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
Engineering
Engineering 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.
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
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
K232A
-
mutant enzyme Lys232Ala is inactive but retains ability to bind both pyridoxal 5'-phosphate and His efficiently
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
-
mutant enzyme His231Asn is 0.2% as active as the wild-type enzyme
-
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
-
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
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
-
D547A/P548A/F549A
-
site-directed mutagenesis, the mutant shows highly 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
-
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/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
G58N
additional information
-
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
the amino acid change can be responsible for the slow autoactivation and the appearance of HDC in the pi chain form
G58N
-
the amino acid change can be responsible for the slow autoactivation and the appearance of HDC in the pi chain form
-
-
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
additional information
the mutation of a stop codon after W317 in gene hdc leads to a truncated enzyme and the Tourette syndrome
additional information
-
the mutation of a stop codon after W317 in gene hdc leads to a truncated enzyme and the Tourette syndrome
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
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
-
additional information
-
construction of deletion mutants with altered activation by butyrate and cleavage by caspase-9, overview
additional information
-
construction of deletion mutants with altered activation by butyrate and cleavage by caspase-9, overview
-