Information on EC 1.14.17.4 - aminocyclopropanecarboxylate oxidase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
1.14.17.4
-
RECOMMENDED NAME
GeneOntology No.
aminocyclopropanecarboxylate oxidase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
1-aminocyclopropane-1-carboxylate + ascorbate + O2 = ethylene + cyanide + dehydroascorbate + CO2 + 2 H2O
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
oxidative decarboxylation
-
-
-
-
redox reaction
-
-
-
-
reduction
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of secondary metabolites
-
-
Cysteine and methionine metabolism
-
-
ethylene biosynthesis I (plants)
-
-
Metabolic pathways
-
-
SYSTEMATIC NAME
IUBMB Comments
1-aminocyclopropane-1-carboxylate oxygenase (ethylene-forming)
A nonheme iron enzyme. Requires CO2 for activity. In the enzyme from plants, the ethylene has signalling functions such as stimulation of fruit-ripening.
CAS REGISTRY NUMBER
COMMENTARY hide
98668-53-2
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
kiwi
SwissProt
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
L.
-
-
Manually annotated by BRENDA team
L.
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
cv. Maradol, gene ACCO-1
-
-
Manually annotated by BRENDA team
Cucumis melo cv. Andes
-
-
-
Manually annotated by BRENDA team
gene ACO-1, climacteric plant
-
-
Manually annotated by BRENDA team
Thumb.
-
-
Manually annotated by BRENDA team
cv. Grand Rapids
UniProt
Manually annotated by BRENDA team
fragment; Morus alba L.
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
AVOe3 gene
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
plant
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
pv. glycinea, strain ICMP2189, gene efe
UniProt
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Vicia sp.
vetch
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
-
the enzyme catalyzes the final step in ethylene biosynthesis. The enzyme is involved in the ethylene signal transduction pathway not directly linked to the enzyme reaction
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1-amino-2-ethylcyclopropane-1-carboxylate + L-ascorbate + O2
1-butene + cyanide + dehydroascorbate + CO2 + H2O
show the reaction diagram
1-amino-2-ethylcyclopropane-1-carboxylate + L-ascorbate + O2 + HCO3-
1-butene + cyanide + dehydroascorbate + CO2 + H2O
show the reaction diagram
1-amino-2-methylcyclopropane-1-carboxylate + L-ascorbate + O2
?
show the reaction diagram
1-aminocyclopropane-1-carboxylate + 5,6-O-isopropylidine L-ascorbate + O2
ethylene + cyanide + 5,6-O-isopropylidine L-dehydroascorbate + CO2 + H2O
show the reaction diagram
-
better cosubstrate than L-ascorbate
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + 2 H2O
show the reaction diagram
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
show the reaction diagram
1-aminocyclopropane-1-carboxylate + ascorbate + O2 + H+
ethylene + cyanide + dehydroascorbate + CO2 + H2O
show the reaction diagram
-
-
-
-
?
1-aminocyclopropane-1-carboxylate + D-ascorbate + O2
ethylene + cyanide + D-dehydroascorbate + CO2 + H2O
show the reaction diagram
-
better cosubstrate than L-ascorbate
-
?
1-aminocyclopropane-1-carboxylate + L-ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
show the reaction diagram
1-aminocyclopropane-1-carboxylic acid + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
show the reaction diagram
alpha-aminoisobutyric acid + L-ascorbate + O2
ammonia + acetone + dehydroascorbate + CO2 + H2O
show the reaction diagram
-
-
-
-
?
D-alanine + L-ascorbate + O2
?
show the reaction diagram
-
-
-
-
?
D-alpha-aminobutyric acid + L-ascorbate + O2
ammonia + acetone + dehydroascorbate + CO2 + H2O
show the reaction diagram
-
-
-
-
?
L-alanine + L-ascorbate + O2
?
show the reaction diagram
-
-
-
-
?
L-alpha-aminobutyric acid + L-ascorbate + O2
ammonia + acetone + dehydroascorbate + CO2 + H2O
show the reaction diagram
-
-
-
-
?
N-hydroxy-alpha-aminoisobutyric acid + L-ascorbate + O2
ammonia + acetone + dehydroascorbate + CO2 + H2O
show the reaction diagram
-
-
-
-
?
O2 + 1-aminocyclopropyl-1-carboxylic acid + ascorbate
?
show the reaction diagram
-
assay at pH 7.2, 25C
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + 2 H2O
show the reaction diagram
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
show the reaction diagram
1-aminocyclopropane-1-carboxylate + ascorbate + O2 + H+
ethylene + cyanide + dehydroascorbate + CO2 + H2O
show the reaction diagram
-
-
-
-
?
1-aminocyclopropane-1-carboxylic acid + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ascorbate
isoascorbate
-
may substitute for ascorbate, 75% of the efficiency of ascorbate
additional information
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(1-amino-1-methyl)ethylphosphonic acid
-
competitive inhibitor versus both 1-aminocyclopropane-1-carboxylate and bicarbonate
1,10-phenanthroline
1-aminocyclopropane-1-carboxylate
-
slight inhibition at high concentration
1-aminocyclopropane-1-phosphonic acid
-
competitive inhibitor versus both 1-aminocyclopropane-1-carboxylate and bicarbonate
2,4,6-Trinitrobenzenesulfonate
-
5 mM, 0.7% residual activity
2,4-Dinitrophenol
-
1 mM, 40% residual activity
2-aminoisobutyric acid
competitive inhibitor; competitive inhibitor
2-oxoglutarate
-
at 1 mM
4-Chloromercuriphenylsulfonate
-
1 mM, 1.7% residual activity
8-hydroxyquinoline
-
-
alpha-aminoisobutyric acid
ascorbate
-
required in vitro, inhibitory in vivo
carbonyl sulfide
-
in presence of HCO3-, noncompetitive and irreversible, not at CO2-binding site
catalase
-
-
-
cyanide
-
inhibitory beyond 1 mM
cyclopropyl-1-aminocyclopropane-1-carboxylate
D-alanine
-
competitive to 1-aminocyclopropane-1-carboxylate
D-alpha-aminobutyric acid
-
competitive to 1-aminocyclopropane-1-carboxylate
diethyl dicarbonate
-
complete inactivation at 1.5 mM, pH 6.8, after 20 min
N-ethylmaleimide
-
1 mM, 10% residual activity
n-propyl gallate
N2
-
complete inhibition of enzyme in anaerobic N2-atmosphere, reversible
p-chloromercuribenzoate
-
-
p-Chloromercuriphenylsulfonate
-
-
Salicylhydroxamic acid
-
1 mM, 15% residual activity
additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,4-pteridinediol
-
i.e. lumazine, competitively activates the enzyme with respect to ascorbate
-
ascorbate
bicarbonate
bovine serum albumin
-
stimulates the recombinant enzyme by 41% at 0.1 mM
-
catalase
-
recombinant enzyme, stimulates by 36% at 0.5 mg/ml
-
cyanide
-
the enzyme is activated by cyanide concentrations between 0.1 and 1 mM with most efficient activation at 0.5 mM
dihydrojasmonate
-
exogenously applied onto fruit skin, it induces the enzyme and the ethylene production in fruits at day 0 of ripening, in the climacteric stage at day 20 of ripening at 20C the ethylene production increases without enzyme induction in trested and untreated fruits, overview
dithiothreitol
ethylene
indole acetic acid
-
0.1 mM, increases level of ACO2 transcript in vivo, not ACO1
LiCl
-
1 mM, increases level of ACO2 transcript in vivo, not ACO1
methyl jasmonate
0.02 mM methyl jasmonate increases the activity of the enzyme to 148%. 0.2 mM and 1.0 mM methyl jasmonate increases enzyme activity by 46% and 47%, while 0.05 mM induces a smaller elevation of activity by 21% in tomato fruits; 0.02 mM methyl jasmonate increases the activity of the enzyme to 148%. 0.2 mM and 1.0 mM methyl jasmonate increases enzyme activity by 46% and 47%, while 0.05 mM induces a smaller elevation of activity by 21% in tomato fruits; 0.02 mM methyl jasmonate increases the activity of the enzyme to 148%. 0.2 mM and 1.0 mM methyl jasmonate increases enzyme activity by 46% and 47%, while 0.05 mM induces a smaller elevation of activity by 21% in tomato fruits; 0.02 mM methyl jasmonate increases the activity of the enzyme to 148%. 0.2 mM and 1.0 mM methyl jasmonate increases enzyme activity by 46% and 47%, while 0.05 mM induces a smaller elevation of activity by 21% in tomato fruits
n-propyl dihydrojasmonate
-
-
-
Triton X-100
additional information
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
114
1-amino-2-ethylcyclopropane-1-carboxylate
-
-
0.012 - 2.3
1-aminocyclopropane-1-carboxylate
0.08939 - 0.401
1-aminocyclopropane-1-carboxylic acid
1
5,6-O-isopropylidine L-ascorbate
-
recombinant enzyme, in presence of 5 mM L-ascorbate and 10 mM HCO3-, pH 7.2, 28C
14.7
alpha-aminoisobutyrate
-
recombinant enzyme, pH 7.0, 30C
0.27 - 2.7
ascorbate
1.7
D-ascorbate
-
recombinant enzyme, in presence of 5 mM L-ascorbate and 10 mM HCO3-, pH 7.2, 28C
0.00029 - 0.0053
Fe2+
40
HCO3-
-
-
4.6 - 16.7
L-ascorbate
0.028
O2
-
recombinant isozyme ACO1, in presence of 0.5 mM L-ascorbate and 20 mM CO2/HCO3-, pH 7.2, 25C
additional information
additional information
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00867 - 5.9
1-aminocyclopropane-1-carboxylate
0.0344 - 0.0914
1-aminocyclopropane-1-carboxylic acid
0.07
alpha-aminoisobutyrate
Malus domestica
-
recombinant enzyme, pH 7.0, 30C
0.2
ascorbate
Solanum lycopersicum
-
in 50 mM MOPS, pH 7.0, at 29C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.021
O2
plant
-
-
9
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.3
(1-amino-1-methyl)ethylphosphonic acid
-
in 50 mM MOPS, pH 7.0, at 29C
38.9
1-aminocyclopropane-1-carboxylate
-
recombinant isozyme ACO1, in presence of 5 mM L-ascorbate and 20 mM CO2/HCO3-, pH 7.2, 25C
1.5
1-aminocyclopropane-1-phosphonic acid
-
in 50 mM MOPS, pH 7.0, at 29C
4.2 - 7.5
alpha-aminoisobutyric acid
28
D-alanine
-
pH7.0, 30C
4.2
D-alpha-aminobutyric acid
-
pH 7.0, 30C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0047
-
crude enzyme extract
0.006
-
pear fruit prior homogenization
0.008
-
at 10 mM L-alanine, purified recombinant enzyme
0.011
-
purified enzyme
0.012
partially purified recombinant isozyme ACO3
0.02
-
purified enzyme
0.023
-
at 10 mM D-alanine, purified recombinant enzyme
0.025
partially purified recombinant isozyme ACO1
0.035
-
purified enzyme
0.051
-
at 10 mM alpha-aminoisobutyric acid, purified recombinant enzyme
0.059
-
at 10 mM D-alpha-aminobutyric acid, purified recombinant enzyme
0.073
purified recombinant mutant K172C
0.1
purified recombinant mutant K172A
0.11
purified recombinant mutant G137P
0.13
-
at 10 mM 1-aminocyclopropane-1-carboxylate, purified recombinant enzyme
0.16
purified recombinant wild-type enzyme
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
-
assay at
7 - 7.5
-
-
additional information
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
38
-
2 optima at 28C and 38C
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
the enzyme is partially suppressed in petals and completely in gynoecia at 32C, but expressed at 34C
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
highest expression in ontological younger tissue
Manually annotated by BRENDA team
highest abundance in epithelial cells of cortical resin ducts
Manually annotated by BRENDA team
genes ACO1 and ACO2 are expressed after harvest
Manually annotated by BRENDA team
-
ACO-1 expression analysis in cut flowers, activity during climateric development, overview
Manually annotated by BRENDA team
-
etiolated; isozyme ACO2 level is decreased by wounding; isozymes ACO1 and ACO2, transcripts accumulate constitutively
Manually annotated by BRENDA team
-
wounded and incubated before enzyme extraction
Manually annotated by BRENDA team
-
companion cells associated with metaphloem sieve elements
Manually annotated by BRENDA team
highest abundance in polyphenolic and ray parenchyma cells
Manually annotated by BRENDA team
-
protophloem sieve elements
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
activity is highest during the onset of embryogenesis, and declines gradually afterwards, no activity during desiccation period
Manually annotated by BRENDA team
relative RNA transcript level 8%
Manually annotated by BRENDA team
relative RNA transcript level 10%
Manually annotated by BRENDA team
plant
-
-
Manually annotated by BRENDA team
-
highest expression in ontological younger tissue
Manually annotated by BRENDA team
plant
-
-
Manually annotated by BRENDA team
additional information
PDB
SCOP
CATH
ORGANISM
UNIPROT
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35350
determined by SDA-PAGE and Western blot analysis
35800
calculated from cDNA and confirmed by immunoblotting
35820
-
electron spray mass spectrometry
36310
determined by SDA-PAGE and Western blot analysis
39000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
-
1 * 35000, SDS-PAGE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
apo-enzyme and in complex with Fe(II) or Co(II)
-
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
enzyme has a short half-life under catalytic conditions undergoing metal-catalyzed oxidative fragmentation
-
highly unstable under assay conditions
-
unstable, activity decreases during in vitro incubation with half-life of 9 min
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 30% glycerol, stable for 11 days
-
2C, 30% glycerol, loss of 30% activity after 24 h
-
2C, 30% glycerol, loss of 85% activity after 7 h
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
180fold to near homogeneity
-
ammonium sulfate precipitation, column chromatography, and gel filtration
-
DEAE Sepharose resin column chromatography
-
glutathione-Sepharose chromatography, anion-exchange chromatography
partial
partial, recombinant from Saccharomyces cerevisiae; partial, recombinant from Saccharomyces cerevisiae; partial, recombinant from Saccharomyces cerevisiae
recombinant ACO is purified by affinity chromatography using nickel nitrilotriacetic acid resin, furthermore Sephadex G-25 resin and a Mono-Q column are used, in addition ACO is extracted from apple leaf and fruit tissue; recombinant ACO is purified by affinity chromatography using nickel nitrilotriacetic acid resin, furthermore Sephadex G-25 resin and a Mono-Q column are used, in addition ACO is extracted from apple leaf and fruit tissue; recombinant ACO is purified by affinity chromatography using nickel nitrilotriacetic acid resin, furthermore Sephadex G-25 resin and a Mono-Q column are used, in addition ACO is extracted from apple leaf and fruit tissue
recombinant enzyme from Escherichia coli to homogeneity
-
recombinant from E. coli, 9.8fold to near homogeneity
-
recombinant from Escherichia coli
-
recombinant GST-fusion protein
-
recombinant isozyme ACO1 from Escherichia coli BL21(DE3)-pLysS, to near homogeneity
-
recombinant wild-type enzyme and mutants from Escherichia coli
recombinant wild-type enzyme and mutants from Escherichia coli BL21(DE3) to near homogeneity
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a cDNA library is constructed
expressed in Escherichia coli
-
expressed in Escherichia coli BL21(DE3) cells
expression in antisense orientation under control of the 35S promoter in plum fruits, var. Bluebyrd and Stanley, by transformation of plum hypocotyls, the transgenic plants show reduced response to exogenous ethylene and delayed fruit ripening and softening in some lines
-
expression in Escherichia coli
-
expression in transgenic plants
-
expression of wild-type and mutants in Escherichia coli
gene ACCO-1, DNA and amino acid sequence determination and analysis
-
gene ACO-1, expression analysis in gynoecia and petals from three carnation flowers
-
gene ACO1, antisense expression in Petunia x hybrida using the Agrobacterium tumefaciens strain LBA4404 transfection method
gene ACO1, differential screening of the petal cDNA library, DNA and amino acid sequence determination and analysis, genetic organization, sequence comparisons, phylogenetic analysis, expression analysis, overview; gene ACO2, differential screening of the petal cDNA library, DNA and amino acid sequence determination and analysis, genetic organization, sequence comparisons, phylogenetic analysis, expression analysis, overview; gene ACO3, differential screening of the petal cDNA library, DNA and amino acid sequence determination and analysis, genetic organization, sequence comparisons, phylogenetic analysis, expression analysis, overview; gene ACO4, differential screening of the petal cDNA library, DNA and amino acid sequence determination and analysis, genetic organization, sequence comparisons, phylogenetic analysis, expression analysis, overview; gene ACO5, differential screening of the petal cDNA library, DNA and amino acid sequence determination and analysis, genetic organization, sequence comparisons, phylogenetic analysis, expression analysis, overview
gene efe, expression under the control of Trichoderma reesei cbh1 promoter in Trichoderma viride strain TL124, protoplast transformation, one copy of efe gene is integrated into the chromosomal DNA, expression analysis
GST-tagged version expressed in Escherichia coli BL21
into the vector pGEM-T Easy and subsequently into pProEX-1 for expression of the protein in Escherichia coli BL21 cells; into the vector pGEM-T Easy and subsequently into pProEX-1 for expression of the protein in Escherichia coli BL21 cells; into the vector pGEM-T Easy and subsequently into pProEX-1 for expression of the protein in Escherichia coli BL21 cells
into the vector PMD 18-T for sequencing
isozyme ACO1, DNA sequence determination and analysis, expression in Saccharomyces cerevisiae; isozyme ACO2, DNA sequence determination and analysis, expression in Saccharomyces cerevisiae; isozyme ACO3, DNA sequence determination and analysis, expression in Saccharomyces cerevisiae
isozyme ACO1, overexpression in Escherichia coli BL21(DE3)-pLysS
-
overexpression in Escherichia coli BL21(DE3)
-
wild-type enzyme and mutants, expression in Escherichia coli BL21(DE3)
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
ACO1 transcript accumulation in the lower parts of elongating internodes
-
damage and low-temperature treatment promote the expression of 1-aminocyclopropane-1-carboxylate oxidase
in fruits during ripening stage
mRNA level increased in the primary root after transfer to pH 4.0, addition of 1-aminocyclopropane-1-carboxylic acid or indole-3-acetic acid (at pH 6.0) induce accumulation of mRNA; white light irradation of dark-grown seedlings following transfer to pH 4.0 induces accumulation of mRNA; white light irradation of dark-grown seedlings following transfer to pH 4.0 induces accumulation of mRNA
the mRNA level and enzyme activity are lower in the 9,10-ketol-octadecadienoic acid-treated fruit than in the untreated control at 119 days after full bloom
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D179E
site-directed mutagenesis, 1% activity compared to the recombinant wild-type enzyme
G137P
site-directed mutagenesis, 98% activity compared to the recombinant wild-type enzyme
H177Q
site-directed mutagenesis, 1% activity compared to the recombinant wild-type enzyme
K158A
site-directed mutagenesis, 1% activity compared to the recombinant wild-type enzyme
K158C
site-directed mutagenesis, 1% activity compared to the recombinant wild-type enzyme
K172A
site-directed mutagenesis, 85% activity compared to the recombinant wild-type enzyme
K172C
site-directed mutagenesis, 64% activity compared to the recombinant wild-type enzyme
G289S
the enzyme activity of the mutant is 3times as high as that of the wild type enzyme
H216D
the mutant shows 76% of wild type activity
H216D/D218E
the mutant shows 78% of wild type activity
H216D/D218E/H273Q
the mutant does not completely lose catalytic activity
H273Q
the mutant shows 62% of wild type activity
R287G
the activity of the mutant is remarkably decreased to nearly 40% compared to the wild type enzyme
C133A
-
the mutant showsincreased activity compared to the wild type enzyme
C133P
-
the mutant shows slightly increased activity compared to the wild type enzyme
C165A
-
the mutant shows reduced activity compared to the wild type enzyme
C28A
-
the mutant shows increased activity compared to the wild type enzyme
E294F
-
the mutant shows reduced activity compared to the wild type enzyme
E297L
-
the mutant shows strongly increased activity compared to the wild type enzyme
E301D
-
the mutant shows reduced activity compared to the wild type enzyme
E301L
-
the mutant shows reduced activity compared to the wild type enzyme
F187Y
-
the mutant shows increased activity compared to the wild type enzyme
F300Q
-
the mutant shows reduced activity compared to the wild type enzyme
F300Y
-
the mutant shows reduced activity compared to the wild type enzyme
K144E
-
the mutant shows reduced activity compared to the wild type enzyme
K158E
-
the mutant shows reduced activity compared to the wild type enzyme
K158L
-
the mutant shows reduced activity compared to the wild type enzyme
K158Q
-
the mutant shows reduced activity compared to the wild type enzyme
K158Q/R175E
-
the mutant shows reduced activity compared to the wild type enzyme
K158Q/R175Q
-
the mutant shows reduced activity compared to the wild type enzyme
K158R
-
the mutant shows reduced activity compared to the wild type enzyme
K158R/R175Q
-
the mutant shows reduced activity compared to the wild type enzyme
K172E
-
the mutant shows reduced activity compared to the wild type enzyme
K199E
-
the mutant shows reduced activity compared to the wild type enzyme
K230E
-
the mutant shows reduced activity compared to the wild type enzyme
K230Q
-
the mutant shows reduced activity compared to the wild type enzyme
K230R
-
the mutant shows reduced activity compared to the wild type enzyme
K292E
-
the mutant shows reduced activity compared to the wild type enzyme
K292R
-
the mutant shows reduced activity compared to the wild type enzyme
K296E
-
the mutant shows increased activity compared to the wild type enzyme
N216F
-
the mutant shows reduced activity compared to the wild type enzyme
P298A
-
the mutant shows strongly increased activity compared to the wild type enzyme
Q188A
-
the mutant shows reduced activity compared to the wild type enzyme
Q188K
-
the mutant shows reduced activity compared to the wild type enzyme
Q188N
-
the mutant shows reduced activity compared to the wild type enzyme
R175A
-
the mutant shows reduced activity compared to the wild type enzyme
R175E
-
the mutant shows reduced activity compared to the wild type enzyme
R175E/R244K
-
the mutant shows reduced activity compared to the wild type enzyme
R175E/S246A
-
the mutant shows reduced activity compared to the wild type enzyme
R175E/T157A
-
the mutant shows reduced activity compared to the wild type enzyme
R175G
-
the mutant shows reduced activity compared to the wild type enzyme
R175H
-
the mutant shows reduced activity compared to the wild type enzyme
R175K
-
the mutant shows reduced activity compared to the wild type enzyme
R175Q
-
the mutant shows reduced activity compared to the wild type enzyme
R244A
-
enzymic activity about 20% of wild-type
R244G
-
enzymic activity about 20% of wild-type
R244K/S246A
-
the mutant shows reduced activity compared to the wild type enzyme
R244K/S246A/T157A
-
the mutant shows reduced activity compared to the wild type enzyme
R244K/T157A
-
the mutant shows reduced activity compared to the wild type enzyme
R299E
-
inactive
R299H
-
the mutant shows reduced activity compared to the wild type enzyme
R299K
-
the mutant shows reduced activity compared to the wild type enzyme
R299L
-
the mutant shows reduced activity compared to the wild type enzyme
S246F
-
enzymic activity less than 5% of wild-type
S246G
-
enzymic activity about 50% of wild-type
S246T
-
enzymic activity less than 5% of wild-type
S246Y
-
enzymic activity less than 5% of wild-type
S257A
-
KM-value similar to wild-type
V159G
-
enzymic activity about 30% of wild-type
W203F
-
the mutant shows reduced activity compared to the wild type enzyme
Y251F
-
the mutant shows reduced activity compared to the wild type enzyme
D179E
-
site-directed mutagenesis, very low activity, stimulation by bicarbonate
D179N
-
site-directed mutagenesis, no activity
H177D
-
site-directed mutagenesis, no activity
H177D/D179E
-
site-directed mutagenesis, no activity
H177E
-
site-directed mutagenesis, very low activity, stimulation by bicarbonate
H177Q
-
site-directed mutagenesis, no activity
H211Q
-
site-directed mutagenesis, slightly reduced activity
H234D
-
site-directed mutagenesis, no activity
H234E
-
site-directed mutagenesis, no activity
H234Q
-
site-directed mutagenesis, no activity
H39Q
-
site-directed mutagenesis, slightly reduced activity
H56Q
-
site-directed mutagenesis, activity similar to the wild-type
H94Q
-
site-directed mutagenesis, slightly reduced activity
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
agriculture
Show AA Sequence (112 entries)
Please use the Sequence Search for a certain query.