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
4.4.1.14
-
RECOMMENDED NAME
GeneOntology No.
1-aminocyclopropane-1-carboxylate synthase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
stereochemistry
-
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.
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1-aminocyclopropane-1-carboxylate synthetase
-
-
-
-
1-aminocyclopropane-1-carboxylic acid synthase
-
-
-
-
ACC synthase
-
-
-
-
aminocyclopropane-1-carboxylate synthase
-
-
-
-
aminocyclopropanecarboxylate synthase
-
-
-
-
aminocyclopropanecarboxylic acid synthase
-
-
-
-
S-adenosyl-L-methionine methylthioadenosine-lyase
-
-
-
-
synthase, 1-aminocyclopropanecarboxylate
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
72506-68-4
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
brassinosteroid enhances the expression of the auxin-responsive ACC synthase 4
SwissProt
Manually annotated by BRENDA team
ecotype Columbia
-
-
Manually annotated by BRENDA team
L. cultivar Varuna and RH 30
-
-
Manually annotated by BRENDA team
Sinta
-
-
Manually annotated by BRENDA team
Carica papaya Sinta
Sinta
-
-
Manually annotated by BRENDA team
Citrullus colocynthis x lanatus
isozyme ACS1; variant lanatus
UniProt
Manually annotated by BRENDA team
Citrullus colocynthis x lanatus
isozyme ACS2, fragment; variant lanatus
UniProt
Manually annotated by BRENDA team
Citrullus colocynthis x lanatus
isozyme ACS3; variant lanatus
UniProt
Manually annotated by BRENDA team
Citrullus colocynthis x lanatus
isozyme ACS4, fragment; variant lanatus
UniProt
Manually annotated by BRENDA team
cucumber
-
-
Manually annotated by BRENDA team
L. var sativus cv Beit Alpha monoecious ffMM and gynoecious FFMM
SWISSPROT
Manually annotated by BRENDA team
Duch. cv. Ebisu, winter squash
-
-
Manually annotated by BRENDA team
zucchini
Uniprot
Manually annotated by BRENDA team
zucchini
-
-
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
gene DcACS1, several cultivars
-
-
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
cv lumian 22
SwissProt
Manually annotated by BRENDA team
cv Xuzhou 142, isoform ACS2
UniProt
Manually annotated by BRENDA team
isozyme ACS1; Japanese morning glory, formerly Pharbitis nil, cultivar Violet
UniProt
Manually annotated by BRENDA team
cv. Tsugaru
UniProt
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
-
SwissProt
Manually annotated by BRENDA team
ACS is encoded by a multigen family, consisting of at least five members
-
-
Manually annotated by BRENDA team
deepwater rice
-
-
Manually annotated by BRENDA team
cv. Hongyanzhenghui, gene PlACS
UniProt
Manually annotated by BRENDA team
Penicillium citrinum AHU 8443
AHU 8443
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
PG29
SwissProt
Manually annotated by BRENDA team
x engelmannii, Fal-1028
SwissProt
Manually annotated by BRENDA team
x engelmannii, Pge, Fal-1028
SwissProt
Manually annotated by BRENDA team
Picea glauca PG29
PG29
SwissProt
Manually annotated by BRENDA team
loblolly pine
Q06IN7 and Q06IN6
UniProt
Manually annotated by BRENDA team
Batsch cultivar Akatsuki
-
-
Manually annotated by BRENDA team
isozyme ACS1; cultivars Early Golden and Shiro
UniProt
Manually annotated by BRENDA team
isozyme ACS3, fragments; cultivars Early Golden and Shiro
B2XCJ8 and B2XCJ9 and B2XCK0
UniProt
Manually annotated by BRENDA team
isozyme ACS4, fragment; cultivars Early Golden and Shiro
UniProt
Manually annotated by BRENDA team
isozyme ACS5; cultivars Early Golden and Shiro
UniProt
Manually annotated by BRENDA team
Pseudotsuga menziesii, Pm, wild
SwissProt
Manually annotated by BRENDA team
Pseudotsuga menziesii, wild
SwissProt
Manually annotated by BRENDA team
Asian pear
-
-
Manually annotated by BRENDA team
cv.Whangkeumbae, gene PpACS1a
UniProt
Manually annotated by BRENDA team
comercial variety Kardinal
SwissProt
Manually annotated by BRENDA team
fragment; cultivar L4783
UniProt
Manually annotated by BRENDA team
isoenzyme ACS2
-
-
Manually annotated by BRENDA team
isoform ACS2
SWISSPROT
Manually annotated by BRENDA team
Mill. cv. Shugyoku
-
-
Manually annotated by BRENDA team
Mill. cv. Shugyoku
SwissProt
Manually annotated by BRENDA team
Solanum lycopersicum Mill.
Mill.
-
-
Manually annotated by BRENDA team
mung bean
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
Q9SXN9
the enzyme belongs to type-1 subfamily of plant 1-aminocyclopropane-1-carboxylate synthases
metabolism
-
harvest periods related to soluble solids contents content of Hayward kiwifruit significantly affect 1-aminocyclopropane-1-carboxylate synthase activity, total soluble protein content and protein profile. ACC synthase activity is suppressed, especially in early harvested fruits, by an inhibition of fruit ripening during controlled atmosphere storage
metabolism
P18485
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
metabolism
Q06402, Q9SAR0
proteolytic turnover of the ACS6 protein is retarded when protein phosphatase 2A activity is reduced. Protein phosphatase 2A and ACS6 proteins associate in seedlings and RCN1-containing protein phosphatase 2A complexes specifically dephosphorylate a C-terminal ACS6 phosphopeptide
metabolism
K0E1C1
1-aminocyclopropane-1-carboxylate synthase and 1-aminocyclopropane-1-carboxylate oxidase are key enzymes in the ethylene production
metabolism
-
the enzyme catalyzes the generally rate-limiting step in the biosynthesis of the phytohormone ethylene. 14-3-3 proteins exhibit a regulatory function in the pathway by reducing the degradation of 1-aminocyclopropane-1-carboxylate synthase through components of a CULLIN-3 E3 ubiquitin ligase, i.e. ethylene-overproducer 1-like proteins or ETO1/EOLs, that target a subset of the 1-aminocyclopropane-1-carboxylate synthase proteins for rapid degradation by the 26S proteasome. 14-3-3 protein positively regulates type-2 ACS protein stability by both increasing the turnover of the ETO1/EOL BTB E3 ligases that target type-2 ACS proteins and by an ETO1/EOL-independent mechanism. 14-3-3 protein promotes the degradation of ETO1/EOLs, likely via the 26S proteasome pathway
physiological function
A2IBN7
cotton ACS2 interacts with Ca2+-dependent protein kinase CPK1. Phosphorylated ACS2 shows significantly increased ACS activity, leading to elevated ethylene production
physiological function
-
ethylene overproduction in protein phosphatase 2A-deficient plants requires isoforms ACS2 and ACS6
physiological function
Q9SXN9
the enzyme might be involved in fruit ripening and in response to salicylic acid, indole-3-acetic acid, and disease
metabolism
-
the enzyme is important in ethylene production
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)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(R,S)-S-adenosyl-L-methionine
vinylglycine + methylthioadenosine
show the reaction diagram
-
-
-
?
(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
-
-
-
?
(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-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
alpha-ketobutyrate + ammonia
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-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
-
-
-
-
?
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
-
-
-
-
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
-
-
-
-
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
-
-
-
?
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
-
-
-
-
?
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
show the reaction diagram
Q42881
-
-
-
?
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
show the reaction diagram
-
-
-
ir
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
show the reaction diagram
-
-
-
ir
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
Diospyros sp.
-
-
-
-
?
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
-
-
-
?
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
show the reaction diagram
Q6U5H3
-
-
?
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
A9NIT9
-
-
-
?
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
A2IA37, A2IA38, A2IA39, A2IA40, A2IA41
-
-
-
?
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
show the reaction diagram
A2IA42, A2IA43, A2IA44
-
-
-
?
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
show the reaction diagram
P18485
-
-
-
?
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
show the reaction diagram
Q06402
-
-
-
?
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
show the reaction diagram
A0JBY6
-
-
-
?
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
show the reaction diagram
O82125
-
-
-
?
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
show the reaction diagram
Q2EN04
-
-
-
?
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
show the reaction diagram
Q10DK7
-
-
-
?
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
show the reaction diagram
B2XCJ7, B2XCJ8 and B2XCJ9 and B2XCK0, B2XCK1, B2XCK2
-
-
-
?
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
show the reaction diagram
Q06IN7 and Q06IN6
-
-
-
?
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
show the reaction diagram
Q307X1
-
-
-
?
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
show the reaction diagram
Q94LA1
-
-
-
?
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
show the reaction diagram
Citrullus colocynthis x lanatus
B2WR79, B2WR80, B2WR81, B2WR82
-
-
-
?
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
show the reaction diagram
A2IBN7
-
-
-
?
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
show the reaction diagram
K0E1C1
-
-
-
?
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
show the reaction diagram
-
biosynthesis of ethylene: plant hormone
-
-
-
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
show the reaction diagram
-
biosynthesis of ethylene: plant hormone
-
-
-
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
show the reaction diagram
P23279
biosynthesis of ethylene: plant hormone
-
-
-
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
show the reaction diagram
-
biosynthesis of ethylene: plant hormone
-
-
-
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
show the reaction diagram
-
biosynthesis of ethylene: plant hormone
-
-
-
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
show the reaction diagram
-
biosynthesis of ethylene: plant hormone
-
-
-
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
show the reaction diagram
-
rate-determining step in the biosynthesis of ethylene
-
?
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
show the reaction diagram
Penicillium citrinum AHU 8443
-
-
-
?
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
show the reaction diagram
Picea glauca PG29
A2IA41
-
-
-
?
S-methyl-L-methionine
alpha-ketobutyrate + ammonia + dimethylsulfide
show the reaction diagram
-
beta,gamma elimination of dimethylsulfide to yield enzyme bound L-vinylglycine, which is subsequently converted to alpha-ketobutyrate and ammonia
-
?
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
-
-
-
?
vinylglycine
alpha-ketobutyrate + ammonia
show the reaction diagram
-
-
-
?
L-vinylglycine
2-oxobutanoate + NH4+
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
rigid specifity for (-)-S-adenosyl-L-methionine, only purine base adenosine and adenosine analogs in which N6 nitrogen is modified
-
-
additional information
?
-
-
rigid specifity for (-)-S-adenosyl-L-methionine, only purine base adenosine and adenosine analogs in which N6 nitrogen is modified, not: S-adenosylhomocysteine
-
-
additional information
?
-
-
not: S-adenosylhomocysteine, L-methionine, S-methylthionine
-
-
additional information
?
-
-
enzyme activity may affect net photosynthetic rate through ethylene-induced changes on foliar gas exchange and leaf growth
-
-
-
additional information
?
-
-
ETOI family proteins specifically interact with and negatively regulate type 2 ACC synthase - Arabidopsis ETOI can regulate type 2 ACC synthase in a heterogous Lycopersicon esculentum
-
-
-
additional information
?
-
-
key enzyme in the regulation of ethylene biosynthesis in higher plants
-
-
-
additional information
?
-
-
possible alternative splicing mechanism in ripening-related ACC synthase genes in hybrid papaya, possibly to modulate or fine-tune gene expression relevant to fruit ripening
-
-
-
additional information
?
-
-
the suppression of fruit softening in stony hard peach cultivar is caused by a low level of ethylene production, which depends on the supressed expression of Pp-ACS-1
-
-
-
additional information
?
-
Q94LA1
ACS6 is involved in system-1 ethylene production in preclimacteric fruit
-
-
-
additional information
?
-
Carica papaya Sinta
-
possible alternative splicing mechanism in ripening-related ACC synthase genes in hybrid papaya, possibly to modulate or fine-tune gene expression relevant to fruit ripening
-
-
-
additional information
?
-
Solanum lycopersicum Mill.
-
ETOI family proteins specifically interact with and negatively regulate type 2 ACC synthase - Arabidopsis ETOI can regulate type 2 ACC synthase in a heterogous Lycopersicon esculentum
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
Q6U5H3
-
-
?
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
show the reaction diagram
-
biosynthesis of ethylene: plant hormone
-
-
-
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
show the reaction diagram
-
biosynthesis of ethylene: plant hormone
-
-
-
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
show the reaction diagram
P23279
biosynthesis of ethylene: plant hormone
-
-
-
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
show the reaction diagram
-
biosynthesis of ethylene: plant hormone
-
-
-
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
show the reaction diagram
-
biosynthesis of ethylene: plant hormone
-
-
-
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
show the reaction diagram
-
biosynthesis of ethylene: plant hormone
-
-
-
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
show the reaction diagram
-
rate-determining step in the biosynthesis of ethylene
-
?
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
show the reaction diagram
Penicillium citrinum AHU 8443
-
-
-
?
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
-
-
-
?
L-alanine + pyridoxal 5'-phosphate
pyruvate + pyridoxamine 5'-phosphate
show the reaction diagram
-
-
-
?
additional information
?
-
-
enzyme activity may affect net photosynthetic rate through ethylene-induced changes on foliar gas exchange and leaf growth
-
-
-
additional information
?
-
-
ETOI family proteins specifically interact with and negatively regulate type 2 ACC synthase - Arabidopsis ETOI can regulate type 2 ACC synthase in a heterogous Lycopersicon esculentum
-
-
-
additional information
?
-
-
key enzyme in the regulation of ethylene biosynthesis in higher plants
-
-
-
additional information
?
-
-
possible alternative splicing mechanism in ripening-related ACC synthase genes in hybrid papaya, possibly to modulate or fine-tune gene expression relevant to fruit ripening
-
-
-
additional information
?
-
-
the suppression of fruit softening in stony hard peach cultivar is caused by a low level of ethylene production, which depends on the supressed expression of Pp-ACS-1
-
-
-
additional information
?
-
Q94LA1
ACS6 is involved in system-1 ethylene production in preclimacteric fruit
-
-
-
additional information
?
-
Carica papaya Sinta
-
possible alternative splicing mechanism in ripening-related ACC synthase genes in hybrid papaya, possibly to modulate or fine-tune gene expression relevant to fruit ripening
-
-
-
additional information
?
-
Solanum lycopersicum Mill.
-
ETOI family proteins specifically interact with and negatively regulate type 2 ACC synthase - Arabidopsis ETOI can regulate type 2 ACC synthase in a heterogous Lycopersicon esculentum
-
-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
small amounts, firmly bound
pyridoxal 5'-phosphate
-
active site lysine binds pyridoxal 5'-phosphate
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
one per subunit
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
KM: 430 nM. Activity without addition of pyridoxal 5'-phosphate is about one-eighth of the maximum activity in presence of pyridoxal 5'-phosphate
pyridoxal 5'-phosphate
Q06IN7 and Q06IN6
-
pyridoxal 5'-phosphate
B2XCJ7, B2XCJ8 and B2XCJ9 and B2XCK0, B2XCK1, B2XCK2
-
pyridoxal 5'-phosphate
Q307X1
-
pyridoxal 5'-phosphate
Citrullus colocynthis x lanatus
B2WR79, B2WR80, B2WR81, B2WR82
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
D1MF34
-
pyridoxal 5'-phosphate
P37821
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
-
-
pyridoxal 5'-phosphate
Q9SXN9
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
no effect: Mg2+, Mn2+, Co2+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1-aminocyclopropane-1-carboxylate
-
-
1-aminoethoxyvinyl glycine
Citrullus colocynthis x lanatus
B2WR79, B2WR80, B2WR81, B2WR82
-
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
Q37001
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
Q37001
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
Q37001
inhibition of ethylene biosynthesis at the step of converting S-adenosylmethionine to 1-aminocyclopropane-1-carboxylic acid by ACC synthase
aminoethoxyvinylglycine
-
-
aminoethoxyvinylglycine
-
-
aminoethoxyvinylglycine
-
-
aminooxyacetic acid
-
-
aminooxyacetic acid
-
-
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
Q94LA1
ACS6 is negatively regulated by endogenous and exogenous ethylene
homocysteine
-
slight
L-canaline
-
-
L-Vinylglycine
-
approx. 60% loss of activity after 5 min, approx. 90% loss of activity after 40 min, biphasic inativation, mechanism based inhibition
L-Vinylglycine
-
mechanism-based inactivation
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
-
inactivation during catalytic action, (+) and (+/-) isomer
S-adenosyl-L-methionine
-
in presence of pyridoxal 5'-phosphate
S-adenosyl-L-methionine
-
-
S-adenosyl-L-methionine
-
-
S-adenosyl-L-methionine
-
mechanism-based inactivation
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
-
naturally occuring antifungal antibiotic isolated from Streptomyces griseus
spermidine
-
-
Trifluoperazine
-
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1-aminocyclopropane-1-carboxylate
Citrullus colocynthis x lanatus
B2WR79, B2WR80, B2WR81, B2WR82
expression of ACS1 is up-regulated by exogenous treatment with 0.1 mM 1-aminocyclopropane-1-carboxylate
1-aminocyclopropane-1-carboxylate
-
the expression of ACS7 is enhanced by 0.02 mM 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
Q06IN7 and Q06IN6
induces gene expression at 1 mM
3-indole acetic acid
B2XCJ7, B2XCJ8 and B2XCJ9 and B2XCK0, B2XCK1, B2XCK2
plant tissues treated with 3-indole acetic acid exhibit dramatic increases in isozyme ACS1 mRNA level; plant tissues treated with 3-indole acetic acid exhibit dramatic increases in isozyme ACS3 mRNA level; plant tissues treated with 3-indole acetic acid exhibit dramatic increases in isozyme ACS5 mRNA level
3-indole acetic acid
Q307X1
3-indole acetic acid applied to the cotyledons of seedlings causes a clear increase of ACS mRNA
3-indole acetic acid
-
exogenous treatment with 3-indole acetic acid increases the promoter activity of ACS4
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
B2XCJ7, B2XCJ8 and B2XCJ9 and B2XCK0, B2XCK1, B2XCK2
;
auxin
Citrullus colocynthis x lanatus
B2WR79, B2WR80, B2WR81, B2WR82
expression of ACS1 is up-regulated by exogenous treatment with 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
B2XCJ7, B2XCJ8 and B2XCJ9 and B2XCK0, B2XCK1, B2XCK2
activates transcription of isozyme ACS1; activates transcription of isozyme ACS4
ethylene
-
ethylene enhances the promoter activities of ACS4 and ACS7 genes but exhibits no obvious impacts on that of ACS5
gibberellin
B2XCJ7, B2XCJ8 and B2XCJ9 and B2XCK0, B2XCK1, B2XCK2
isozyme ACS1 expression level is slightly induced by 0.0004 mM gibberellin and declines thereafter to reach their basal level with higher concentrations; isozyme ACS3 expression level is slightly induced by 0.0004 mM gibberellin and declines thereafter to reach their basal level with higher concentrations; isozyme ACS5 expression level is slightly induced by 0.0004 mM gibberellin and declines thereafter to reach their basal level with higher concentrations
gibberellin
Citrullus colocynthis x lanatus
B2WR79, B2WR80, B2WR81, B2WR82
expression of ACS1 is up-regulated by exogenous treatment with 0.5 mM 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
B2WR79, B2WR80, B2WR81, B2WR82
0.05 mM
jasmonic acid
-
exogenous treatment with jasmonic acid increases the promoter activity of ACS4
xanthine-xanthine oxidase
-
generator of superoxide radicals
-
methylviologen
-
generator of superoxide radicals
additional information
-
scavengers of reactive oxygen species like 1,4-diazabicyclo(2,2,2) octane, superoxide dismutase, n-propyl gallate, catalase have no effect
-
additional information
Q06IN7 and Q06IN6
transcript levels of this ACC synthase gene increase rapidly in response to bending stress but return to near starting levels within 30 min
-
additional information
B2XCJ7, B2XCJ8 and B2XCJ9 and B2XCK0, B2XCK1, B2XCK2
isozyme ACS4 is not activated by treatments with gibberellin, cytokinin, 3-indole acetic acid, 1-naphthyl acetic acid, and 3-indole butyric acid
-
additional information
-
increased enzyme activity after wounding of the potatoe
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.02
(-)-S-adenosyl-L-methionine
-
-
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
L-Vinylglycine
-
deamination
1.4
L-Vinylglycine
-
alpha-ketobutyrate production
1.4
L-Vinylglycine
-
deamination
1.4
L-Vinylglycine
-
-
0.01
S-adenosyl-L-methionine
-
pH 8.5, 30°C
0.012
S-adenosyl-L-methionine
-
-
0.012
S-adenosyl-L-methionine
-
elimination
0.0133
S-adenosyl-L-methionine
-
-
0.017
S-adenosyl-L-methionine
-
-
0.02
S-adenosyl-L-methionine
-
-
0.023
S-adenosyl-L-methionine
P23279
refolded enzyme
0.02927
S-adenosyl-L-methionine
-
without chilling in the presence of xanthine–xanthine oxidase and catalase
0.0315
S-adenosyl-L-methionine
-
30°C, pH 8.5, wild-type enzyme
0.03168
S-adenosyl-L-methionine
-
8 h after chilling
0.03213
S-adenosyl-L-methionine
-
without chilling in the presence of xanthine–xanthine oxidase
0.03565
S-adenosyl-L-methionine
-
without chilling in the presence of methylviologen and catalase
0.03608
S-adenosyl-L-methionine
-
without chilling in the presence of methylviologen
0.038 - 0.167
S-adenosyl-L-methionine
-
Km increases from pH 7.5 to 9.5
0.03977
S-adenosyl-L-methionine
-
8 h after chilling in the presence of catalase; 8 h after chilling in the presence of n-propyl gallate
0.04
S-adenosyl-L-methionine
-
-
0.04
S-adenosyl-L-methionine
-
3 h after chilling
0.04056
S-adenosyl-L-methionine
-
8 h after chilling in the presence of superoxide dismutase
0.04098
S-adenosyl-L-methionine
-
without chilling in the presence of xanthine–xanthine oxidase and superoxide dismutase
0.04101
S-adenosyl-L-methionine
-
12 h after chilling
0.04136
S-adenosyl-L-methionine
-
without chilling in the presence of methylviologen and superoxide dismutase
0.04208
S-adenosyl-L-methionine
-
without chilling in the presence of xanthine–xanthine oxidase and n-propyl gallate
0.04216
S-adenosyl-L-methionine
-
without chilling in the presence of xanthine–xanthine oxidase and 1,4-diazabicyclo(2,2,2) octane
0.04322
S-adenosyl-L-methionine
-
without chilling in the presence of methylviologen and 1,4-diazabicyclo(2,2,2) octane
0.04438
S-adenosyl-L-methionine
-
without chilling in the presence of methylviologen and n-propyl gallate
0.04443
S-adenosyl-L-methionine
-
8 h after chilling in the presence of 1,4-diazabicyclo(2,2,2) octane
0.0458
S-adenosyl-L-methionine
-
30°C, pH 8.5, mutant enzyme Y151F
0.05232
S-adenosyl-L-methionine
-
-
0.055
S-adenosyl-L-methionine
-
-
0.056
S-adenosyl-L-methionine
-
recombinant enzyme, pH 8.5, 30°C
0.05712
S-adenosyl-L-methionine
-
without chilling in the presence of H2O2
0.12
S-adenosyl-L-methionine
-
-
0.12
S-adenosyl-L-methionine
-
-
0.168
S-adenosyl-L-methionine
-
30°C, pH 8.5, mutant enzyme Y151G
0.409
S-adenosyl-L-methionine
-
30°C, pH 8.5, mutant enzyme Y151F/Y152F
0.514
S-adenosyl-L-methionine
-
30°C, pH 8.5, mutant enzyme Y152F
1.4
S-adenosyl-L-methionine
-
pH 9.0, 30°C
4.1
S-methyl-L-methionine
-
beta,gamma-elimination
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
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
L-alanine
-
transamination
0.0029
L-alanine
-
transamination
0.0012
L-arginine
-
transamination
0.004
L-Vinylglycine
-
inactivation
0.7 - 1
L-Vinylglycine
-
deamination
0.71
L-Vinylglycine
-
deamination
1.8
L-Vinylglycine
-
alpha-ketobutyrate production
1.8
L-Vinylglycine
-
deamination
1.8
L-Vinylglycine
-
-
0.052 - 2.1
S-adenosyl-L-methionine
-
-
0.18
S-adenosyl-L-methionine
-
30°C, pH 8.5, mutant enzyme Y151F/Y152F
0.39
S-adenosyl-L-methionine
-
30°C, pH 8.5, mutant enzyme Y152F
0.75
S-adenosyl-L-methionine
-
pH 9.0, 30°C
1.3
S-adenosyl-L-methionine
-
30°C, pH 8.5, mutant enzyme Y151G
1.41
S-adenosyl-L-methionine
-
30°C, pH 8.5, wild-type enzyme
1.5
S-adenosyl-L-methionine
-
30°C, pH 8.5, mutant enzyme Y151F
9.2
S-adenosyl-L-methionine
-
elimination
9.79
S-adenosyl-L-methionine
-
-
0.0008
S-methyl-L-methionine
-
transamination
0.0016
S-methyl-L-methionine
-
inactivation
0.045
S-methyl-L-methionine
-
beta,gamma-elimination
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000015
7-(4-methoxyphenyl)-2-(phenylamino)-7,8-dihydroquinazolin-5(6H)-one
Q37001
pH 8.0, 25°C
0.000023
aminoethoxyvinylglycine
Q37001
pH 8.0, 25°C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0079
2-(cyclopentylamino)-7,7-dimethyl-7,8-dihydroquinazolin-5(6H)-one
Q37001
pH 8.0, 25°C
0.0014
2-(cyclopentylamino)-7-(4-methylphenyl)-7,8-dihydroquinazolin-5(6H)-one
Q37001
pH 8.0, 25°C
0.0005
7-(4-methoxyphenyl)-2-(phenylamino)-7,8-dihydroquinazolin-5(6H)-one
Q37001
pH 8.0, 25°C
0.0007
aminoethoxyvinylglycine
Q37001
pH 8.0, 25°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
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
Q2EN04
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
P23279
refolded enzyme
1.85
A2IBN7
pH 7.5, 30°C, native enzyme
2.78
A2IBN7
pH 7.5, 30°C, enzyme phosphorylated by CPK1
additional information
-
-
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.5
-
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
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
LITERATURE
24
-
highest enzyme activity in petals at day 10 after cutting
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5
-
isoenzyme ACS
5.7
A2IA37, A2IA38, A2IA39, A2IA40, A2IA41
-
5.74
-
isoenzyme ACS2
5.84
D1MF34
calculated
5.9
-
isoenzyme ACS2
5.93
A2IA37, A2IA38, A2IA39, A2IA40, A2IA41
-
6
-
isoenzyme ACS1
6.19
A2IA37, A2IA38, A2IA39, A2IA40, A2IA41
;
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
7.49
A2IA42, A2IA43, A2IA44
-
7.5
-
isoenzyme ACS5
7.61
-
isoenzyme ACS3
7.86
-
isoenzyme ACS1A
7.9
D8L307
calculated
8.2
-
isoenzyme ACS4
8.2
-
isoenzyme ACS1
8.23
-
isoenzyme ACS1B
8.48
A2IA37, A2IA38, A2IA39, A2IA40, A2IA41
-
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Q9SXN9
high expression level
Manually annotated by BRENDA team
Q06IN7 and Q06IN6
-
Manually annotated by BRENDA team
Citrullus colocynthis x lanatus
-
-
Manually annotated by BRENDA team
Q06IN7 and Q06IN6
-
Manually annotated by BRENDA team
Citrullus colocynthis x lanatus
-
-
Manually annotated by BRENDA team
Diospyros sp.
-
-
Manually annotated by BRENDA team
-
intact and wounded fruits of different ripening stages
Manually annotated by BRENDA team
-
wounded fruits
Manually annotated by BRENDA team
-
Pp-ACS1 is suppressed during fruit ripening in stony hard peaches
Manually annotated by BRENDA team
-
immature green, mature green, turning, pink, red, full ripe
Manually annotated by BRENDA team
Q66VB2
maximum expression in ripe fruit pulp, very low expression in ripe fruit peel
Manually annotated by BRENDA team
D8L307
transcript accumulation of ACS1 is detected at a low level only in the later stage of fruit ripening
Manually annotated by BRENDA team
Carica papaya Sinta
-
-
-
Manually annotated by BRENDA team
Citrullus colocynthis x lanatus
-
-
Manually annotated by BRENDA team
A9NIT9
of the seedling
Manually annotated by BRENDA team
O82125
plant growth apic, bud
Manually annotated by BRENDA team
Q06IN7 and Q06IN6
-
Manually annotated by BRENDA team
K0E1C1
enzyme expression increases during petals development
Manually annotated by BRENDA team
Q06IN7 and Q06IN6
newly elongated internode shoots prior to needle elongation
Manually annotated by BRENDA team
Q06IN7 and Q06IN6
-
Manually annotated by BRENDA team
Citrullus colocynthis x lanatus
-
-
Manually annotated by BRENDA team
Q06IN7 and Q06IN6
-
Manually annotated by BRENDA team
-
specific ACS isozymes are targets for regulation by protein phosphatase 2A during Arabidopsis thaliana seedling growth and reduced protein phosphatase 2A function causes increased ACS activity in the roots curl in 1-N-naphthylphthalamic acid 1 mutant
Manually annotated by BRENDA team
Citrullus colocynthis x lanatus
-
-
Manually annotated by BRENDA team
A2IA37, A2IA38, A2IA39, A2IA40, A2IA41
bud
Manually annotated by BRENDA team
Picea glauca PG29
-
bud
-
Manually annotated by BRENDA team
A2IA37, A2IA38, A2IA39, A2IA40, A2IA41
-
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
Citrullus colocynthis x lanatus
-
-
Manually annotated by BRENDA team
-
flower stem, expression pattern of the three different genes of 1-aminocyclopropane-1-carboxylate synthase in gravistimulated stems
Manually annotated by BRENDA team
Citrullus colocynthis x lanatus
B2WR79, B2WR80, B2WR81, B2WR82
ACS1 is not expressed in stem
Manually annotated by BRENDA team
Citrullus colocynthis x lanatus
-
-
Manually annotated by BRENDA team
Citrullus colocynthis x lanatus
B2WR79, B2WR80, B2WR81, B2WR82
the highest ACS1 transcript level is detected in tendrils
Manually annotated by BRENDA team
Q06IN7 and Q06IN6
-
Manually annotated by BRENDA team
additional information
Citrullus colocynthis x lanatus
B2WR79, B2WR80, B2WR81, B2WR82
not detecte in flower, leaf, shoot, stem, tendril, root, and cotyledon
Manually annotated by BRENDA team
additional information
Q66VB2
mRNA is not detected in root, stem and leaf tissues
Manually annotated by BRENDA team
additional information
Q9SXN9
no activity in root and petals, expression profiling, overview
Manually annotated by BRENDA team
additional information
K0E1C1
the enzyme expression levels in young tissues are higher than that in other tissues
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
associated with particulate fraction
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
45000
-
two-dimensional denaturing gel-electrophoresis
34584
48000
-
SDS-PAGE
34585
48000
-
immunoaffinity purification
34592
50000
-
SDS-PAGE
34565
50000
-
two-dimensional gel electrophoresis, gel filtration
34571
50000
A2IA37, A2IA38, A2IA39, A2IA40, A2IA41
predicted
682414
50400
A2IA37, A2IA38, A2IA39, A2IA40, A2IA41
predicted
682414
53800
-
conceptual translation
34587
57000
-
gel filtration
34567, 34574
58100
A2IA37, A2IA38, A2IA39, A2IA40, A2IA41
predicted
682414
58200
A2IA37, A2IA38, A2IA39, A2IA40, A2IA41
predicted
682414
58800
A2IA37, A2IA38, A2IA39, A2IA40, A2IA41
predicted
682414
58900
A2IA42, A2IA43, A2IA44
predicted
682414
96000
-
gel filtration
650624
100000
P23279
refolded enzyme, gel filtration
34582
100000
-
crosslinking, gel filtration
34588
125000
-
gel filtration
34566
160000
-
gel filtration
34570
160000
-
gel filtration
34572
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
Q6U5H3
x * 55000, SDS-PAGE
?
Q66VB2
x * 55000, SDS-PAGE
?
-
x * 50200, isoenzyme ACS2
?
-
x * 51000, isoenzymes ACS4 and ACS5
?
-
x * 52900, iosenzymes ACS1A and ACS1B
?
-
x * 53100, iosenzyme ACS1
?
-
x * 53100-54800
?
-
x * 53300, iosenzyme ACS2
?
-
x * 53800, iosenzymes ACS4 and ACS5
?
-
x * 54100, iosenzyme ACS1
?
-
x * 54600, iosenzyme ACS1
?
-
x * 55000, iosenzyme ACS2
?
-
x * 55000, iosenzymes ACS1 and ACS3
?
-
x * 55600, iosenzyme ACS2
?
-
x * 55800, iosenzyme ACS
?
-
x * 55800, iosenzyme ACS1A, x * 55900, iosenzyme ACS1B
?
-
x * 56000, iosenzyme ACS1
?
D1MF34
x * 48500, calculated
?
O24062, Q1HAW0, Q1HAW1
x * 50000, two-dimensional electrophoresis
?
D8L307
x * 27300, calculated
?
A2IBN7
x * 57000, SDS-PAGE, x * 57900, calculated
dimer
-
-
dimer
-
2 * 48000, SDS-PAGE
dimer
-
2 * 52000, SDS-PAGE
dimer
-
2 * 46000, SDS-PAGE
dimer
-
2 * 65000, SDS-PAGE
dimer
-
2 * 84000, SDS-PAGE
dimer
-
the Arabidopsis genome encodes nine ACS polypeptides that form eight functional (ACS2, ACS4-9, ACS-11) and one nonfunctional homodimer. Coexpressing the K278A and Y92A mutants of different polypeptides shows that all of them have the capacity to heterodimerize. Functional heterodimers are formed only among gen family members that belong to one or the other of the two phylogenetic branches. It is proposed that heterodimerization enhances the isoenzyme diversity of the ACS gene family and provides physiological versatility by being able to operate in a broad gradient of S-adenosylmethionine concentration in various cells/tussues during plant growth and development. Nonfunctional heterodimerization may also play a regulatory role during the plant life cycle
dimer
Penicillium citrinum AHU 8443
-
2 * 48000, SDS-PAGE
-
monomer
-
1 * 50000, SDS-PAGE, gel filtration
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
Q06402, Q9SAR0
RCN1-containing protein phosphatase 2A complexes specifically dephosphorylate a C-terminal ACS6 phosphopeptide
glycoprotein
K0E1C1
the enzyme harbors an N-glycosylation site
phosphoprotein
P18485
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
additional information
-
posttranslational regulation of ethylene biosynthesis
phosphoprotein
A2IBN7
cotton ACS2 interacts with Ca2+-dependent protein kinase CPK1. Bacterially expressed and purified recombinant ACS2 is phosphorylated by CPK1 in vitro and residue S460 is a possible phosphorylation site for CPK1. Phosphorylated ACS2 shows significantly increased ACS activity, leading to elevated ethylene production
additional information
Q10DK7
putative phosphorylation of the C-termini of ACS may promote interaction between ACS and 14-3-3 and may inhibit binding to ETO1 proteins, resulting in 1-aminocyclopropane-1-carboxylate and ethylene synthesis
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
P37821
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
Q66VB2
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
LITERATURE
6 - 7
-
-
34597
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
-
stable, for at least 3 h
34578
40
-
inactivated above
34566
42
-
50% loss of activity after 15 min
34578
52
-
97% loss of activity after 15 min
34578
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, 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
-
4°C, potassium buffer, 10 days, 50% activity lost
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
treatment with polyethylene glycol and acetone
-
inclusion body purified
P23279
by centrifugation and Sephadex G-25 column chromatography
-
by treatment with polyethylene glycol and acetone
Diospyros sp.
-
recombinant protein
A2IBN7
recombinant ACC synthase
-
recombinant C-terminally truncated ACC synthase
-
recombinant truncated form of ACC synthase
-
recombinant ACC synthase
-
by centrifugation and Sephadex G-25 column chromatography
A2IA37, A2IA38, A2IA39, A2IA40, A2IA41
recombinant ACC synthase
Q6U5H3
by (NH4)2SO4 saturation
P18485
isoenzyme LeACS2 and five ACC synthase mutants (Y151F, Y151G, Y152F, Y152G and Y151F/Y152F) in Escherichia coli
-
recombinant ACC synthase
-
by centrifugation and Sephadex G-25 column chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
-
expression in Escherichia coli
-
isoform ACS5, expression in Escherichia coli
Q37001
five clones from one gene existing as a single copy in Carica papaya Sinta genome
-
into plasmid pMOSblue-T
Q2EN04
expression in Escherichia coli
-
expression in Escherichia coli and Saccharomyces cerevisiae
-
gene DcACS1, recombinant expression in Escherichia coli
-
expression in Escherichia coli
A2IBN7
into Escherichia coli, PMD18-T vector for sequencing
A9NIT9
expressed in Escherichia coli BL21(DE3); expressed in Escherichia coli BL21(DE3); expressed in Escherichia coli BL21(DE3)
O24062, Q1HAW0, Q1HAW1
expression in Pichia pastoris
-
expression of ACC synthase in Escherichia coli
-
overexpression of C-terminally truncated ACC synthase in Pichia pastoris
-
expression in Escherichia coli
-
into Escherichia coli, pUC118 or pGEM-T Easy vector for sequencing
-
into the pGBKT7 in yeast
Q10DK7
DNA and amino acid sequence determination and analysis, genomic structure, sequence comparions and phylogenetic analysis
K0E1C1
expression in Escherichia coli and Saccharomyces cerevisiae
-
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
A2IA37, A2IA38, A2IA39, A2IA40, A2IA41
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
A2IA42, A2IA43, A2IA44
gene PpACS1a, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, real-time quantitative PCR expression analysis
Q9SXN9
expression of cDNA in Escherichia coli
Q6U5H3
-
D8L307
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
Q42881
expression in Escherichia coli
-
expression of C-terminal deletion mutant in Escherichia coli
-
expression of C-terminal truncated ACCC synthase in Escherichia coli
-
expression of the tomato isoenzyme Lw-ACS2 in Escherichia coli
-
overexpression of isoenzyme LeACS2 and five ACC synthase mutants (Y151F, Y151G, Y152F, Y152G and Y151F/Y152F) in Escherichia coli
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression in fruit skin 116 days after full bloom
P37821, Q9MB64
expression in fruit skin 16 and 37 days after full bloom
P37821, Q9MB64
the enzyme expression might be induced by the developmental signal
K0E1C1
the PpACS1a gene expression is regulated by salicylic acid and indole-3-acetic acid in fruits and during fruit ripening
Q9SXN9
ethylene is not a regulatory factor of RiEXPA1 expression in raspberry fruit
D8L307
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
S460G
A2IBN7
level of CPK1 phosphorylation is significantly decreased
S460G/S478A/S481A/S486A
A2IBN7
level of CPK1 phosphorylation is significantly decreased
S478A/S481A/S486A
A2IBN7
CPK1 phosphorylation efficiency does not significantly change compared to wild-type
A46V
P37821
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
O24062, Q1HAW0, Q1HAW1
naturally occuring mutation, no activity
K273A
-
no ACC synthase activity
R407L
-
20fold increase in Km for s-adenosyl-l-methionine
Y233F
-
24fold increase in Km
Y233F
-
24fold increase in Km for s-adenosyl-L-methionine
Y85A
-
inactive ACC synthase
Y85A
-
no ACC synthase activity
Y85F
-
partially active ACC synthase
Y85W
-
partially active ACC synthase
R407K
-
increase in Km for S-adenosyl-L-methionine and drop in kcat/Km
R286A
-
almost complete loss of activity
R286I
-
almost complete loss of activity
R286L
-
low affinity for both pyridoxal 5'-phosphate and S-adenosyl-L-methionine, 8000fold decrease in overall catalytic activity, i.e. kcat/Km
R286L
-
low affinity for pyridoxal 5' phosphate and S-adenosylmethionine
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
Q06402
transformation of Arabidopsis by the floral dip method to yield an AtACS4 and b-glucuronidase construct, characterization of atacs4, atacs8 and atacs4atacs8 knockouts, auxin-resistant 1, axr1-3, and auxin-resistant 2, axr2-1, mutants can not be activated by brassinosteroid
additional information
-
a transient expression system in Arabidopsis protoplasts is used to determine if the interaction with 14-3-3 protein increases the half-life of ACS5. Coexpression of HA-14-3-3v increases the half-life of myc-tagged ACS5 protein in this system
Y233F
-
24-fold increase in the Km for S-adenosyl-L-methionine and no change in kcat
additional information
-
-
additional information
-
deletion of residues 2-12 from the non-conserved N-terminus leads to slight increase in activity in vitro
additional information
-
deletion of the COOH terminus through Arg429 results in complete inactivation
additional information
-
deletion of 11 amino acids through Glu-23 from the N-terminus results in a substantial reduction of in vitro activity, deletion of residues 3 through 27, from the N-terminus abolished enzyme activity completely
additional information
-
deleltion of 46-52 amino acids from the COOH terminus results in an nine times higher affinity for S-adenosylmehtionine
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
P23279
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
-
harvest periods related to soluble solids contents content of Hayward kiwifruit significantly affect 1-aminocyclopropane-1-carboxylate synthase activity, total soluble protein content and protein profile. ACC synthase activity is suppressed, especially in early harvested fruits, by an inhibition of fruit ripening during controlled atmosphere storage
food industry
-
silencing of the ACACS2 gene using genetic engineering techniques can be used to control natural flowering in commercial situations
agriculture
Q06402
expression of ACC synthase is the rate limiting step in ethylene biosynthesis and is controlled by a multiple regulatory pathway of auxin, brassinosteroid and light in Arabidopsis seedlings
agriculture
-
ethylene overproduction in protein phosphatase 2A-deficient plants requires isoforms ACS2 and ACS6
agriculture
Q37001
identification of compounds inhibiting ethylene biosynthesis at the step of converting S-adenosylmethionine to 1-aminocyclopropane-1-carboxylic acid by ACC synthase
agriculture
Q2EN04
ethylene is produced in increasing amounts during the germination process, the embryonic axis is the main producer, the abundance of Ca-ACS1 mRNA was highest at the onset of embryogenesis (stage-1), middle (stages 3–6) and low desiccation stages and dry seed, the transcript levels of Ca-ACS1 does not correlate with ACS activity
agriculture
O82125
1-aminocyclopropane-1-carboxylate synthase is the rate-limiting enzyme in the ethylene biosynthetic pathway, which is the major plant hormone regulating female sex expression, an additional copy of the Cs-ACS1 gene is linked to the female locus, this female-specific Cs-ACS1G originates from a gene duplication between the branched-chain amino acid transaminase gene and Cs-ACS1 gene
agriculture
A0JBY6
expression of CyACS1 is involved in high-temperature induced necrosis of plant tissue
agriculture
-
ethylene production in cut carnation flowers cv. Excerea is suppressed by high-temperatures because of inhibition of ACC synthase, no ethylene production detected in flowers kept at 32°C, climacteric ethylene production observed during days 9-12 in flowers kept at 24°C
food industry
Diospyros sp.
-
wounding and pre-treatment with 1-methylcyclopropene promotes ethylene production by inducing expression of the ACC synthase, which accelerates persimmon fruit softening
agriculture
A9NIT9
1-aminocyclopropane-1-carboxylate synthase is the rate-limiting enzyme in ethylene biosynthesises, its mRNA expression is induced by abiotic factors like wounding, treatment with abscisic acid, and CuCl2
food industry
-
due to increased ACC synthesis treatment with 0.5 ml/l of ethylene for 12 h accelerates ripening of the fruits, fruits are edible 3 days after treatment, compared to 6-7 days for untreated mangoes
food industry
-
1-aminocyclopropane-1-carboxylate synthase is the rate-limiting enzyme in ethylene biosynthesises, ethylene biosynthesis in ripening banana fruit is controlled differently in the pulp tissue and in the peel tissue, treatment with 1-methylcyclopropene, an ethylene action inhibitor, either induces or prevents 1-aminocyclopropane-1-carboxylate (ACC) synthase activity
agriculture
Q10DK7
ethylene governs both development and stress responses throughout plant development, the mechanism by which plants regulate ethylene biosynthesis is unclear, 14-3-3 proteins are required to cause a change in ACS function after phosphorylation
agriculture
-
the enzyme regulates ethylene production in conifers, ethylene signalling induces chemical defenses against insects or pathogens
agriculture
Picea glauca PG29
-
the enzyme regulates ethylene production in conifers, ethylene signalling induces chemical defenses against insects or pathogens
-
agriculture
-
the enzyme regulates ethylene production in conifers, ethylene signalling induces chemical defenses against insects or pathogens
agriculture
-
ethylene governs both development and stress responses throughout plant development, the mechanism by which plants regulate ethylene biosynthesis is unclear, ethylene overproducer 1 protein is a negative regulator of ethylene biosynthesis that inhibits the activity of 1-aminocyclopropane-1-carboxylate synthase and promotes its degradation by a proteasome dependent pathway
agriculture
P18485
UV-B radiation influences ethylene biosynthesis by changes in the expression of the ACC synthase
food industry
-
chilling stress induces increased ethylene production, O2 – is involved in the chilling induced increases in ACS activity, but not H2O2