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
-
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
- 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
Advanced search results
Reaction
Reaction on EC 4.1.1.22 - histidine decarboxylase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
L-histidine = histamine + CO2
structure-activity relationship, active site structure, molecular modeling, the imidazole ring is located in a pocket composed of residues Tyr-81B, Asn-302B, Ser-304B, Lys-305B, Leu-102A, Phe-104A, and Ser-354A
L-histidine = histamine + CO2
catalytic mechanism, quantum mechanics-molecular mechanics study and molecular dynamics simulations using the enzyme's crystal structure, PDB ID 4E1O, overview. The reaction involves two sequential steps: the decarboxylation of L-histidine and the protonation of the generated intermediate from which results histamine. The rate-limiting step is the first one with an activation barrier of 17.9 kcal/mol. In contrast, the second step is very fast and exergonic. When the substrate L-histidine is available in the active site of HDC, it binds to the pyridoxal 5'-phosphate cofactor. In this process, the imine bond formed between pyridoxal 5'-phosphate and Lys305A is cleaved and a new external aldimine intermediate is created between the pyridoxal 5'-phosphate cofactor and the amino group of the substrate