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

Word Map on EC 4.4.1.14
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


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
ethylene biosynthesis I (plants)
-
-
L-methionine salvage cycle II (plants)
-
-
Cysteine and methionine metabolism
-
-
Metabolic pathways
-
-
Biosynthesis of secondary metabolites
-
-
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
animal
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Manually annotated by BRENDA team
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
Sinta
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
-
-
-
Automatic Mining of ENzyme DAta
Citrullus colocynthis x lanatus
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Manually annotated by BRENDA team
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
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
Diospyros sp.
kaki, Thunb. cv.Saijo, persimmon fruit
-
-
Manually annotated by BRENDA team
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
Manila
-
-
Manually annotated by BRENDA team
AAA group, Cavendish subgroup, cv. Grand Nain
-
-
Manually annotated by BRENDA team
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
cv. Hongyanzhenghui, gene PlACS
UniProt
Manually annotated by BRENDA team
-
-
-
Automatic Mining of ENzyme DAta
AHU 8443
-
-
Manually annotated by BRENDA team
-
-
-
Automatic Mining of ENzyme DAta
PG29
SwissProt
Manually annotated by BRENDA team
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
comercial variety Kardinal
SwissProt
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
-
-
-
Automatic Mining of ENzyme DAta
Mill.
-
-
Manually annotated by BRENDA team
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
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-Vinylglycine
L-vinylglyine
-
-
-
methoxyethoxyvinylglycine
-
-
methoxyvinylglycine
-
slight
methylthioadenosine
-
weak
propyl 3,4,5-trihydroxybenzoate
-
-
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
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
auxin
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
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 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
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