, molecular modeling, overview
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
P54772
structure-function relationship, molecular modeling, overview
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
P28578
structure-function relationship, molecular modeling, overview
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
-
structure-function relationship, molecular modeling, overview
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
P28577
structure-function relationship, molecular modeling, overview
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
Q05733
structure-function relationship, molecular modeling, overview
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
Q7TMW5
structure-function relationship, molecular modeling, overview
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
Q56581, Q79JY8
structure-function relationship, molecular modeling, overview
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
Q894Q7
structure-function relationship, molecular modeling, overview
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
Q7NIG4
structure-function relationship, molecular modeling, overview
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
Q846V2
structure-function relationship, molecular modeling, overview
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
Q8RV06
structure-function relationship, molecular modeling, overview
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
Q9MA74
structure-function relationship, molecular modeling, overview
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
-
substrate-specific
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
P19113
the binding site of HDC does not tolerate groups other than the imidazole side chain of histidine
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
-
the enzyme is a group II pyridoxal 5-phosphate-dependent L-amino acid decarboxylase, L-aaDCII
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
Photobacterium damselae JCM 8968
Q1JU60
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
show the reaction diagram
Tetragenococcus halophilus H
B1B5I3
-
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
Proteus vulgaris AU34
Q83VD5
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
Morganella morganii JCM1672T
Q83VD9
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
Raoultella planticola 8433
Q83UY1
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
Lactobacillus sakei LTH2076
Q32UL2
-
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
Photobacterium phosphoreum NBRC 13896
Q1JU62
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
show the reaction diagram
Photobacterium phosphoreum YS4-7
Q1JU61
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
show the reaction diagram
Pediococcus parvulus P270
-
expression of hdc is also mediated by the bacterial growth phase, overview
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
Pediococcus parvulus P270
-
-
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
Q83VD4
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
Staphylococcus capitis IFIJ12
A9IZZ1
-
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
Mus musculus BDF1
-
HDC is the rate-limiting enzyme for histamine synthesis
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
Tetragenococcus muriaticus JCM 10006T
-
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
Photobacterium phosphoreum MB36
Q83VD3
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
Lactobacillus hilgardii 464
-
expression of hdc is also mediated by the bacterial growth phase, overview
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
Lactobacillus hilgardii 464
-
-
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
Staphylococcus epidermidis TYH1
B3Y006
-
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
Lactobacillus hilgardii 6
Q5DLT9
-
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
Oenococcus oeni 4042
-
expression of hdc is also mediated by the bacterial growth phase, overview
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
Oenococcus oeni 4042
-
-
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
Tetragenococcus muriaticus JCM10006
Q75UV3
-
-
-
?
Npi-Methylhistidine
?
show the reaction diagram
Morganella morganii, Morganella morganii AM-15
-
-
-
-
-
L-histidine
histamine + CO2
show the reaction diagram
Oenococcus oeni 9204
O66000
-
-
-
?
additional information
?
-
-
induction by phorbol myristate acetate
-
-
-
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
?
-
-
mast cells are known to produce histamine through a difference mechanism than HDC induction
-
-
-
additional information
?
-
-
HDC is the key enzyme for histamine biosynthesis
-
-
-
additional information
?
-
Staphylococcus epidermidis, Staphylococcus epidermidis TYH1
B3Y006
no substrates: lysine, arginine, tyrosine, tryptophan or ornithine
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-histidin
histamine + CO2
show the reaction diagram
-
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
-
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
-
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
-
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
-
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
-
-
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
-
-
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
-
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
-
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
-
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
-
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
-
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
-
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
P00862
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
-
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
Q83VD4
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
Q83VD3
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
Q83VD2
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
-
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
Q83VD9
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
Q83UY1
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
Q83VD5
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
Q86BW8
-
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
Q98A07
-
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
P16453
-
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
P95477
-
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
P05034
-
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
P54772
-
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
P28578
-
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
P19113
-
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
-
-
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
P28577
-
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
Q05733
-
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
Q7TMW5
-
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
Q56581, Q79JY8
-
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
Q894Q7
-
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
Q7NIG4
-
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
Q846V2
-
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
Q8RV06
-
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
Q9MA74
-
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
-
expression of hdc is also mediated by the bacterial growth phase, overview
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
-
HDC induction may contribute to the replenishment of the reduced pool of mast cell histamine in the anaphylactic period
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
-
HDC is the key enzyme involved in histamine production
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
-
HDC is the rate-limiting enzyme for histamine synthesis
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
-
histamine is a bioactive amine acting as a neurotransmitter as well as a chemical mediator
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
Q1JU59
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
show the reaction diagram
Q1JU60
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
show the reaction diagram
Q1JU61, Q1JU62
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
the enzyme has roles in inflammatory and neurological diseases, and in progression of several cancer types
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
Photobacterium damselae JCM 8968
Q1JU60
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
show the reaction diagram
Proteus vulgaris AU34
Q83VD5
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
Morganella morganii JCM1672T
Q83VD9
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
Raoultella planticola 8433
Q83UY1
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
Photobacterium phosphoreum NBRC 13896
Q1JU62
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
show the reaction diagram
Photobacterium phosphoreum YS4-7
Q1JU61
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
show the reaction diagram
Pediococcus parvulus P270
-
expression of hdc is also mediated by the bacterial growth phase, overview
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
Q83VD4
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
Mus musculus BDF1
-
HDC is the rate-limiting enzyme for histamine synthesis
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
Tetragenococcus muriaticus JCM 10006T
-
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
Photobacterium phosphoreum MB36
Q83VD3
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
Lactobacillus hilgardii 464, Oenococcus oeni 4042
-
expression of hdc is also mediated by the bacterial growth phase, overview
-
-
?
additional information
?
-
-
induction by phorbol myristate acetate
-
-
-
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
?
-
-
mast cells are known to produce histamine through a difference mechanism than HDC induction
-
-
-
additional information
?
-
-
HDC is the key enzyme for histamine biosynthesis
-
-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
-
required; tightly bound to the apoenzyme. Non-competitive inhibition at high concentrations
pyridoxal 5'-phosphate
-
the enzyme binds 4 pyridoxal 5'-phosphate per tetramer
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
contains 1 mol of pyridoxal 5'-phosphate per mol of subunit
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
-
required
pyridoxal 5'-phosphate
-
dependent on
pyridoxal 5'-phosphate
-
dependent on
pyridoxal 5'-phosphate
-
activates, but does not influence the enzyme expression level
pyridoxal 5'-phosphate
-
dependent on
pyridoxal 5'-phosphate
Q86BW8
dependent on, binding structure involving a Schiff base, overview
pyridoxal 5'-phosphate
Q9MA74
dependent on, binding structure involving a Schiff base, overview
pyridoxal 5'-phosphate
Q894Q7
dependent on, binding structure involving a Schiff base, overview
pyridoxal 5'-phosphate
Q05733
dependent on, binding structure involving a Schiff base, overview
pyridoxal 5'-phosphate
P28577
dependent on, binding structure involving a Schiff base, overview
pyridoxal 5'-phosphate
Q7NIG4
dependent on, binding structure involving a Schiff base, overview
pyridoxal 5'-phosphate
-
dependent on, binding structure involving a Schiff base, overview
pyridoxal 5'-phosphate
Q98A07
dependent on, binding structure involving a Schiff base, overview
pyridoxal 5'-phosphate
P05034
dependent on, binding structure involving a Schiff base, overview
pyridoxal 5'-phosphate
Q7TMW5
dependent on, binding structure involving a Schiff base, overview
pyridoxal 5'-phosphate
Q8RV06
dependent on, binding structure involving a Schiff base, overview
pyridoxal 5'-phosphate
Q846V2
dependent on, binding structure involving a Schiff base, overview
pyridoxal 5'-phosphate
P95477
dependent on, binding structure involving a Schiff base, overview
pyridoxal 5'-phosphate
P28578
dependent on, binding structure involving a Schiff base, overview
pyridoxal 5'-phosphate
P16453
dependent on, binding structure involving a Schiff base, overview
pyridoxal 5'-phosphate
P54772
dependent on, binding structure involving a Schiff base, overview
pyridoxal 5'-phosphate
Q56581, Q79JY8
dependent on, binding structure involving a Schiff base, overview; dependent on, binding structure involving a Schiff base, overview
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
Q32UL2
-
pyridoxal 5'-phosphate
B1B5I3
-
pyridoxal 5'-phosphate
Q75UV3
-
pyridoxal 5'-phosphate
A9IZZ1
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
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
Pyruvoyl group
-
dependent on
additional information
-
HDC uses a covalently bound pyruvoyl moiety as cofactor
-
additional information
Q5DLT9
pyruvoyl-residue at the NH2-terminus
-
additional information
Q32UL2
pyruvoyl-residue at the NH2-terminus
-
additional information
O66000
pyruvoyl-residue at the NH2-terminus
-
additional information
B1B5I3
pyruvoyl-residue at the NH2-terminus
-
additional information
Q75UV3
pyruvoyl-residue at the NH2-terminus
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CaCl2
-
maximal activity is observed only in the presence of high concentrations of various salts: KCl, NaCl, NaBr, K2SO4, CaCl2 or MgCl2
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
Mn2+
-
0.1 mM, enhances activity by 7-8%
additional information
-
constitutive and inducible enzyme show optimal activity in absence of NaCl
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(-)-epigallocatechin 3-gallate
-
-
(S)-alpha-fluoromethylhistidine
-
0.001 mM, complete inhibition
2-Hydrazino-3-(4-imidazolyl)propionic acid
-
-
2-Hydroxy-5-nitrobenzylbromide
-
-
4-coumaric acid
-
slight inhibition
5,5'-dithiobis(2-nitrobenzoate)
-
-
alpha-Fluoromethylhistidine
-
the (S)-isomer is a suicide substrate inhibitor, the (R)-isomer is an at least 10times less potent inhibitor
alpha-Fluoromethylhistidine
-
irreversible
alpha-Fluoromethylhistidine
-
-
alpha-Fluoromethylhistidine
-
-
alpha-Fluoromethylhistidine
-
-
alpha-Fluoromethylhistidine
-
-
alpha-Fluoromethylhistidine
-
-
alpha-Fluoromethylhistidine
-
alpha-FMH, specific inhibitor of HDC
alpha-Fluoromethylhistidine
-
irreversible inhibitor
alpha-Fluoromethylhistidine
-
-
alpha-Fluoromethylhistidine
-
-
alpha-Methylhistidine
-
-
alpha-Methylhistidine
-
-
alpha-Methylhistidine
-
-
caffeic acid
-
slight inhibition
carnosine
-
-
Citric acid
-
diminishes hdc gene expression
Co(NO3)2
-
slight
Co2+
-
0.1 mM, 20% decrease of activity
Cu2+
-
0.1 mM, strong inhibition
curcumin
-
slight inhibition
Cyanoborohydride
-
NaCNBH3
Cyanoborohydride
-
-
D-fructose
-
diminishes hdc gene expression
D-glucose
-
diminishes hdc gene expression
dithiothreitol
-
-
dithiothreitol
-
-
dithiothreitol
-
-
dithiothreitol
-
-
epicatechin
-
-
Epicatechin gallate
-
competitive versus L-histidine
epigallocatechin
-
-
epigallocatechin gallate
-
time-dependent inhibition, only under aerobic conditions
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
epsilon-N-Pyridoxyllysine
-
-
gallic acid
-
slight inhibition
guanidine
-
-
Hg2+
-
0.1 mM, strong inhibition
histamine
-
at high concentrations
histamine
-
-
Histidine methyl ester
-
-
Histidine methyl ester
-
mixed-type inhibition
imidazole
-
-
imidazole
-
competitively inhibited
Imidazoleacetic acid
-
-
kaempferol
-
slight inhibition
KCl
-
50% inhibition at 1.5 M
KCN
-
non-competitive
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-His-L-Phe
-
-
L-Histidine ethyl ester
-
-
L-histidine methyl ester
-
-
L-Malic acid
-
26% hdc gene expression at 4 g/l
malic acid
-
diminishes hdc gene expression
myricetin
-
-
N-pyridoxyl-L-histidine methyl ester
-
60% inhibition at 0.2 mM
NaCl
-
50% inhibition at 1.5 M
NaCl
Q1JU59
-
NaCl
Q1JU61, Q1JU62
;
NaCl
B3Y006
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
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
reduced glutathione
-
-
rosmarinic acid
-
-
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
Semicarbazide
-
-
Shoyuflavones
-
isolated from soy sauce
Sinapic acid
-
slight inhibition
tellimagrandin II
-
compound isolated from Filipendula ulmaria, non-competitive
Urocanic acid
-
-
Urocanic acid
-
-
Urocanic acid
-
-
methylgallate
-
slight inhibition
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
-
histamine causes a decrease in the expression of gene hdc
-
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
-
knockdown of the transcription factor C/EBPbeta by dehydroxymethylepoxyquinomicin reduces the HDC expression in lipopolysaccharide-treated cells
-
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
-
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
E7AXS8
not inhibitory: NaCl up to 5%
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Butyrate
-
highly activating for the wild-type enzyme
C/EBPbeta
-
essential for the HDC induction
-
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
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
pyridoxal 5'-phosphate
-
activates, but does not influence the enzyme expression level
pyruvate
-
contains several functionally essential pyruvate residues, covalently bound through an amide linkage to a Phe residue of the peptide chain. The free carbonyl group of these pyruvate residues undergoes Schiff base formation with His as part of the catalytic process
pyruvate
-
pyruvoyl-group is covalently bound to the alpha-subunit and undergoes Schiff base formation with histamine
pyruvate
-
contains a pyruvoyl group at the active centre
pyruvate
P00862
-
SH-groups
-
wild type and mutant enzyme each contain two SH groups per alpha-chain
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
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
monosodium urate
P23738
monosodium urate crystals injected into the air pouch lead to a highly upregulated mRNA level of HDC
-
additional information
-
intraperitoneal or oral administration of aspirin, dexamethasone or indomethacin elevates histidine decarboxylase activity in the stomach
-
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
-
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
-
tartaric acid, L-lactic acid, and sulfur dioxide have no effect on enzyme synthesis and activity
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.13
3,4-dihydroxyphenylalanine
-
mutant S354G, pH 6.8, 37C
5.8
alpha-methyl-DL-His
-
-
0.078
L-His
-
-
0.12
L-His
-
-
0.154
L-His
-
enzyme form 1
0.181
L-His
-
enzyme form 2
0.213
L-His
-
enzyme form 3
0.26
L-His
-
-
0.27
L-His
-
-
0.29
L-His
-
-
0.33
L-His
-
-
0.43
L-His
-
membrane-bound enzyme
0.46
L-His
-
solublilized membrane-bound enzyme
0.52
L-His
-
soluble enzyme
0.7
L-His
-
-
1.1
L-His
-
-
1.2
L-His
-
pH 6.5-6.7
1.4
L-His
-
wild-type enzyme
2.4
L-His
-
-
2.5
L-His
-
-
35
L-His
-
mutant enzyme
0.09
L-histidine
-
mutant C180/C418S, pH 6.8, 37C
0.1
L-histidine
-
wild-type, pH 6.8, 37C
0.3
L-histidine
P00862
pH 4.8
0.74
L-histidine
-
-
1.1
L-histidine
B3Y006
pH 4.8, 37C
1.45
L-histidine
-
mutant S354G, pH 6.8, 37C
100
L-histidine
P00862
pH 7.0
additional information
additional information
-
between pH 6 and pH 9 the Km-value for L-His declines from 1 mM to about 0.01 mM
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.29
3,4-dihydroxyphenylalanine
-
mutant S354G, pH 6.8, 37C
1.73
L-histidine
-
wild-type, pH 6.8, 37C
1.87
L-histidine
-
mutant C180/C418S, pH 6.8, 37C
2.01
L-histidine
-
mutant S354G, pH 6.8, 37C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
9.9
3,4-dihydroxyphenylalanine
-
mutant S354G, pH 6.8, 37C
1782
1.4
L-histidine
-
mutant S354G, pH 6.8, 37C
349
17.3
L-histidine
-
wild-type, pH 6.8, 37C
349
20.8
L-histidine
-
mutant C180/C418S, pH 6.8, 37C
349
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.01
Epicatechin gallate
-
pH 6.8, 37C, recombinant enzyme, versus L-histidine
0.00046
Histidine methyl ester
-
pH 6.8, 37C
0.001
rugosin A
-
pH 6.8, 37C
0.00041
rugosin A methyl ester
-
pH 6.8, 37C
0.00035
rugosin D
-
pH 6.8, 37C
0.00094
tellimagrandin II
-
pH 6.8, 37C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.00000014
-
HDC activity in cultured brain microvascular endothelial cells
0.0002
-
purified recombinant enzyme from Saccharomyces cerevisiae
0.75
-
-
0.8
-
-
17.26
-
-
32.75
B3Y006
pH 4.8, 37C
136
-
purified recombinant enzyme
143
Q1JU61, Q1JU62
purified recombinant enzyme
144
Q1JU61, Q1JU62
purified recombinant enzyme
147
Q1JU59
purified recombinant enzyme
147
Q1JU60
purified recombinant enzyme
166
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
tissue-specific activity induced by lipopolysaccharide, overview
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.8
-
wild-type and mutant enzyme
4.8
-
HDC is essentially inactive at neutral and alkaline pH and active at low pH, low pH shifts HDC from the inactive, i.e. T-state, to the active, i.e. R-state
6.2
-
-
6.2
-
assay at
6.5
-
soluble and membrane-associated enzyme
6.6
-
-
6.7
-
assay at
6.8
-
assay at
6.8
-
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3.5 - 8
-
50% of maximal activity at pH 3.5
4
B3Y006
about 50% of maximum activity
4.2
E7AXS8
83% of maximum activity
4.5 - 8.5
Q1JU59
abrupt decrease at pH 4.5
4.5 - 8.5
Q1JU60
-
4.5 - 8.5
-
abrupt decrease at pH 4.5
5.5 - 8
-
pH 5.5: about 35% of maximal activity, pH 8.0: about 10% of maximal activity, membrane-bound enzyme; pH 5.5: about 50% of maximal activity, pH 8.0: about 40% of maximal activity, soluble enzyme
5.5 - 8.5
Q1JU61, Q1JU62
rapid loss of activity below pH 5.5; rapid loss of activity below pH 5.5
6 - 7.6
-
pH 6.0: about 50% of maximal activity, pH 7.6: about 40% of maximal activity
6
-
constitutive enzyme
6
E7AXS8
65% of maximum activity
6.5
-
inducible enzyme
7 - 9
-
pH 7.0: about 85% of maximal activity, pH 9.0: about 70% of maximal activity
7 - 9
-
about 45% of maximal activity at pH 7.0 and at pH 9.0
7
B3Y006
sharp decline in activiy above
8
E7AXS8
18% of maximum activity
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 50
Q1JU59
50% of maximal activity at 50C, no activity at 60C
4 - 50
Q1JU60
50% of maximal activity at 50C, no activity at 60C
4 - 50
Q1JU61, Q1JU62
low activity at 50C; low activity at 50C
4 - 50
-
50% of maximal activity at 50C, no activity at 60C
4 - 50
-
HDC activity is very low at 4 and 50C
47 - 60
-
47C: about 50% of maximal activity, 60C: about 75% of maximal activity, no activity detectable at 65C
83
B3Y006
83% of maximum activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.7 - 4.8
-
isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
the posterodorsal medial amygdala has high levels of histidine decarboxylase
Manually annotated by BRENDA team
-
in basophilic leukemia
Manually annotated by BRENDA team
-
from patients with mastocytosis
Manually annotated by BRENDA team
-
the enzyme is not expressed after ischemic infarct
Manually annotated by BRENDA team
-
HDC expression is significantly increased in carcinoma cells
Manually annotated by BRENDA team
-
of osteoarthritic cartilage
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
high levels of HDC protein are also found in the striatum
Manually annotated by BRENDA team
-
ear skin
Manually annotated by BRENDA team
-
tuberomammillary nucleus of the hypothalamus
Manually annotated by BRENDA team
-
HDC mRNA is highly expressed in the posterior hypothalamus
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
P23738
pregnancy associated elevation of histidine decarboxylase activity is successfully affected by enzyme antisense oligonucleotide treatment, inducing short-term histamine deficiency
Manually annotated by BRENDA team
-
immature, low expression level in basophilic leukemia
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
Mus musculus BDF1
-
-
-
Manually annotated by BRENDA team
-
peritoneal cavity
Manually annotated by BRENDA team
Mus musculus BDF1
-
peritoneal cavity
-
Manually annotated by BRENDA team
-
differential activity of HDC in normal and pre-eclamptic placentae, overview
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
ear skin
Manually annotated by BRENDA team
-
in enterochromaffin-like cell, not in G cells
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
acrosomes of spermatids and spermatozoa
-
Manually annotated by BRENDA team
-
N-terminal membrane localization of the precursor 74-kDa form of the enzyme, which has neither an amino terminal signal sequence nor a hydrophobic membrane anchor, but a large C-terminal cytosolic portion, overview
Manually annotated by BRENDA team
additional information
-
granules of elicited mouse polymorphonuclear leukocytes. Histamine is synthesized by the enzyme attached to the granule membrane of polymorphonuclear leukocytes
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Lactobacillus sp. (strain 30a)
Lactobacillus sp. (strain 30a)
Lactobacillus sp. (strain 30a)
Lactobacillus sp. (strain 30a)
Lactobacillus sp. (strain 30a)
Lactobacillus sp. (strain 30a)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
34200
A9IZZ1
pi chain of HDC
692805
95000
-
enzyme form 1, 2 and 3, gel filtration
4147
100000
-
gel filtration
4163
110000
-
gel filtration
4149
110000
-
gel filtration
4158
113400
-
gel filtration
4150
115000
-
native PAGE
4158
121000
B3Y006
gel filtration
727564
170000
-
gel filtration
4150, 4153
190000
-
-
4141
208000
-
equilibrium sedimentation
4138
210000
-
gel filtration
4144
258000
-
gel filtration
651607
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 55000, SDS-PAGE
?
-
x * 74000, enzyme from particulate fraction, SDS-PAGE in absence of 2-mercaptoethanol
?
-
x * 9000 + x * 29700, the larger subunit contains a pyruvate residue
?
-
x * 37000, uncleaved proenzyme, SDS-PAGE
?
-
x * 54000, processed HDC protein, SDS-PAGE
dimer
-
-
dimer
-
-
dimer
-
2 * 50000, SDS-PAGE
dimer
-
2 * 55000, SDS-PAGE
dimer
-
2 * 53000, SDS-PAGE
dimer
-
2 * 54000, SDS-PAGE
dimer
-
2 * 54000, SDS-PAGE
dimer
-
2 * and 4 * 42500, 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
dimer
-
2 * 53000, SDS-PAGE, 2 * 74000, recombinant 5'-3fold FLAG-tagged and 3'-HA-tagged enzyme, SDS-PAGE
dimer
Mus musculus BDF1
-
2 * 53000, SDS-PAGE, 2 * 74000, recombinant 5'-3fold FLAG-tagged and 3'-HA-tagged enzyme, SDS-PAGE
-
dodecamer
-
6 * 27000, alpha, + 6 * 9000, beta, SDS-PAGE
dodecamer
-
6 * 24892, alpha, + 6 * 8856, beta, calculation from amino acid sequence, 6 * 28000, alpha, + 6 * 8000, beta, SDS-PAGE
dodecamer
-
alpha6beta6, 6 * 28800 + 6 * 13400, SDS-PAGE
dodecamer
Tetragenococcus muriaticus JCM 10006T
-
alpha6beta6, 6 * 28800 + 6 * 13400, SDS-PAGE
-
heterodimer
-
1 * 24000 + 1 * 12000, mature enzyme, 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
Oenococcus oeni 9204
-
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
-
homodimer
-
-
multimer
B3Y006
putative alpha-chain of 27-30 kDa, beta-chain of 7-9 kDa, and a third 35-37 kDa band, SDS-PAGE
multimer
Staphylococcus epidermidis TYH1
-
putative alpha-chain of 27-30 kDa, beta-chain of 7-9 kDa, and a third 35-37 kDa band, SDS-PAGE
-
tetramer
-
4 * 43000, SDS-PAGE
tetramer
-
4 * and 2 * 42500, SDS-PAGE
tetramer
Morganella morganii AM-15
-
4 * 43000, SDS-PAGE
-
monomer
-
1 * 54000, enzyme from soluble fraction, SDS-PAGE in absence of 2-mercaptoethanol
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
-
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 molecular modeling
additional information
-
monomeric structure modeling
additional information
Q86BW8
structure-function relationship, molecular modeling, overview
additional information
Q98A07
structure-function relationship, molecular modeling, overview
additional information
P16453
structure-function relationship, molecular modeling, overview
additional information
P95477
structure-function relationship, molecular modeling, overview
additional information
P05034
structure-function relationship, molecular modeling, overview
additional information
P54772
structure-function relationship, molecular modeling, overview
additional information
P28578
structure-function relationship, molecular modeling, overview
additional information
-
structure-function relationship, molecular modeling, overview
additional information
P28577
structure-function relationship, molecular modeling, overview
additional information
Q05733
structure-function relationship, molecular modeling, overview
additional information
Q7TMW5
structure-function relationship, molecular modeling, overview
additional information
-
structure-function relationship, molecular modeling, overview
additional information
Q894Q7
structure-function relationship, molecular modeling, overview
additional information
Q7NIG4
structure-function relationship, molecular modeling, overview
additional information
Q846V2
structure-function relationship, molecular modeling, overview
additional information
Q8RV06
structure-function relationship, molecular modeling, overview
additional information
Q9MA74
structure-function relationship, molecular modeling, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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 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
Mus musculus BDF1
-
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
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
core domain, to 1.8 A resolution. Three dimers per asymmetric unit. Molecular replacement carried out using the AroDC structure as a model
-
in complex with the inhibitor histidine methyl ester, to 1.8 A resolution. Cofactor pyridoxal 5'-phosphate 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. Residue Ser354 is a key residue for substrate specificity
-
crystal structure at 3.0 A resolution
-
crystal structure of active HDC at pH 4.8 at 2.5 A resolution, crystal structure of less active HDC at pH 8.0 at 2.7 A resolution, crystals are grown at room temperatur by hanging-drop vapor diffusion, drops contain 0.004 ml HDC at 12.5 mg/ml, 0.001 ml n-dodecyl-beta-D-maltoside and 0.005 ml precipitant solution from the well containing 25% polyethylene glycol 400, 8% polyethylene glycol 400, 100 mM Tris pH 8.0, and 100 mM sodium acetate, enzyme activity is regulated by pH-induced structural changes
P00862
modeling of complex with inhibitor epigallocatechin-3-gallate. 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
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.5
-
activity drops by 86% at pH 8.5
692809
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 50
Q1JU61, Q1JU62
low activity at 50C; low activity at 50C
677685
40
-
not stable beyond 40C
4150
40
-
2% loss of activity after 20 min
651607
45
-
stable for at least 30 min, without pyridoxal 5'-phosphate
4145
50
-
40% loss of activity after 30 min, 5fold increase of half-life in presence of saturating concentrations of pyridoxal 5'-phosphate
4145
55
-
50% loss of activity in 13 min, 5fold increase of half-life in presence of saturating concentrations of pyridoxal 5'-phosphate
4145
55
-
denaturation of enzyme activity
4161
57
-
50% loss of activity in 4 min, 5fold increase of half-life in presence of saturating concentrations of pyridoxal 5'-phosphate
4145
60
-
50% loss of activity in 2 min, 5fold increase of half-life in presence of saturating concentrations of pyridoxal 5'-phosphate
4145
60
E7AXS8
20 min, 72% residual activity
728063
64
-
50% loss of activity in 30 s, 5fold increase of half-life in presence of saturating concentrations of pyridoxal 5'-phosphate
4145
65
E7AXS8
20 min, 20% residual activity
728063
70
-
85% loss of activity after 20 min
651607
75
E7AXS8
2 min, inactivation
728063
80
-
complete loss of activity after 20 min
651607
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
HDC is a short-lived enzyme with a half-life of 1-2 h
-
inactivated by freezing and thawing
-
after dialysis for 48 h against buffer containing 1 mM semicarbazide, about 50% loss of activity, full recovery by adding pyridoxal 5'-phosphate
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, purified recombinant enzyme, 3 months
Q1JU59
-20C, 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
-
0C, 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
-
-20C, purified recombinant enzyme, 3 months
Q1JU60
-20C, purified recombinant enzyme, 3 months
Q1JU61, Q1JU62
-20C, purified recombinant enzyme, 3 months, complete loss of activity
Q1JU61, Q1JU62
-20C, purified recombinant enzyme, 3 months
-
-20C, 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
-
-70C, 94% of the original activity in the fresh preparation
-
-70C, no loss of activity for at least 6 months
-
4C, stable for about 1 week
-
-30C, stable for 7 days
B3Y006
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
separation of unmodified alpha and beta subunits and for reconstitution of fully active histidine decarboxylase
-
partially purified 53000 Da HDC
-
partial, 3 enzyme forms: 1, 2 and 3
-
phenyl-Sepharose column chromatography, DEAE column chromatography, and hydroxyapatite column chromatography
-
recombinant HDC
-
recombinant His-tagged enzyme
-
recombinant protein
-
His-Trap-FF crude chelating affinity chromatography
A9IZZ1
Ni2+-NTA column chromatography
-
ammonium sulfate, anion-exchange column, hydroxyapatite column
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence analysis and comparison, intron-exon relationships, phylogenetic analysis, overview
Q86BW8
DNA and amino acid sequence analysis and comparison, intron-exon relationships, phylogenetic analysis, overview
Q9MA74
DNA and amino acid sequence analysis and comparison, intron-exon relationships, phylogenetic analysis, overview
Q894Q7
DNA and amino acid sequence analysis and comparison, intron-exon relationships, phylogenetic analysis, overview
Q05733
DNA and amino acid sequence analysis and comparison, intron-exon relationships, phylogenetic analysis, overview
P28577
expression in Escherichia coli
-
-
Q83VD4
DNA and amino acid sequence analysis and comparison, intron-exon relationships, phylogenetic analysis, overview
Q7NIG4
2 enzyme forms: 74000 Da and 74000 Da, expression in Escherichia coli
-
DNA and amino acid sequence analysis and comparison, intron-exon relationships, phylogenetic analysis, overview
-
expression in COS7 cell
-
expression in Escherichia coli
-
quantitative expression analysis in mast cells of different maturation stage of patients with systemic mastocytosis, overview
-
expressed in Escherichia coli DH5alpha cells
Q5DLT9
expressed in Escherichia coli DH5alpha cells
Q32UL2
DNA and amino acid sequence analysis and comparison, intron-exon relationships, phylogenetic analysis, overview
Q98A07
DNA and amino acid sequence analysis and comparison, intron-exon relationships, phylogenetic analysis, overview
P05034
expression in Escherichia coli
-
gene hdc, DNA and amino acid sequence determination and analysis
Q1JU59
cDNA encodes a protein of about 74000 Da, expression in Sf9 cells
-
DNA and amino acid sequence analysis and comparison, intron-exon relationships, phylogenetic analysis, overview
Q7TMW5
expression in COS-7 cells as Myc- or EGFP-tagged constructs, targeting of the endoplasmic reticulum membranes, subcellular distribution pattern, overview
-
expression in Sf9 insect cells
-
expression of 5'-3fold FLAG-tagged and 3'-HA-tagged enzyme in 293FT and P-815 cells using a lentiviral expression system
-
expressed in Escherichia coli DH5alpha cells
O66000
DNA and amino acid sequence analysis and comparison, intron-exon relationships, phylogenetic analysis, overview
Q8RV06
gene hdc, DNA and amino acid sequence determination and analysis
Q1JU60
DNA and amino acid sequence analysis and comparison, intron-exon relationships, phylogenetic analysis, overview
Q846V2
gene hdc, DNA and amino acid sequence determination and analysis; gene hdc, DNA and amino acid sequence determination and analysis
Q1JU61, Q1JU62
DNA and amino acid sequence analysis and comparison, intron-exon relationships, phylogenetic analysis, overview
P95477
DNA and amino acid sequence analysis and comparison, intron-exon relationships, phylogenetic analysis, overview
P28578
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
-
expression in Escherichia coli
-
cDNA encoding for residues 1-512 of HDC
-
cDNA expression in AGS-B cells
-
DNA and amino acid sequence analysis and comparison, intron-exon relationships, phylogenetic analysis, overview
P16453
expression in COS-7 cells; expression of cDNA in COS-7 cells
-
expression in COS7 cell
-
expression in Escherichia coli
-
mutant enzymes expressed in Escherichia coli
-
DNA and amino acid sequence analysis and comparison, intron-exon relationships, phylogenetic analysis, overview
P54772
expressed in Escherichia coli JM109 (DE3) cells
A9IZZ1
expressed in Lactococcus lactis strain NZ9000 and Escherichia coli DH5alpha cells
-
expressed in Escherichia coli DH5alpha cells
B1B5I3
expressed in Escherichia coli DH5alpha cells
Q75UV3
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
Q56581, Q79JY8
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
12-O-tetradecanoylphorbol-13-acetate induces HDC in mast cells
-
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
Lactobacillus hilgardii ISE 5211
-
-
histidine decarboxylase expression is 2fold higher in the B16F10 melanoma cells as compared to non-cancerous Melan-A cells
-
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
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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
S51A/G58D
-
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
-
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
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
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
Morganella morganii AM-15
-
mutant enzyme His231Asn is 0.2% as active as the wild-type enzyme
-
S229A
Morganella morganii AM-15
-
mutant Ser229Ala or Ser229Cys are about 7% as active as the wild-type enzyme
-
S229C
Morganella morganii AM-15
-
mutant Ser229Ala or Ser229Cys are about 7% as active as the wild-type enzyme
-
C552A
-
site-directed mutagenesis, the mutant shows similar cleavage by caspase-9 as the wild-type enzyme
D517A
-
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
-
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
-
site-directed mutagenesis, the mutant shows reduced cleavage by caspase-9 compared to the wild-type enzyme
K524A
-
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
-
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
-
site-directed mutagenesis, the mutant shows highly reduced cleavage by caspase-9 compared to the wild-type enzyme
D517A
Mus musculus BDF1
-
site-directed mutagenesis, the mutant shows reduced cleavage by caspase-9 compared to the wild-type enzyme
-
D518A
Mus musculus BDF1
-
site-directed mutagenesis, the mutant shows reduced cleavage by caspase-9 compared to the wild-type enzyme
-
T544A/M545A/P546A
Mus musculus BDF1
-
site-directed mutagenesis, the mutant shows highly reduced cleavage by caspase-9 compared to the wild-type enzyme
-
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
-
no enzymatic activity
D543A/D544A
-
mutation in conserved di-aspartate motif. Mutation does not lead to a loss in levels of any of the processed isoforms
DD519A/D520A
-
mutation in conserved di-aspartate motif. Mutation does not lead to a loss in levels of any of the processed isoforms
DELTA517-656
-
C-terminall truncated enzyme is fully active
DELTA517-656/C104S
-
activity is significantly decreased relative to wild-type enzyme
DELTA517-656/C115S
-
activity is significantly decreased relative to wild-type enzyme
DELTA517-656/C254S
-
activity is significantly decreased relative to wild-type enzyme
DELTA517-656/C316S
-
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
-
no activity detectable
DELTA517-656/Q343G344ins
-
no activity detectable
DELTA517-656/Q343ins
-
activity is 2.3fold lower than wild-type activity
DELTA517-656/S307G
-
activity is 13.4fold lower than wild-type activity
H197G
-
mutant retains 10% of the wild type HDC activity
G58N
A9IZZ1
the amino acid change can be responsible for the slow autoactivation and the appearance of HDC in the pi chain form
G58N
Staphylococcus capitis IFIJ12
-
the amino acid change can be responsible for the slow autoactivation and the appearance of HDC in the pi chain form
-
S82A
-
the HdcA mutant mimics the proenzyme
K305G
-
complete loss of activity
additional information
-
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
K232A
-
mutant enzyme Lys232Ala is inactive but retains ability to bind both pyridoxal 5'-phosphate and His efficiently
additional information
-
none of the four residues Met233, Cys230, Cys239 and Ser322 are essential for activity, altough all replacements reduce the activity of the enzyme significantly
H231Q
Morganella morganii AM-15
-
mutant His231Gln is 12% as active as the wild-type enzyme
-
additional information
Morganella morganii AM-15
-
none of the four residues Met233, Cys230, Cys239 and Ser322 are essential for activity, altough all replacements reduce the activity of the enzyme significantly
-
K527A
-
site-directed mutagenesis, the mutant shows reduced cleavage by caspase-9 compared to the wild-type enzyme
additional information
-
construction of deletion mutants with altered activation by butyrate and cleavage by caspase-9, overview
D547A/P548A/F549A
Mus musculus BDF1
-
site-directed mutagenesis, the mutant shows highly reduced cleavage by caspase-9 compared to the wild-type enzyme
-
additional information
Mus musculus BDF1
-
construction of deletion mutants with altered activation by butyrate and cleavage by caspase-9, overview
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
-
confirmatory test for identification of Enterobacter aerogenes
diagnostics
-
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
-
loss of HDC is a marker of malignant transformation and dedifferentiation of B-cells infiltrating the skin
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
-
suppression of histamine signaling by inhibition of HDC may be a novel target of probiotics in preventing allergic diseases
nutrition
E7AXS8
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 75C for 2 min
nutrition
Streptococcus thermophilus PRI60
-
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 75C for 2 min
-