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Information on EC 4.4.1.14 - 1-aminocyclopropane-1-carboxylate synthase and Organism(s) Solanum lycopersicum and UniProt Accession P18485

for references in articles please use BRENDA:EC4.4.1.14
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IUBMB Comments
A pyridoxal 5'-phosphate protein. The enzyme catalyses an alpha,gamma-elimination.
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Select one or more organisms in this record: ?
This record set is specific for:
Solanum lycopersicum
UNIPROT: P18485
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The taxonomic range for the selected organisms is: Solanum lycopersicum
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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S-adenosyl-L-methionine methylthioadenosine-lyase
-
1-aminocyclopropane carboxylic acid synthase
-
-
1-aminocyclopropane-1-carboxylate synthase
-
1-aminocyclopropane-1-carboxylate synthase 6
-
1-aminocyclopropane-1-carboxylate synthetase
-
-
-
-
1-aminocyclopropane-1-carboxylic acid synthase
-
-
-
-
1-aminocyclopropanecarboxylate synthase
-
-
-
-
ACC synthase
aminocyclopropane-1-carboxylate synthase
-
-
-
-
aminocyclopropanecarboxylate synthase
-
-
-
-
aminocyclopropanecarboxylic acid synthase
-
-
-
-
S-adenosyl-L-methionine methylthioadenosine-lyase
S-adenosyl-L-methionine methylthioadenosine-lyase (1-aminocyclopropane-1-carboxylate-forming)
-
-
-
-
synthase, 1-aminocyclopropanecarboxylate
-
-
-
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type 2 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
stereochemistry
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
show the reaction diagram
additional information
?
-
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
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
-
best inhibitor tested
1-aminocyclopropane-1-carboxylate
-
-
2-amino-7-(4-methylphenyl)-7,8-dihydro-5(6H)-quinazolinone
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uncompetitive
2-[(3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl)-imino]-5-phosphonopent-3-enoic acid
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strong binding capacity
aminoethoxyvinylglycine
-
-
aminooxyacetic acid
-
-
chlorpromazine
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and analogs
ethylene
ACS6 is negatively regulated by endogenous and exogenous ethylene
L-canaline
-
-
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-isobutyl-1-deazaadenosine
-
-
S-isobutyl-3-deazaadenosine
-
-
S-isobutyl-7-deazaadenosine
-
-
S-isobutyladenosine
-
-
sinefungin
spermidine
-
-
Trifluoperazine
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.02
(-)-S-adenosyl-L-methionine
-
-
0.02 - 0.514
S-adenosyl-L-methionine
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.052 - 9.79
S-adenosyl-L-methionine
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
-
associated with particulate fraction
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
phosphorylation/dephosphorylation of ACS2 regulates its turnover upstream of the ubiquitin-26S-proteasome degradation pathway. ACS2 is stabilized by phosphorylation and degraded after dephosphorylation. The amount of ACS2 affected by the protein kinase/phosphatase inhibitors significantly influences cellular ACS activity, 1-aminocyclopropane-1-carboxylic acid content, and ethylene production levels in tomato fruit tissue. Calcium-dependent protein kinase CDPK2, is one of the protein kinases that are able to phosphorylate ACS2 at residue S460. ACS2 is immediately phosphorylated after translation by CDPK and mitogen-activated protein kinase at different sites in response to wound signaling and almost all functional ACS2 molecules are phosphorylated in the cell. Phosphorylation at both sites is required for ACS2 stability
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
1A12_SOLLC
485
0
54663
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45000
-
two-dimensional denaturing gel-electrophoresis
50000
57000
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 53100-54800
monomer
-
1 * 50000, SDS-PAGE, gel filtration
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
phosphorylation/dephosphorylation of ACS2 regulates its turnover upstream of the ubiquitin-26S-proteasome degradation pathway. ACS2 is stabilized by phosphorylation and degraded after dephosphorylation. The amount of ACS2 affected by the protein kinase/phosphatase inhibitors significantly influences cellular ACS activity, 1-aminocyclopropane-1-carboxylic acid content, and ethylene production levels in tomato fruit tissue. Calcium-dependent protein kinase CDPK2, is one of the protein kinases that are able to phosphorylate ACS2 at residue S460. ACS2 is immediately phosphorylated after translation by CDPK and mitogen-activated protein kinase at different sites in response to wound signaling and almost all functional ACS2 molecules are phosphorylated in the cell. Phosphorylation at both sites is required for ACS2 stability
phosphoprotein
-
in presence of oligogalacturonic acids, formation of phosphorylated isoform ACS2 is observed
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
R286A
-
almost complete loss of activity
R286I
-
almost complete loss of activity
R286L
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
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
stable, for at least 3 h
42
-
50% loss of activity after 15 min
52
-
97% loss of activity after 15 min
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
stable for at least 3 days, in ice
-
unstable even during storage at -20°C
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
by (NH4)2SO4 saturation
isoenzyme LeACS2 and five ACC synthase mutants (Y151F, Y151G, Y152F, Y152G and Y151F/Y152F) in Escherichia coli
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recombinant ACC synthase
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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
expression in Escherichia coli
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expression of C-terminal deletion mutant in Escherichia coli
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expression of C-terminal truncated ACCC synthase in Escherichia coli
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expression of the tomato isoenzyme Lw-ACS2 in Escherichia coli
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overexpression of isoenzyme LeACS2 and five ACC synthase mutants (Y151F, Y151G, Y152F, Y152G and Y151F/Y152F) in Escherichia coli
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
presence of oligogalacturonic acids upregulates expression of both ACC synthase ACS2 and ACC oxidase ACO1
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
agriculture
UV-B radiation influences ethylene biosynthesis by changes in the expression of the ACC synthase
agriculture
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Satoh, S.; Yang, S.F.
S-Adenosylmethionine-dependent inactivation and radiolabeling of 1-aminocyclopropane-1-carboxylate synthase isolated from tomato fruits
Plant Physiol.
88
109-114
1988
Solanum lycopersicum
Manually annotated by BRENDA team
Adams, D.O.; Yang, S.F.
1-Aminocyclopropane-1-carboxylate synthase
Methods Enzymol.
143
426-429
1987
Solanum lycopersicum
-
Manually annotated by BRENDA team
Miyazaki, J.H.; Yang, S.F.
Inhibition of the methionine cycle enzymes
Phytochemistry
26
2655-2660
1987
Solanum lycopersicum
-
Manually annotated by BRENDA team
Khani-Oskouee, S.; Ramalingam, K.; Kalvin, D.; Woodard, R.W.
Alternate substrates and inhibitors of 1-aminocyclopropane-1-carboxylic acid synthase
Bioorg. Chem.
15
92-99
1987
Solanum lycopersicum
-
Manually annotated by BRENDA team
Bleecker, A.B.; Kenyon, W.H.; Somerville, S.C.; Kende, H.
Use of monoclonal antibodies in the purification and characterization of 1-aminocyclopropane-1-carboxylate synthase, an enzyme in ehtylene biosynthesis
Proc. Natl. Acad. Sci. USA
83
7755-7759
1986
Solanum lycopersicum
Manually annotated by BRENDA team
Ramalingam, K.; Lee, K.M.; Woodard, R.W.; Bleecker, A.B.; Kende, H.
Stereochemical course of the reaction catalyzed by the pyridoxal phosphate-dependent enzyme 1-aminocyclopropane-1-carboxylate synthase
Proc. Natl. Acad. Sci. USA
82
7820-7824
1985
Solanum lycopersicum
Manually annotated by BRENDA team
Acaster, M.A.; Kende, H.
Properties and partial purification of 1-aminocyclopropane-1-carboxylate synthase
Plant Physiol.
72
139-145
1983
Solanum lycopersicum
Manually annotated by BRENDA team
Mattoo, A.K.; Adams.D.O.; Patterson, G.W.; Lieberman, M.
Inihibition of 1-aminocyclopropane-1-carboxylic acid synthase by phenotiazines
Plant Sci. Lett.
28
173-179
1983
Solanum lycopersicum
-
Manually annotated by BRENDA team
Kende, H.; Boller, T.
Wound ethylene and 1-aminocyclopropane-1-carboxylate synthase in ripening tomato fruit
Planta
151
476-481
1981
Solanum lycopersicum
Manually annotated by BRENDA team
Yu, Y.B.; Adams, D.O.; Yang, S.F.
1-Aminocyclopropanecarboxylate synthase, a key enzyme in ethylene biosynthesis
Arch. Biochem. Biophys.
198
280-286
1979
Solanum lycopersicum
Manually annotated by BRENDA team
Boller, T.; Herner, R.C.; Kende, H.
Assay for an enzymatic formation of an ethylene precursor, 1-aminocyclopropane-1-carboxylic acid
Planta
145
293-303
1979
Solanum lycopersicum
Manually annotated by BRENDA team
Li, N.; Huxtable, S.; Yang, S.F.; Kung, S.D.
Effects of N-terminal deletions on 1-aminocyclopropane-1-carboxylate synthase activity
FEBS Lett.
378
286-290
1996
Solanum lycopersicum
Manually annotated by BRENDA team
Tarun, A.S.; Lee, J.S.; Theologis, A.
Random mutagenesis of 1-aminocyclopropane-1-carboxylate synthase: a key enzyme in ethylene biosynthesis
Proc. Natl. Acad. Sci. USA
95
9796-9801
1998
Solanum lycopersicum
Manually annotated by BRENDA team
Casas, J.L.; Barcia-Canovas, F.; Tudela, J.; Acosta, M.
A kinetic study of simultaneous suicide inactivation and irreversible inhibition of an enzyme. Application to 1-aminocyclopropane-1-carboxylate (ACC) synthase inactivation by its substrate S-adenosylmethionine
J. Enzyme Inhib.
7
1-14
1993
Solanum lycopersicum
Manually annotated by BRENDA team
Van der Straeten, D.; van Wiemeersch, L.; Goodman, H.M.; van Montagu, M.
Purification and partial characterization of 1-aminocyclopropane-1-carboxylate synthase from tomato pericarp
Eur. J. Biochem.
182
639-647
1989
Solanum lycopersicum
Manually annotated by BRENDA team
Yip, W.K.; Dong, J.G.; Kenny, J.W.; Thompson, G.A.; Yang, S.F.
Characterization and sequencing of the active site of 1-aminocyclopropane-1-carboxylate synthase
Proc. Natl. Acad. Sci. USA
87
7930-7934
1990
Solanum lycopersicum, Malus sylvestris
Manually annotated by BRENDA team
Li, N.; Mattoo, A.K.
Deletion of the carboxyl-terminal region of 1-aminocyclopropane-1-carboxylic acid synthase, a key protein in the biosynthesis of ethylene, results in catalytically hyperactive, monomeric enzyme
J. Biol. Chem.
269
6908-6917
1994
Solanum lycopersicum
Manually annotated by BRENDA team
Zhou, H.; Huxtable, S.; Xin, H.; Li, N.
Enhanced high-level expression of soluble 1-aminocyclopropane-1-carboxylase synthase and rapid purification by expanded-bed adsorption
Protein Expr. Purif.
14
178-184
1998
Cucurbita pepo, Solanum lycopersicum
Manually annotated by BRENDA team
Nakatsuka, A.; Murachi, S.; Okunishi, H.; Shiomi, S.; Nakano, R.; Kubo, Y.; Inaba, A.
Differential expression and internal feedback regulation of 1-aminocyclopropane-1-carboxylate synthase, 1-aminocyclopropane-1-carboxylate oxidase, and ethylene receptor genes in tomato fruit during development and ripening
Plant Physiol.
118
1295-1305
1998
Solanum lycopersicum
Manually annotated by BRENDA team
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
Huai, Q.; Xia, Y.; Chen, Y.; Callahan, B.; Li, N.; Ke, H.
Crystal structures of 1-aminocyclopropane-1-carboxylate (ACC) synthase in complex with aminoethoxyvinylglycine and pyridoxal-5'-phosphate provide new insight into catalytic mechanisms
J. Biol. Chem.
276
38210-38216
2001
Solanum lycopersicum
Manually annotated by BRENDA team
Zhou, H.; Wang, H.W.; Zhu, K.; Sui, S.F.; Xu, P.; Yang, S.F.; Li, N.
The multiple roles of conserved arginine 286 of 1-aminocyclopropane-1-carboxylate synthase. Coenzyme binding, substrate binding, and beyond
Plant Physiol.
121
913-919
1999
Solanum lycopersicum
Manually annotated by BRENDA team
Yoshida, H.; Nagata, M.; Saito, K.; Wang, K.L.; Ecker, J.R.
Arabidopsis ETO1 specifically interacts with and negatively regulates type 2 1-aminocyclopropane-1-carboxylate synthases
BMC Plant Biol.
5
14
2005
Solanum lycopersicum, Solanum lycopersicum Mill.
Manually annotated by BRENDA team
Li, J.F.; Qu, L.H.; Li, N.
Tyr152 plays a central role in the catalysis of 1-aminocyclopropane-1-carboxylate synthase
J. Exp. Bot.
56
2203-2210
2005
Solanum lycopersicum
Manually annotated by BRENDA team
An, L.; Xu, X.; Tang, H.; Zhang, M.; Hou, Z.; Liu, Y.; Zhao, Z.; Feng, H.; Xu, S.; Wang, X.
Ethylene production and 1-aminocyclopropane-1-carboxylate (ACC) synthase gene expression in tomato (Lycopsicon esculentum Mill.) leaves under enhanced UV-B radiation
J. Integr. Plant Biol.
48
1190-1196
2006
Solanum lycopersicum (P18485)
-
Manually annotated by BRENDA team
Yoshida, H.; Wang, K.L.; Chang, C.M.; Mori, K.; Uchida, E.; Ecker, J.R.
The ACC synthase TOE sequence is required for interaction with ETO1 family proteins and destabilization of target proteins
Plant Mol. Biol.
62
427-437
2006
Solanum lycopersicum, Solanum lycopersicum (Q42881)
Manually annotated by BRENDA team
Liu, K.; Shen, L.; Sheng, J.
Improvement in cadmium tolerance of tomato seedlings with an antisense DNA for 1-aminocyclopropane-1-carboxylate synthase
J. Plant Nutr.
31
809-827
2008
Solanum lycopersicum
-
Manually annotated by BRENDA team
Chang, S.; Lu, L.; Wang, N.N.; Charng, Y.
Negative feedback regulation of system-1 ethylene production by the tomato 1-aminocyclopropane-1-carboxylate synthase 6 gene promoter
Plant Sci.
175
149-160
2008
Solanum lycopersicum (Q94LA1)
Manually annotated by BRENDA team
Kamiyoshihara, Y.; Iwata, M.; Fukaya, T.; Tatsuki, M.; Mori, H.
Turnover of LeACS2, a wound-inducible 1-aminocyclopropane-1-carboxylic acid synthase in tomato, is regulated by phosphorylation/dephosphorylation
Plant J.
64
140-150
2010
Solanum lycopersicum (P18485), Solanum lycopersicum
Manually annotated by BRENDA team
Ma, Y.; Zhou, L.; Wang, Z.; Chen, J.; Qu, G.
Oligogalacturonic acids promote tomato fruit ripening through the regulation of 1-aminocyclopropane-1-carboxylic acid synthesis at the transcriptional and post-translational levels
BMC Plant Biol.
16
13
2016
Solanum lycopersicum
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