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Information on EC 4.4.1.14 - 1-aminocyclopropane-1-carboxylate synthase and Organism(s) Malus domestica and UniProt Accession P37821

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EC Tree
IUBMB Comments
A pyridoxal 5'-phosphate protein. The enzyme catalyses an alpha,gamma-elimination.
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This record set is specific for:
Malus domestica
UNIPROT: P37821
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The taxonomic range for the selected organisms is: Malus domestica
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
acc synthase, 1-aminocyclopropane-1-carboxylate synthase, 1-aminocyclopropane-1-carboxylic acid synthase, mdacs1, le-acs2, acs-1, leacs2, le-acs4, le-acs3, ghacs1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1-aminocyclopropane-1-carboxylate synthase
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1-aminocyclopropane-1-carboxylate synthase
1-aminocyclopropane-1-carboxylate synthetase
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-
-
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1-aminocyclopropane-1-carboxylic acid synthase
-
-
-
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1-aminocyclopropanecarboxylate synthase
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-
-
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ACC synthase
aminocyclopropane-1-carboxylate synthase
-
-
-
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aminocyclopropanecarboxylate synthase
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-
-
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aminocyclopropanecarboxylic acid synthase
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-
-
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S-adenosyl-L-methionine methylthioadenosine-lyase
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-
-
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S-adenosyl-L-methionine methylthioadenosine-lyase (1-aminocyclopropane-1-carboxylate-forming)
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-
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synthase, 1-aminocyclopropanecarboxylate
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-
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine S-methyl-5'-thioadenosine-lyase (1-aminocyclopropane-1-carboxylate-forming)
A pyridoxal 5'-phosphate protein. The enzyme catalyses an alpha,gamma-elimination.
CAS REGISTRY NUMBER
COMMENTARY hide
72506-68-4
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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
NATURAL SUBSTRATE
NATURAL 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
-
-
-
?
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
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
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
pyridoxal 5'-phosphate
-
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(2E,3E)-4-(2-aminoethoxy)-2-[([3-hydroxy-2-methyl-5[(phosphonooxy)methyl]pyridin-4-yl]methyl)imino] but-3-enoic acid
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best inhibitor tested
2-amino-7-(4-methylphenyl)-7,8-dihydro-5(6H)-quinazolinone
-
uncompetitive
2-[(3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl)-imino]-5-phosphonopent-3-enoic acid
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strong binding capacity
L-Vinylglycine
S-methyl-L-methionine
-
covalent inactivation after elimination of dimethylsulfide
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.037
(R,S)-S-adenosyl-L-methionine
-
beta,gamma-elimination
0.037
(R,S)-S-adenosylmethionine
-
beta,gamma-elimination
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
0.012
S-adenosyl-L-methionine
-
elimination
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
-
beta,gamma-elimination
0.079
(R,S)-S-adenosylmethionine
-
beta,gamma-elimination
9.2
(S,S)-S-adenosyl-L-methionine
-
alpha,gamma-elimination
18
(S,S)-S-adenosylmethionine
-
alpha,gamma-elimination
0.019
alanine
-
transamination
0.0025 - 0.0029
L-alanine
0.0012
L-arginine
-
transamination
0.004 - 1.8
L-Vinylglycine
9.2
S-adenosyl-L-methionine
-
elimination
0.0008 - 0.045
S-methyl-L-methionine
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
1A1C_MALDO
473
0
53251
Swiss-Prot
other Location (Reliability: 5)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50000
x * 50000, two-dimensional electrophoresis
52000
-
2 * 52000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 50000, two-dimensional electrophoresis
dimer
-
2 * 52000, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
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
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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
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
Y233F
Y85F
-
partially active ACC synthase
Y85W
-
partially active ACC synthase
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, truncated ACC synthase, at least 6 months, no loss of activity
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant ACC synthase
-
recombinant C-terminally truncated ACC synthase
-
recombinant truncated form of ACC synthase
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3)
expression in Pichia pastoris
-
expression of ACC synthase in Escherichia coli
-
overexpression of C-terminally truncated ACC synthase in Pichia pastoris
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression in fruit skin 116 days after full bloom
expression in fruit skin 16 and 37 days after full bloom
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Jakubowicz, M.
Structure, catalytic activity and evolutionary relationships of 1-aminocyclopropane-1-carboxylate synthase, the key enzyme of ethylene synthesis in higher plants
Acta Biochim. Pol.
49
757-774
2002
Arabidopsis thaliana, Brassica oleracea, Citrus sinensis, Cucumis melo, Cucurbita maxima, Cucurbita pepo, Lupinus albus, Solanum lycopersicum, Malus domestica, Oryza sativa, Pelargonium x hortorum, Vigna radiata, Solanum tuberosum
Manually annotated by BRENDA team
Ko, S.; Eliot, A.C.; Kirsch, J.F.
S-methylmethionine is both a substrate and an inactivator of 1-aminocyclopropane-1-carboxylate synthase
Arch. Biochem. Biophys.
421
85-90
2004
Malus domestica
Manually annotated by BRENDA team
Feng, L.; Geck, M.K.; Eliot, A.C.; Kirsch, J.F.
Aminotransferase activity and bioinformatic analysis of 1-aminocyclopropane-1-carboxylate synthase
Biochemistry
39
15242-15249
2000
Malus domestica
Manually annotated by BRENDA team
Feng, L.; Kirsch, J.F.
L-Vinylglycine is an alternative substrate as well as a mechanism-based inhibitor of 1-aminocyclopropane-1-carboxylate synthase
Biochemistry
39
2436-2444
2000
Malus domestica
Manually annotated by BRENDA team
McCarthy, D.L.; Capitani, G.; Feng, L.; Gruetter, M.G.; Kirsch, J.F.
Glutamate 47 in 1-aminocyclopropane-1-carboxylate synthase is a major specificity determinant
Biochemistry
40
12276-12284
2001
Malus domestica
Manually annotated by BRENDA team
Capitani, G.; Eliot, A.C.; Gut, H.; Khomutov, R.M.; Kirsch, J.F.; Grutter, M.G.
Structure of 1-aminocyclopropane-1-carboxylate synthase in complex with an amino-oxy analogue of the substrate: implications for substrate binding
Biochim. Biophys. Acta
1647
55-60
2003
Malus domestica
Manually annotated by BRENDA team
Capitani, G.; Hohenester, E.; Feng, L.; Storici, P.; Kirsch, J.F.; Jansonius, J.N.
Structure of 1-aminocyclopropane-1-carboxylate synthase, a key enzyme in the biosynthesis of the plant hormone ethylene
J. Mol. Biol.
294
745-756
1999
Malus domestica
Manually annotated by BRENDA team
Capitani, G.; Tschopp, M.; Eliot, A.C.; Kirsch, J.F.; Grutter, M.G.
Structure of ACC synthase inactivated by the mechanism-based inhibitor L-vinylglycine
FEBS Lett.
579
2458-2462
2005
Malus domestica
Manually annotated by BRENDA team
Ban, Y.; Oyama-Okubo, N.; Honda, C.; Nakayama, M.; Moriguchi, T.
Emitted and endogenous volatiles in 'Tsugaru' apple: The mechanism of ester and (E,E)-?-farnesene accumulation
Food Chem.
118
272-277
2010
Malus domestica (P37821), Malus domestica (Q9MB64)
Manually annotated by BRENDA team
Wang, A.; Yamakake, J.; Kudo, H.; Wakasa, Y.; Hatsuyama, Y.; Igarashi, M.; Kasai, A.; Li, T.; Harada, T.
Null mutation of the MdACS3 gene, coding for a ripening-specific 1-aminocyclopropane-1-carboxylate synthase, leads to long shelf life in apple fruit
Plant Physiol.
151
391-399
2009
Malus domestica (O24062), Malus domestica (Q1HAW0), Malus domestica (Q1HAW1), Malus domestica
Manually annotated by BRENDA team
Schaerer, M.A.; Eliot, A.C.; Gruetter, M.G.; Capitani, G.
Structural basis for reduced activity of 1-aminocyclopropane-1-carboxylate synthase affected by a mutation linked to andromonoecy
FEBS Lett.
585
111-114
2011
Malus domestica (P37821), Malus domestica
Manually annotated by BRENDA team
Ayadi, N.; Aloui, S.; Shaiek, R.; Rokbani, O.; Raboudi, F.; Fattouch, S.
In silico study of ethylene biosynthesis Seeking new effectors of ACC synthase and ACC oxidase
Curr. Bioinform.
11
346-356
2016
Solanum lycopersicum, Malus domestica
-
Manually annotated by BRENDA team