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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

Reaction

L-histidine
=
histamine
+
CO2

Synonyms

DCHS, Decarboxylase, histidine, HDC, HdcA, HisDCase, histamine-forming enzyme, L-Histidine decarboxylase, pyruvoyl-dependent decarboxylase, pyruvoyl-dependent histidine decarboxylase, TOM92

ECTree

     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.1 Carboxy-lyases
                4.1.1.22 histidine decarboxylase

Engineering

Engineering on EC 4.1.1.22 - histidine decarboxylase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
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
K305G
complete loss of activity
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
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
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
-
H231Q
-
mutant His231Gln is 12% 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
-
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
S82A
-
the HdcA mutant mimics the proenzyme
additional information