Information on EC 4.4.1.14 - 1-aminocyclopropane-1-carboxylate synthase

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

EC NUMBER
COMMENTARY hide
4.4.1.14
-
RECOMMENDED NAME
GeneOntology No.
1-aminocyclopropane-1-carboxylate synthase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine = 1-aminocyclopropane-1-carboxylate + methylthioadenosine
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
elimination
additional information
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of secondary metabolites
-
-
Cysteine and methionine metabolism
-
-
ethylene biosynthesis I (plants)
-
-
L-methionine salvage cycle II (plants)
-
-
Metabolic pathways
-
-
SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine methylthioadenosine-lyase (1-aminocyclopropane-1-carboxylate-forming)
A pyridoxal-phosphate protein. The enzyme catalyses an alpha,gamma-elimination.
CAS REGISTRY NUMBER
COMMENTARY hide
72506-68-4
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Sinta
-
-
Manually annotated by BRENDA team
Sinta
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
Citrullus colocynthis x lanatus
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Ruby Eyes ‘Golden Star’ and its mericlone mutant, non-high-temperature-induced necrosis (nhn) mutant that is tolerant of high temperatures
SwissProt
Manually annotated by BRENDA team
Thunb.
-
-
Manually annotated by BRENDA team
Diospyros sp.
kaki, Thunb. cv.Saijo, persimmon fruit
-
-
Manually annotated by BRENDA team
cv. Williams82
UniProt
Manually annotated by BRENDA team
isozyme ACS1; Japanese morning glory, formerly Pharbitis nil, cultivar Violet
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
apple
-
-
Manually annotated by BRENDA team
Manila
-
-
Manually annotated by BRENDA team
cv Giant governor
UniProt
Manually annotated by BRENDA team
AAA group, Cavendish subgroup, cv. Grand Nain
-
-
Manually annotated by BRENDA team
tobacco
-
-
Manually annotated by BRENDA team
cv. Hongyanzhenghui, gene PlACS
UniProt
Manually annotated by BRENDA team
AHU 8443
-
-
Manually annotated by BRENDA team
AHU 8443
-
-
Manually annotated by BRENDA team
PG29
SwissProt
Manually annotated by BRENDA team
loblolly pine
Q06IN7 and Q06IN6
UniProt
Manually annotated by BRENDA team
pea
-
-
Manually annotated by BRENDA team
Batsch cultivar Akatsuki
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
comercial variety Kardinal
SwissProt
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
Mill.
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
the enzyme belongs to type-1 subfamily of plant 1-aminocyclopropane-1-carboxylate synthases
metabolism
physiological function
additional information
-
14-3-3 proteins interact with multiple 1-aminocyclopropane-1-carboxylate synthase isoforms in Arabidopsis thaliana, 14-3-3 likely acts on all three classes of enzyme proteins
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(R,S)-S-adenosyl-L-methionine
vinylglycine + methylthioadenosine
show the reaction diagram
(S,S)-S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
show the reaction diagram
L-alanine + pyridoxal 5'-phosphate
pyruvate + pyridoxamine 5'-phosphate
show the reaction diagram
L-arginine + pyridoxal 5'-phosphate
2-oxo-5-guanidinopentanoate + pyridoxamine 5'-phosphate
show the reaction diagram
-
-
-
?
L-aspartate + pyridoxal 5'-phosphate
2-oxo-succinate + pyridoxamine 5'-phosphate
show the reaction diagram
-
very slow transamination activity
-
?
L-phenylalanine + pyridoxal 5'-phosphate
2-oxo-3-phenylpropanoate + pyridoxamine 5'-phosphate
show the reaction diagram
-
slow transamination activity
-
?
L-vinylglycine
2-oxobutanoate + NH4+
show the reaction diagram
-
-
-
-
?
L-vinylglycine
alpha-ketobutyrate + ammonia
show the reaction diagram
pyridoxal 5'-phosphate + alanine
pyridoxamine 5'-phosphate + pyruvate
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
show the reaction diagram
S-methyl-L-methionine
alpha-ketobutyrate + ammonia + dimethylsulfide
show the reaction diagram
S-methyl-L-methionine + pyridoxal 5'-phosphate
4-dimethylsulfonium-2-oxobutyrate + pyridoxamine 5'-phosphate
show the reaction diagram
-
transamination reaction
-
?
vinylglycine
alpha-ketobutyrate + ammonia
show the reaction diagram
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
(R,S)-S-adenosyl-L-methionine
vinylglycine + methylthioadenosine
show the reaction diagram
-
-
-
?
(S,S)-S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
show the reaction diagram
-
-
-
?
L-alanine + pyridoxal 5'-phosphate
pyruvate + pyridoxamine 5'-phosphate
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
show the reaction diagram
S-methyl-L-methionine
alpha-ketobutyrate + ammonia + dimethylsulfide
show the reaction diagram
-
-
-
?
S-methyl-L-methionine + pyridoxal 5'-phosphate
4-dimethylsulfonium-2-oxobutyrate + pyridoxamine 5'-phosphate
show the reaction diagram
-
transamination reaction
-
?
vinylglycine
alpha-ketobutyrate + ammonia
show the reaction diagram
-
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
no effect: Mg2+, Mn2+, Co2+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-aminocyclopropane-1-carboxylate
-
-
1-aminoethoxyvinyl glycine
Citrullus colocynthis x lanatus
-
1-methylcyclopropene
B2XCJ7, B2XCJ8 and B2XCJ9 and B2XCK0, B2XCK1, B2XCK2
completely inhibits the ethylene-associated transcription of isozyme ACS1 in the whole fruit; completely inhibits the ethylene-associated transcription of isozyme ACS4 in the whole fruit
2-(cyclopentylamino)-7,7-dimethyl-7,8-dihydroquinazolin-5(6H)-one
inhibition of ethylene biosynthesis at the step of converting S-adenosylmethionine to 1-aminocyclopropane-1-carboxylic acid by ACC synthase
2-(cyclopentylamino)-7-(4-methylphenyl)-7,8-dihydroquinazolin-5(6H)-one
inhibition of ethylene biosynthesis at the step of converting S-adenosylmethionine to 1-aminocyclopropane-1-carboxylic acid by ACC synthase
2-aminooxyisobutyric acid
-
75% inhibition at 1.1 mM. The compound's action resembles aminooxyacetic acid. The inhibitor significantly increases the vase life of cut flowers by highly reducing the ethylene production through inhibition of the enzyme
-
7-(4-methoxyphenyl)-2-(phenylamino)-7,8-dihydroquinazolin-5(6H)-one
inhibition of ethylene biosynthesis at the step of converting S-adenosylmethionine to 1-aminocyclopropane-1-carboxylic acid by ACC synthase
aminoethoxyvinylglycine
aminooxyacetic acid
chlorpromazine
-
and analogs
EOL1
-
also named ETO1-LIKE 1, directs the degradation of type-2 ACS proteins (ACS4, ACS5 and ACS9) but not of type-1 or type-3 ACSs
-
ethylene
ACS6 is negatively regulated by endogenous and exogenous ethylene
homocysteine
-
slight
L-canaline
-
-
L-Vinylglycine
L-vinylglyine
-
-
-
methoxyethoxyvinylglycine
-
-
methoxyvinylglycine
-
slight
methylthioadenosine
-
weak
propyl 3,4,5-trihydroxybenzoate
-
-
putrescine
-
-
rhizobitoxine
-
-
S-(3-deazaadenosyl)homocysteine
-
-
S-adenosyl-L-homocysteine
-
-
S-adenosyl-L-methionine
S-adenosylhomocysteine
-
-
S-isobutyl-1-deazaadenosine
-
-
S-isobutyl-3-deazaadenosine
-
-
S-isobutyl-7-deazaadenosine
-
-
S-isobutyladenosine
-
-
S-methyl-L-methionine
-
covalent inactivation after elimination of dimethylsulfide
Semicarbazide
-
-
sinefungin
spermidine
-
-
Trifluoperazine
-
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-aminocyclopropane-1-carboxylate
1-naphthyl acetic acid
B2XCJ7, B2XCJ8 and B2XCJ9 and B2XCK0, B2XCK1, B2XCK2
plant tissues treated with 1-naphthyl acetic acid exhibit dramatic increases in isozyme ACS1 mRNA level; plant tissues treated with 1-naphthyl acetic acid exhibit dramatic increases in isozyme ACS3 mRNA level; plant tissues treated with 1-naphthyl acetic acid exhibit dramatic increases in isozyme ACS5 mRNA level
3-indole acetic acid
3-indole butyric acid
B2XCJ7, B2XCJ8 and B2XCJ9 and B2XCK0, B2XCK1, B2XCK2
plant tissues treated with 3-indole butyric acid exhibit dramatic increases in isozyme ACS1 level; plant tissues treated with 3-indole butyric acid exhibit dramatic increases in isozyme ACS3 level; plant tissues treated with 3-indole butyric acid exhibit dramatic increases in isozyme ACS5 level
abscisic acid
-
exogenous treatment with abscisic acid increases the promoter activity of ACS4
cytokinin
B2XCJ7, B2XCJ8 and B2XCJ9 and B2XCK0, B2XCK1, B2XCK2
a dramatic increase in ACS1 transcript levels is detected with increasing cytokinin concentrations (0.004-0.04 mM)
ethylene
gibberellin
indole-3-acetic acid
-
the application of 0.01 mM indole-3-acetic acid on defoliated plants results in increase in ACS activity, the application of 0.1 mM indole-3-acetic acid on no-defoliation and defoliated plants increases ACS activity
iodoacetic acid
Citrullus colocynthis x lanatus
0.05 mM
jasmonic acid
-
exogenous treatment with jasmonic acid increases the promoter activity of ACS4
methylviologen
-
generator of superoxide radicals
xanthine-xanthine oxidase
-
generator of superoxide radicals
-
additional information
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.02
(-)-S-adenosyl-L-methionine
-
-
0.037
(R,S)-S-adenosyl-L-methionine
0.012
(S,S)-S-adenosyl-L-methionine
-
alpha,gamma-elimination
0.026
(S,S)-S-adenosylmethionine
-
alpha,gamma-elimination
37
alanine
-
transamination
35
L-alanine
-
transamination
40
L-arginine
-
transamination
0.27 - 1.4
L-Vinylglycine
0.01 - 1.4
S-adenosyl-L-methionine
4.1
S-methyl-L-methionine
-
beta,gamma-elimination
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.079
(R,S)-S-adenosyl-L-methionine
9.2
(S,S)-S-adenosyl-L-methionine
Malus domestica
-
alpha,gamma-elimination
18
(S,S)-S-adenosylmethionine
Malus domestica
-
alpha,gamma-elimination
0.019
alanine
Malus domestica
-
transamination
0.0025 - 0.0029
L-alanine
0.0012
L-arginine
Malus domestica
-
transamination
0.004 - 1.8
L-Vinylglycine
0.052 - 9.79
S-adenosyl-L-methionine
0.0008 - 0.045
S-methyl-L-methionine
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000015
7-(4-methoxyphenyl)-2-(phenylamino)-7,8-dihydroquinazolin-5(6H)-one
pH 8.0, 25°C
0.000023
aminoethoxyvinylglycine
pH 8.0, 25°C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0079
2-(cyclopentylamino)-7,7-dimethyl-7,8-dihydroquinazolin-5(6H)-one
Arabidopsis thaliana
Q37001
pH 8.0, 25°C
0.0014
2-(cyclopentylamino)-7-(4-methylphenyl)-7,8-dihydroquinazolin-5(6H)-one
Arabidopsis thaliana
Q37001
pH 8.0, 25°C
0.0005
7-(4-methoxyphenyl)-2-(phenylamino)-7,8-dihydroquinazolin-5(6H)-one
Arabidopsis thaliana
Q37001
pH 8.0, 25°C
0.0007
aminoethoxyvinylglycine
Arabidopsis thaliana
Q37001
pH 8.0, 25°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.000000003
-
of the crude cell lysate of the peel at ripening day 2 after treatment with propylene and 1-methylcyclopropene
0.000000013
-
of the crude cell lysate of the peel at ripening day 2 after treatment with propylene
0.000000025
-
of the crude cell lysate of the pulp at ripening day 2 after treatment with propylene
0.000000067
-
of the crude cell lysate of the pulp at ripening day 2 after treatment with propylene and 1-methylcyclopropene
0.00000008
at embryonic stage 6 in the crude cell lysate
0.0000002333
-
control, fresh weight
0.000000315
-
3rd h after 5h of chilling, fresh weight
0.0000003683
-
12th h after 5h of chilling, fresh weight
0.0000004366
-
7th h after 5h of chilling, fresh weight
0.35
-
-
1.5
refolded enzyme
1.85
pH 7.5, 30°C, native enzyme
2.78
pH 7.5, 30°C, enzyme phosphorylated by CPK1
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 10
7 - 9
-
75% and 60% of optimal activity at pH 7.0 and pH 9.0
7.5 - 9.5
-
pH 7.5: about 50% of maximal activity, pH 9.5: about 60% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
24
-
highest enzyme activity in petals at day 10 after cutting
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5
-
isoenzyme ACS
5.74
-
isoenzyme ACS2
5.9
-
isoenzyme ACS2
6
-
isoenzyme ACS1
6.4
-
isoenzyme ACS1
6.41
-
isoenzyme ACS1
6.44
-
isoenzyme ACS5
6.58
-
isoenzyme ACS4
6.63
-
isoenzyme ACS1
6.72
-
isoenzyme ACS2
7.06
-
isoenzyme ACS1
7.3 - 7.4
-
isoenzymes ACS1 and ACS2
7.5
-
isoenzyme ACS5
7.61
-
isoenzyme ACS3
7.86
-
isoenzyme ACS1A
7.9
calculated
8.23
-
isoenzyme ACS1B
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
high expression level
Manually annotated by BRENDA team
Q06IN7 and Q06IN6
-
Manually annotated by BRENDA team
Q06IN7 and Q06IN6
-
Manually annotated by BRENDA team
Q06IN7 and Q06IN6
newly elongated internode shoots prior to needle elongation
Manually annotated by BRENDA team
-
ACC synthase is rapidly induced in excised top portions but no significant ACC synthase activity is observed in excised bottom portions. In top portions, ACC synthase reaches a peak 8 h after harvest and thereafter starts to decline
Manually annotated by BRENDA team
wounded bark; wounded bark; wounded bark
Manually annotated by BRENDA team
Citrullus colocynthis x lanatus
the highest ACS1 transcript level is detected in tendrils
Manually annotated by BRENDA team
Q06IN7 and Q06IN6
-
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
-
associated with particulate fraction
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45000
-
two-dimensional denaturing gel-electrophoresis
53800
-
conceptual translation
57000
-
gel filtration
96000
-
gel filtration
100000
125000
-
gel filtration
160000
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
-
1 * 50000, SDS-PAGE, gel filtration
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
the enzyme harbors an N-glycosylation site
phosphoprotein
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystal structure at 2.4 A resolution
-
crystal structure of ACC synthase in complex with the substrate analogue [2-(aminooxy)ethyl](5'deoxyadenosin-5'-yl)(methyl)sulfonium at 2.01 A resolution, crystals are obtained with the sitting drop method, 0.001 ml of protein solution, consisting of 20 mg/ml ACC synthase, 10 mM [2-(aminooxy)ethyl](5'deoxyadenosin-5'-yl)(methyl)sulfonium, 50 mM HEPES, pH 7.9, 0.01 mM pyridoxal 5'-phosphate, 1 mM dithiothreitol, is mixed with 0.001 ml of precipitating solution containing 30% 2-methyl-2-4-pentanediol and 50 mM MES, pH 6.5
-
recombinant enzyme, cocrystals of the enzyme-L-vinylglycine complex are obtained by sitting drop method. The crystals belong to space group C2 with cell constants a = 103.3 A, b = 59.4 A, c = 79.0 A, beta = 124.2°. The crystal structure of the covalent adduct of the inactivated enzyme is determined at 2.25 A resolution
-
to 1.35 A resolution. The internal aldimine Schiff base linking the C4' atom of the pyridoxal 5'-phosphate cofactor and the side chain nitrogen of K273 in the N'-pyridoxyl-lysine-5'-monophosphate adduct coexists with a small portion, about 20%, of free K273. Modeling of the mutation A46V, corresponding to A57V in Cucumis melo, which results in andromonoecious plants. The mutation changes the structure of the neighbouring active site residues only marginally. The mutation may cause an improper orientation of SAM in the active site
in silico three-dimensional modelling. The overall structure of the modelled binding site for pyridoxal 5'-phosphate and aminoethylvinylglycine in ACS1 is very similar to the known structure for the binding site in apple and tomato ACC synthase. The structures show good conservation of the catalytic residues
in complex with pyridoxal 5'-phosphate and aminoethoxyvinylglycine
-
vapor diffusion method, well buffer consists of 20 mM sodium cacodylate, pH 6.0, 200 mM Li2SO4 and 19-23% polyethylene glycol 3350, crystal structure of ACC synthase complexed with pyridoxal 5'-phosphate and aminoethoxyvinylglycine at 2.7 A resolution
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 7
-
-
34597
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
stable, for at least 3 h
40
-
inactivated above
42
-
50% loss of activity after 15 min
52
-
97% loss of activity after 15 min
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
14-3-3 proteins interact with multiple 1-aminocyclopropane-1-carboxylate synthase isoforms in Arabidopsis thaliana leading to stabilization of the isozymes
-
high phosphate concentrations stabilize
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, potassium buffer, 10 days, 50% activity lost
-
4°C, truncated ACC synthase, at least 6 months, no loss of activity
-
stable for at least 3 days, in ice
-
unstable even during storage at -20°C
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
by (NH4)2SO4 saturation
by centrifugation and Sephadex G-25 column chromatography
by treatment with polyethylene glycol and acetone
Diospyros sp.
-
inclusion body purified
isoenzyme LeACS2 and five ACC synthase mutants (Y151F, Y151G, Y152F, Y152G and Y151F/Y152F) in Escherichia coli
-
partial
recombinant ACC synthase
recombinant C-terminally truncated ACC synthase
-
recombinant protein
recombinant truncated form of ACC synthase
-
treatment with polyethylene glycol and acetone
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cloning of LE-ACS1A into the two-hybrid vector pACT2 in yeast; cloning of LE-ACS2 into the two-hybrid vector pACT2 in yeast; cloning of LE-ACS3 into the two-hybrid vector pACT2 in yeast, the C-terminus of LE-ACS3 is fused to the C-terminus of green fluorescent protein GFP and transformed into rice calli and Arabidopsis by Agrobacterium-mediated transformation; cloning of LE-ACS4 into the two-hybrid vector pACT2 in yeast; cloning of LE-ACS6 into the two-hybrid vector pACT2 in yeast
coexpression of HA-tagged EOL2, HA-tagged isozyme ACS5, and increasing levels of HA-tagged 14-3-3omega protein in Arabidospis thaliana protoplasts, seedling phenotypes, overview
-
DNA and amino acid sequence determination and analysis, genomic structure, sequence comparions and phylogenetic analysis
expressed in Escherichia coli BL21(DE3); expressed in Escherichia coli BL21(DE3); expressed in Escherichia coli BL21(DE3)
expression in Escherichia coli
expression in Escherichia coli and Saccharomyces cerevisiae
expression in Pichia pastoris
-
expression of ACC synthase in Escherichia coli
-
expression of C-terminal deletion mutant in Escherichia coli
-
expression of C-terminal truncated ACCC synthase in Escherichia coli
-
expression of cDNA in Escherichia coli
expression of the tomato isoenzyme Lw-ACS2 in Escherichia coli
-
five clones from one gene existing as a single copy in Carica papaya Sinta genome
-
gene DcACS1, recombinant expression in Escherichia coli
-
gene PpACS1a, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, real-time quantitative PCR expression analysis
into Escherichia coli, pCR2.1-TOPO vector for sequencing; into Escherichia coli, pCR2.1-TOPO vector for sequencing; into Escherichia coli, pCR2.1-TOPO vector for sequencing
into Escherichia coli, pCR2.1-TOPO vector for sequencing; into Escherichia coli, pCR2.1-TOPO vector for sequencing; into Escherichia coli, pCR2.1-TOPO vector for sequencing; into Escherichia coli, pCR2.1-TOPO vector for sequencing; into Escherichia coli, pCR2.1-TOPO vector for sequencing
into Escherichia coli, PMD18-T vector for sequencing
into Escherichia coli, pUC118 or pGEM-T Easy vector for sequencing
-
into plasmid pMOSblue-T
into the pGBKT7 in yeast
isoform ACS5, expression in Escherichia coli
overexpression of C-terminally truncated ACC synthase in Pichia pastoris
-
overexpression of isoenzyme LeACS2 and five ACC synthase mutants (Y151F, Y151G, Y152F, Y152G and Y151F/Y152F) in Escherichia coli
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
ethylene is not a regulatory factor of RiEXPA1 expression in raspberry fruit
expression in fruit skin 116 days after full bloom; expression in fruit skin 16 and 37 days after full bloom
the enzyme expression might be induced by the developmental signal
the PpACS1a gene expression is regulated by salicylic acid and indole-3-acetic acid in fruits and during fruit ripening
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
S460G
level of CPK1 phosphorylation is significantly decreased
S460G/S478A/S481A/S486A
level of CPK1 phosphorylation is significantly decreased
S478A/S481A/S486A
CPK1 phosphorylation efficiency does not significantly change compared to wild-type
A46V
modeling of the mutation, corresponding to A57V in Cucumis melo, which results in andromonoecious plants. The mutation changes the structure of the neighbouring active site residues only marginally. The mutation may cause an improper orientation of SAM in the active site
E47D
-
3.8% of wild-type ACC synthase activity
E47Q
-
0.9% of wild-type ACC synthase activity
G289V
naturally occuring mutation, no activity
K273A
-
no ACC synthase activity
R407L
-
20fold increase in Km for s-adenosyl-l-methionine
Y85F
-
partially active ACC synthase
Y85W
-
partially active ACC synthase
R407K
-
increase in Km for S-adenosyl-L-methionine and drop in kcat/Km
Y233F
-
24-fold increase in the Km for S-adenosyl-L-methionine and no change in kcat
R286A
-
almost complete loss of activity
R286I
-
almost complete loss of activity
R286T
-
almost complete loss of activity
R286V
-
almost complete loss of activity
Y151F
-
activity is reduced by 27%
Y151F/Y152F
-
activity is reduced by 99%
Y151G
-
activity is reduced by 83%
Y152F
-
activity is reduced by 98%
Y152G
-
inactive mutant enzyme
Y92F
-
partially active ACC synthase
Y92H
-
no activity
Y92L
-
no activity
Y92W
-
partially active ACC synthase
additional information
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
refolding by a combination of dialysis and dilution in 100mM MOPS, pH 8, 30 mM Chaps and 5 mM GSH
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
agriculture
food industry
Show AA Sequence (233 entries)
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