Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 4.1.1.22 - histidine decarboxylase and Organism(s) Mus musculus and UniProt Accession P23738

for references in articles please use BRENDA:EC4.1.1.22
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.1 Carboxy-lyases
                4.1.1.22 histidine decarboxylase
IUBMB Comments
A pyridoxal-phosphate protein (in animal tissues). The bacterial enzyme has a pyruvoyl residue as prosthetic group.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Mus musculus
UNIPROT: P23738
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
hide
The taxonomic range for the selected organisms is: Mus musculus
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
hide
L-histidine
=
histamine
+
CO2
=
+
Synonyms
hdc, histidine decarboxylase, l-histidine decarboxylase, histamine-forming enzyme, hisdcase, pyruvoyl-dependent histidine decarboxylase, pyruvoyl-dependent decarboxylase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Decarboxylase, histidine
-
-
-
-
HisDCase
-
-
-
-
histamine-forming enzyme
-
-
L-Histidine decarboxylase
-
-
-
-
TOM92
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
decarboxylation
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
L-histidine carboxy-lyase (histamine-forming)
A pyridoxal-phosphate protein (in animal tissues). The bacterial enzyme has a pyruvoyl residue as prosthetic group.
CAS REGISTRY NUMBER
COMMENTARY hide
9024-61-7
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-histidine
histamine + CO2
show the reaction diagram
-
-
-
?
L-His
Histamine + CO2
show the reaction diagram
L-histidine
histamine + CO2
show the reaction diagram
additional information
?
-
-
mast cells are known to produce histamine through a difference mechanism than HDC induction
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-histidine
histamine + CO2
show the reaction diagram
-
-
-
?
L-histidine
histamine + CO2
show the reaction diagram
additional information
?
-
-
mast cells are known to produce histamine through a difference mechanism than HDC induction
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
pyridoxal 5'-phosphate
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
alpha-Fluoromethylhistidine
-
-
Histidine methyl ester
-
-
Shoyuflavones
-
isolated from soy sauce
additional information
-
knockdown of the transcription factor C/EBPbeta by dehydroxymethylepoxyquinomicin reduces the HDC expression in lipopolysaccharide-treated cells
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
monosodium urate
monosodium urate crystals injected into the air pouch lead to a highly upregulated mRNA level of HDC
-
Butyrate
-
highly activating for the wild-type enzyme
C/EBPbeta
-
essential for the HDC induction
-
lipopolysaccharide
-
excreted from Escherichia coli after oral infection, stimulates the enzyme in dental pulp and gingiva, tissue-specific effects, oveview
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.26 - 0.29
L-His
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.75
-
-
0.8
-
-
166
-
-
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.2
-
-
6.6
-
-
6.7
-
assay at
6.8
-
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 7.6
-
pH 6.0: about 50% of maximal activity, pH 7.6: about 40% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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
quadriceps femoris
Manually annotated by BRENDA team
masseter, pectoralis, and quadriceps femoris, in cells in the endomysium and around blood vessels, and also in some muscle fibers
Manually annotated by BRENDA team
-
high levels of HDC protein are also found in the striatum
Manually annotated by BRENDA team
-
HDC mRNA is highly expressed in the posterior hypothalamus
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
-
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
-
peritoneal cavity
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
additional information
immunostaining of HDC in murine skeletal muscle tissues, overview
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
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
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
DCHS_MOUSE
662
0
74045
Swiss-Prot
other Location (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100000
-
gel filtration
110000
-
gel filtration
115000
-
native PAGE
53000
54000
55000
-
2 * 55000, SDS-PAGE
74000
-
2 * 53000, SDS-PAGE, 2 * 74000, recombinant 5-3fold FLAG-tagged and 3-HA-tagged enzyme, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 54000, processed HDC protein, SDS-PAGE
dimer
additional information
structure-function relationship, molecular modeling, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
K527A
-
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
additional information
-
construction of deletion mutants with altered activation by butyrate and cleavage by caspase-9, overview
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 50 mM potassium phosphate, pH 6.8, 0.2 mM dithiothreitol, 0.01 mM pyridoxal 5'-phosphate, 2% polyethylene glycol, stable for at least 3 months, even at a low protein concentration, 0.01 mg/ml
-
0°C, 50 mM potassium phosphate, pH 6.8, 0.2 mM dithiothreitol, 0.01 mM pyridoxal 5'-phosphate, 2% polyethylene glycol No. 300, withoout significant loss of enzyme activity after 2 weeks
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
partially purified 53000 Da HDC
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
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
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
induction of the histamine-forming enzyme histidine decarboxylase in skeletal muscles by prolonged muscular work, interleukin-1beta (IL-1beta) and TNF-alpha may cooperatively mediate this induction. IL-1beta increases HDC activity in all the muscles tested (masseter, pectoralis, and quadriceps femoris). HDC activity in these tissues peaks at around 5 h after the injection of IL-1beta (10 ng/g), injection of TNF-alpha (100 ng/g) also increases HDC activity in all of these muscles
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
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Aures, D.; Hakanson, R.
Histidine decarboxylase (mammalian)
Methods Enzymol.
17B
667-677
1971
Mus musculus, Rattus norvegicus
-
Manually annotated by BRENDA team
Martin, S.A.M.; Bishop, J.O.
Purification and characterization of histidine decarboxylase from mouse kidney
Biochem. J.
234
349-354
1986
Mus musculus
Manually annotated by BRENDA team
Yamamoto, J.; Fukui, T.; Suzuki, K.; Tanaka, S.; Yatsunami, K.; Ichikawa, A.
Expression and characterization of recombinant mouse mastocytoma histidine decarboxylase
Biochim. Biophys. Acta
1216
431-40
1993
Mus musculus
Manually annotated by BRENDA team
Kinoshita, E.; Saito, M.
Novel histamine measurement by HPLC analysis used to assay histidine decarboxylase inhibitory activity of shoyuflavones
Biosci. Biotechnol. Biochem.
62
1488-1491
1998
Clostridium perfringens, Mus musculus
Manually annotated by BRENDA team
Ohmori, E.; Fukui, T.; Imanishi, N.; Yatsunami, K.; Ichikawa, A.
Purification and characterization of L-histidine decarboxylase from mouse mastocytoma P-815 cells
J. Biochem.
107
834-839
1990
Mus musculus
Manually annotated by BRENDA team
Watabe, A.; Fukui, T.; Ohmori, E.; Ichikawa, A.
Purification and properties of L-histidine decarboxylase from mouse stomach
Biochem. Pharmacol.
43
587-593
1992
Mus musculus
Manually annotated by BRENDA team
Hirasawa, N.; Murakami, A.; Ohuchi, K.
Expression of 74-kDa histidine decarboxylase protein in a macrophage-like cell line RAW 264.7 and inhibition by dexamethasone
Eur. J. Pharmacol.
418
23-28
2001
Mus musculus
Manually annotated by BRENDA team
Ayada, K.; Oguri, S.; Yamaguchi, K.; Kumagai, K.; Endo, Y.
Elevation of histidine decarboxylase activity in the stomach of mice by ulcerogenic drugs
Eur. J. Pharmacol.
460
63-69
2003
Mus musculus
Manually annotated by BRENDA team
Yamaguchi, K.; Motegi, K.; Kurimoto, M.; Endo, Y.
Induction of the activity of the histamine-forming enzyme, histidine decarboxylase, in mice by IL-18 and by IL-18 plus IL-12
Inflamm. Res.
49
513-519
2000
Mus musculus
Manually annotated by BRENDA team
Safina, F.; Tanaka, S.; Inagaki, M.; Tsuboi, K.; Sugimoto, Y.; Ichikawa, A.
Expression of L-histidine decarboxylase in mouse male germ cells
J. Biol. Chem.
277
14211-14215
2002
Mus musculus
Manually annotated by BRENDA team
Wagner, W.; Fogel, W.A.
Mammary histidine decarboxylase vulnerability to enzyme antisense oligonucleotides: histamine and polyamine systems cross-talk
Amino Acids
26
311-316
2004
Mus musculus (P23738), Mus musculus
Manually annotated by BRENDA team
Tanaka, S.; Deai, K.; Konomi, A.; Takahashi, K.; Yamane, H.; Sugimoto, Y.; Ichikawa, A.
Expression of L-histidine decarboxylase in granules of elicited mouse polymorphonuclear leukocytes
Eur. J. Immunol.
34
1472-1482
2004
Mus musculus
Manually annotated by BRENDA team
Pos, Z.; Mller, K.; Novalphak, I.; Buzas, E.; Solbach, W.; Falus, A.; Laskay, T.
Different patterns of the L-histidine decarboxylase (HDC) gene expression in mice resistant and susceptible to experimental cutaneous leishmaniasis
Inflamm. Res.
53
38-43
2004
Mus musculus
Manually annotated by BRENDA team
Fogel, W.A.; Dudkowska, M.; Wagner, W.; Grzelakowska-Sztabert, B.; Manteuffel-Cymborowska, M.
Ornithine and histidine decarboxylase: Activities in hypertrophic and hyperplastic mouse kidney
Inflamm. Res.
54
S62-S63
2005
Mus musculus
-
Manually annotated by BRENDA team
Shoji, N.; Yoshida, A.; Yu, Z.; Endo, Y.; Sasano, T.
Lipopolysaccharide stimulates histamine-forming enzyme (histidine decarboxylase) activity in murine dental pulp and gingiva
Arch. Oral Biol.
51
856-860
2006
Mus musculus
Manually annotated by BRENDA team
Furuta, K.; Ichikawa, A.; Nakayama, K.; Tanaka, S.
Membrane orientation of the precursor 74-kDa form of L-histidine decarboxylase
Inflamm. Res.
55
185-191
2006
Mus musculus
Manually annotated by BRENDA team
Deng, X.; Wu, X.; Yu, Z.; Arai, I.; Sasano, T.; Sugawara, S.; Endo, Y.
Inductions of histidine decarboxylase in mouse tissues following systemic antigen challenge: contributions made by mast cells, non-mast cells and IL-1
Int. Arch. Allergy Immunol.
144
69-78
2007
Mus musculus
Manually annotated by BRENDA team
Furuta, K.; Nakayama, K.; Sugimoto, Y.; Ichikawa, A.; Tanaka, S.
Activation of histidine decarboxylase through post-translational cleavage by caspase-9 in a mouse mastocytoma P-815
J. Biol. Chem.
282
13438-13446
2007
Mus musculus, Mus musculus BDF1
Manually annotated by BRENDA team
Okigami, H.; Ueno, H.
Bioinformatic study on histidine decarboxylase
J. Biol. Macromol.
6
11-27
2006
Morganella morganii (P05034), Rattus norvegicus (P16453), Homo sapiens (P19113), Klebsiella aerogenes (P28577), Raoultella planticola (P28578), Solanum lycopersicum (P54772), Pseudomonas fluorescens (P95477), Drosophila melanogaster (Q05733), Vibrio anguillarum (Q56581), Vibrio anguillarum (Q79JY8), Gloeobacter violaceus (Q7NIG4), Mus musculus (Q7TMW5), Photobacterium phosphoreum (Q846V2), Aplysia californica (Q86BW8), Clostridium tetani (Q894Q7), Oryza sativa (Q8RV06), Mesorhizobium loti (Q98A07), Arabidopsis thaliana (Q9MA74)
-
Manually annotated by BRENDA team
Pessler, F.; Mayer, C.T.; Jung, S.M.; Behrens, E.M.; Dai, L.; Menetski, J.P.; Schumacher, H.R.
Identification of novel monosodium urate crystal regulated mRNAs by transcript profiling of dissected murine air pouch membranes
Arthritis Res. Ther.
10
R64
2008
Mus musculus (P23738), Mus musculus
Manually annotated by BRENDA team
Suzuki, E.; Ninomiya, Y.; Umezawa, K.
Induction of histidine decarboxylase in macrophages inhibited by the novel NF-kappaB inhibitor (-)-DHMEQ
Biochem. Biophys. Res. Commun.
379
379-383
2009
Mus musculus
Manually annotated by BRENDA team
Zhao, C.; Martinez, V.; Piqueras, L.; Wang, L.; Tache, Y.; Chen, D.
Control of gastric acid secretion in somatostatin receptor 2 deficient mice: shift from endocrine/paracrine to neurocrine pathways
Endocrinology
149
498-505
2008
Mus musculus
Manually annotated by BRENDA team
Szebeni, A.; Prohaszka, Z.; Buzas, E.; Falus, A.; Kecskemeti, V.
Effects of vaccination with heat shock proteins on streptozotocin induced diabetes in histidine decarboxylase knockout mice
Inflamm. Res.
57
178-182
2008
Mus musculus
Manually annotated by BRENDA team
Beghdadi, W.; Porcherie, A.; Schneider, B.S.; Dubayle, D.; Peronet, R.; Huerre, M.; Watanabe, T.; Ohtsu, H.; Louis, J.; Mecheri, S.
Inhibition of histamine-mediated signaling confers significant protection against severe malaria in mouse models of disease
J. Exp. Med.
205
395-408
2008
Mus musculus
Manually annotated by BRENDA team
Leite-de-Moraes, M.C.; Diem, S.; Michel, M.L.; Ohtsu, H.; Thurmond, R.L.; Schneider, E.; Dy, M.
Cutting edge: Histamine receptor H4 activation positively regulates in vivo IL-4 and IFN-gamma production by invariant NKT cells
J. Immunol.
182
1233-1236
2009
Mus musculus
Manually annotated by BRENDA team
Davis, S.C.; Clark, S.; Hayes, J.R.; Green, T.L.; Gruetter, C.A.
Up-regulation of histidine decarboxylase expression and histamine content in B16F10 murine melanoma cells
Inflamm. Res.
60
55-61
2011
Mus musculus
Manually annotated by BRENDA team
Funayama, H.; Huang, L.; Asada, Y.; Endo, Y.; Takada, H.
Enhanced induction of a histamine-forming enzyme, histidine decarboxylase, in mice primed with NOD1 or NOD2 ligand in response to various Toll-like receptor agonists
Innate Immun.
16
265-272
2010
Mus musculus
Manually annotated by BRENDA team
Krusong, K.; Ercan-Sencicek, A.G.; Xu, M.; Ohtsu, H.; Anderson, G.M.; State, M.W.; Pittenger, C.
High levels of histidine decarboxylase in the striatum of mice and rats
Neurosci. Lett.
495
110-114
2011
Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Pino-Angeles, A.; Morreale, A.; Negri, A.; Sanchez-Jimenez, F.; Moya-Garcia, A.
Substrate uptake and protein stability relationship in mammalian histidine decarboxylase
Proteins
78
154-161
2010
Mus musculus
Manually annotated by BRENDA team
Ayada, K.; Tsuchiya, M.; Yoneda, H.; Yamaguchi, K.; Kumamoto, H.; Sasaki, K.; Tadano, T.; Watanabe, M.; Endo, Y.
Induction of the histamine-forming enzyme histidine decarboxylase in skeletal muscles by prolonged muscular work histological demonstration and mediation by cytokines
Biol. Pharm. Bull.
40
1326-1330
2017
Mus musculus (P23738), Mus musculus BALB/c (P23738)
Manually annotated by BRENDA team