4.1.1.22: histidine decarboxylase
This is an abbreviated version!
For detailed information about histidine decarboxylase, go to the full flat file.
Word Map on EC 4.1.1.22
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4.1.1.22
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high-dose
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mast
-
autologous
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histaminergic
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mucosa
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stomach
-
gastrin
-
marrow
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alpha-fluoromethylhistidine
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hypothalamus
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hematopoietic
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enterochromaffin-like
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cyclophosphamide
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oxyntic
-
allergic
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etoposide
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biogenic
-
relapsed
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chromogranin
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thiotepa
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basophil
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decarboxylases
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melphalan
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cimetidine
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tuberomammillary
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carboplatin
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pyrilamine
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stem-cell
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omeprazole
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event-free
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hypergastrinemia
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h1-receptors
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morganii
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morganella
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thioperamide
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mucositis
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carmustine
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standard-dose
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busulfan
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pentagastrin
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tourette
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mepyramine
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sleep-wake
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fundic
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mastocytoma
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reinfusion
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cell-deficient
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drug development
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medicine
-
aminergic
-
diagnostics
-
nutrition
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chlorpheniramine
-
snell
- 4.1.1.22
-
high-dose
-
mast
-
autologous
-
histaminergic
- mucosa
- stomach
- gastrin
- marrow
- alpha-fluoromethylhistidine
- hypothalamus
-
hematopoietic
-
enterochromaffin-like
- cyclophosphamide
-
oxyntic
-
allergic
- etoposide
-
biogenic
-
relapsed
-
chromogranin
-
thiotepa
-
basophil
- decarboxylases
- melphalan
- cimetidine
-
tuberomammillary
- carboplatin
-
pyrilamine
-
stem-cell
- omeprazole
-
event-free
-
hypergastrinemia
-
h1-receptors
- morganii
- morganella
- thioperamide
- mucositis
- carmustine
-
standard-dose
-
busulfan
- pentagastrin
- tourette
-
mepyramine
-
sleep-wake
- fundic
- mastocytoma
-
reinfusion
-
cell-deficient
- drug development
- medicine
-
aminergic
- diagnostics
- nutrition
-
chlorpheniramine
-
snell
Reaction
Synonyms
DCHS, Decarboxylase, histidine, HDC, HdcA, HisDCase, histamine-forming enzyme, L-Histidine decarboxylase, pyruvoyl-dependent decarboxylase, pyruvoyl-dependent histidine decarboxylase, TOM92
ECTree
4.1.1.22 histidine decarboxylaseAdvanced search results
results (
results (Subunits
Subunits on EC 4.1.1.22 - histidine decarboxylase
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SUBUNIT 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
dimer
dodecamer
hexamer
monomer
-
1 * 54000, enzyme from soluble fraction, SDS-PAGE in absence of 2-mercaptoethanol
multimer
tetramer
additional information
?
-
x * 74000, enzyme from particulate fraction, SDS-PAGE in absence of 2-mercaptoethanol
dimer
-
2 * 53000, SDS-PAGE, 2 * 74000, recombinant 5'-3fold FLAG-tagged and 3'-HA-tagged enzyme, SDS-PAGE
dimer
-
2 * 53000, SDS-PAGE, 2 * 74000, recombinant 5'-3fold FLAG-tagged and 3'-HA-tagged enzyme, SDS-PAGE
-
dimer
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2 * 53000-58000, SDS-PAGE, the exact sequence of each monomer is not known
dodecamer
-
6 * 24892, alpha, + 6 * 8856, beta, calculation from amino acid sequence
hexamer
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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
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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
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multimer
putative alpha-chain of 27-30 kDa, beta-chain of 7-9 kDa, and a third 35-37 kDa band, SDS-PAGE
multimer
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putative alpha-chain of 27-30 kDa, beta-chain of 7-9 kDa, and a third 35-37 kDa band, SDS-PAGE
-
additional information
structure-function relationship, molecular modeling, overview
additional information
structure-function relationship, molecular modeling, overview
additional information
structure-function relationship, molecular modeling, overview
additional information
structure-function relationship, molecular modeling, overview
additional information
structure-function relationship, molecular modeling, overview
additional information
structure-function relationship, molecular modeling, overview
additional information
the 150 amino acid long C-terminal region present in mammalian HDC but absent in homologous Gram-negative bacteria HDC and all mammalian DDCs. The C-terminus has not got a well-defined secondary structure and it must be removed to reach the active conformation of mammalian HDC. The C-terminus is probably required for sorting the enzyme to the endoplasmic reticulum (ER), after which it can be removed to render the active form of the enzyme located in ER lumen
additional information
-
the 150 amino acid long C-terminal region present in mammalian HDC but absent in homologous Gram-negative bacteria HDC and all mammalian DDCs. The C-terminus has not got a well-defined secondary structure and it must be removed to reach the active conformation of mammalian HDC. The C-terminus is probably required for sorting the enzyme to the endoplasmic reticulum (ER), after which it can be removed to render the active form of the enzyme located in ER lumen
additional information
structure-function relationship, molecular modeling, overview
additional information
-
a pyruvate-free proenzyme pi-chain, MW: 37000, is converted during activation to a beta-chain, MW 9000, with a carboxy-terminal Ser residue and an alpha-chain, MW: 28000, with a pyruvoyl group blocking the amino-terminus
additional information
structure-function relationship, molecular modeling, overview
additional information
structure-function relationship, molecular modeling, overview
additional information
structure-function relationship, molecular modeling, overview
additional information
structure-function relationship, molecular modeling, overview
additional information
structure-function relationship, molecular modeling, overview
additional information
structure-function relationship, molecular modeling, overview
additional information
structure-function relationship, molecular modeling, overview
additional information
-
five HDC isoforms of 63000 Da, 54000 Da, 48000 Da, 40000 Da and 36000 Da, that derive from the 74000 Da full-length primary translation isoform
additional information
structure-function relationship, molecular modeling, overview
additional information
structure-function relationship, molecular modeling, overview
additional information
structure-function relationship, molecular modeling, overview
additional information
structure-function relationship, molecular modeling, overview
