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Information on EC 4.4.1.14 - 1-aminocyclopropane-1-carboxylate synthase
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4.4.1.14 1-aminocyclopropane-1-carboxylate synthaseIUBMB Comments
A pyridoxal-phosphate protein. The enzyme catalyses an alpha,gamma-elimination.
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Word Map
- 4.4.1.14
-
dipeptidyl
- ethylene
-
peptidase-4
-
glucagon-like
-
incretins
- tomato
-
peptide-1
-
antidiabetic
- metformin
-
ripening
-
glycemic
- vildagliptin
- linagliptin
-
hypoglycemia
- glucagon
-
monotherapy
- esculentum
- sulfonylurea
-
insulinotropic
-
postprandial
-
dpp-4is
-
glucose-lowering
- saxagliptin
- lycopersicon
-
glucose-dependent
- auxin
- alogliptin
-
exenatide
-
liraglutide
- agriculture
-
antihyperglycemic
-
climacteric
- aminoethoxyvinylglycine
-
add-on
-
gliptins
-
incretin-based
- caryophyllus
-
ethylene-forming
- dianthus
-
auxin-induced
-
once-weekly
- 1-methylcyclopropene
-
sglt-2
-
ethylene-induced
-
sodium-glucose
-
dipeptidyl-peptidase
-
ethephon
- carnation
- food industry
-
sulphonylureas
- glimepiride
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
Synonyms
acc synthase, 1-aminocyclopropane-1-carboxylic acid synthase, le-acs2, acs-1, leacs2, le-acs4, le-acs3, ghacs1, le-acs6, le-acs1a, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
1-aminocyclopropane carboxylic acid synthase
1-aminocyclopropane-1-carboxylate synthase
1-aminocyclopropane-1-carboxylate synthase 4
1-aminocyclopropane-1-carboxylate synthetase
-
-
-
-
1-aminocyclopropane-1-carboxylic acid synthase
ACC synthase
ACS
ACS1
ACS2
ACS3
ACS4
ACS5
ACS6
aminocyclopropane-1-carboxylate synthase
aminocyclopropanecarboxylate synthase
-
-
-
-
aminocyclopropanecarboxylic acid synthase
-
-
-
-
PgACS4
S-adenosyl-L-methionine methylthioadenosine-lyase
synthase, 1-aminocyclopropanecarboxylate
-
-
-
-
type 2 1-aminocyclopropane-1-carboxylate synthase
1-aminocyclopropane carboxylic acid synthase
-
1-aminocyclopropane-1-carboxylate synthase
-
1-aminocyclopropane-1-carboxylic acid synthase
-
-
-
-
ACC synthase
-
-
-
-
ACC synthase
-
aminocyclopropane-1-carboxylate synthase
-
-
-
-
S-adenosyl-L-methionine methylthioadenosine-lyase
-
-
-
-
S-adenosyl-L-methionine methylthioadenosine-lyase
-
S-adenosyl-L-methionine methylthioadenosine-lyase
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine = 1-aminocyclopropane-1-carboxylate + methylthioadenosine
-
-
-
-
S-adenosyl-L-methionine = 1-aminocyclopropane-1-carboxylate + methylthioadenosine
stereochemistry
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
elimination
additional information
elimination
-
-
alpha, gamma-elimination; of H2S or RSH, C-S bond cleavage
-
additional information
14-3-3 protein may inhibit binding to ethylene overproducer 1 proteins, resulting in 1-aminocyclopropane-1-carboxylate and ethylene synthesis
additional information
two introns are in the genomic DNA sequence, Southern blot analysis suggests that there might be a multi-gene family encoding for ACC synthase, alignment analysis shows a close association with the wound-inducible ACS of citrus
additional information
-
by Agrobacterium mediated transformation, two transgenic pineapple lines have been produced containing co-suppression constructs designed to down-regulate the expression of the ACACS2 gene
additional information
high levels of expression of CyACS1 in the necrotic inflorescences of wild-type Cymbidium at high temperatures, no bud necrosis in the mericlone mutant, but application of exogenous ACC or ethephon to the young inflorescences of nhn restored the high-temperature necrosis response
additional information
LE-ACS3 shows a strong interaction with the protein ethylene overproducer 1, the C-terminal tail of ACS is essential for the interaction with ethylene overproducer 1 and signals the proteasome-dependent protein destabilization
additional information
-
LE-ACS3 shows a strong interaction with the protein ethylene overproducer 1, the C-terminal tail of ACS is essential for the interaction with ethylene overproducer 1 and signals the proteasome-dependent protein destabilization
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PATHWAY SOURCE
PATHWAYS
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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.
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CAS REGISTRY NUMBER
COMMENTARY
72506-68-4
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-arginine + pyridoxal 5'-phosphate
2-oxo-5-guanidinopentanoate + pyridoxamine 5'-phosphate
-
-
-
?
L-aspartate + pyridoxal 5'-phosphate
2-oxo-succinate + pyridoxamine 5'-phosphate
-
very slow transamination activity
-
?
L-phenylalanine + pyridoxal 5'-phosphate
2-oxo-3-phenylpropanoate + pyridoxamine 5'-phosphate
-
slow transamination activity
-
?
pyridoxal 5'-phosphate + alanine
pyridoxamine 5'-phosphate + pyruvate
-
-
-
?
S-methyl-L-methionine + pyridoxal 5'-phosphate
4-dimethylsulfonium-2-oxobutyrate + pyridoxamine 5'-phosphate
-
transamination reaction
-
?
(R,S)-S-adenosyl-L-methionine
vinylglycine + methylthioadenosine
-
-
-
?
(R,S)-S-adenosyl-L-methionine
vinylglycine + methylthioadenosine
-
-
-
?
(S,S)-S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
-
-
-
?
(S,S)-S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
-
-
-
?
L-alanine + pyridoxal 5'-phosphate
pyruvate + pyridoxamine 5'-phosphate
-
-
-
?
L-alanine + pyridoxal 5'-phosphate
pyruvate + pyridoxamine 5'-phosphate
-
-
-
?
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
-
-
-
-
?
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
-
-
-
?
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
-
-
-
-
?
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
-
-
-
?
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
-
-
-
?
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
-
-
-
?
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
-
-
-
?
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
-
-
-
?
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
-
-
-
?
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
-
-
-
?
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
-
-
-
?
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
-
-
-
?
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
-
biosynthesis of ethylene: plant hormone
-
-
-
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
-
-
-
?
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
biosynthesis of ethylene: plant hormone
-
-
-
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
-
biosynthesis of ethylene: plant hormone
-
-
-
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
-
-
-
?
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
-
-
-
-
?
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
-
-
-
-
?
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
Diospyros sp.
-
-
-
-
?
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
-
-
-
?
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
-
-
-
?
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
-
-
-
?
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
-
-
-
?
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
-
-
-
?
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
-
-
-
?
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
-
-
-
?
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
-
-
-
?
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
-
-
-
?
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
-
-
-
?
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
-
rate-determining step in the biosynthesis of ethylene
-
?
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
-
biosynthesis of ethylene: plant hormone
-
-
-
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
-
-
-
-
?
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
-
-
-
-
?
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
-
-
-
?
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
-
-
-
?
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
-
-
-
?
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
-
-
-
?
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
-
-
-
?
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
-
-
-
?
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
-
-
-
?
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
-
-
-
?
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
-
-
-
?
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
-
-
-
?
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
-
-
-
?
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
-
-
-
?
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
-
-
-
?
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
-
-
?
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
-
-
-
-
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
-
-
-
-
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
-
-
-
-
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
-
-
-
?
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
-
-
-
?
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
-
-
-
?
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
-
-
-
-
?
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
-
-
-
?
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
-
-
-
ir
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
-
-
-
ir
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
-
-
-
?
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
-
-
-
?
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
-
biosynthesis of ethylene: plant hormone
-
-
-
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
-
-
-
?
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
-
-
-
?
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
-
biosynthesis of ethylene: plant hormone
-
-
-
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
-
-
-
-
?
S-methyl-L-methionine
alpha-ketobutyrate + ammonia + dimethylsulfide
-
-
-
?
S-methyl-L-methionine
alpha-ketobutyrate + ammonia + dimethylsulfide
-
beta,gamma elimination of dimethylsulfide to yield enzyme bound L-vinylglycine, which is subsequently converted to alpha-ketobutyrate and ammonia
-
?
additional information
?
-
-
enzyme activity may affect net photosynthetic rate through ethylene-induced changes on foliar gas exchange and leaf growth
-
-
-
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
?
-
-
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
?
-
-
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
-
-
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
?
-
ACS6 is involved in system-1 ethylene production in preclimacteric fruit
-
-
-
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
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(R,S)-S-adenosyl-L-methionine
vinylglycine + methylthioadenosine
-
-
-
?
(S,S)-S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
-
-
-
?
L-alanine + pyridoxal 5'-phosphate
pyruvate + pyridoxamine 5'-phosphate
-
-
-
?
S-methyl-L-methionine
alpha-ketobutyrate + ammonia + dimethylsulfide
-
-
-
?
S-methyl-L-methionine + pyridoxal 5'-phosphate
4-dimethylsulfonium-2-oxobutyrate + pyridoxamine 5'-phosphate
-
transamination reaction
-
?
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
-
-
-
?
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
-
-
-
?
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
-
-
-
?
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
-
-
-
?
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
-
-
-
?
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
-
-
-
?
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
-
biosynthesis of ethylene: plant hormone
-
-
-
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
-
-
-
?
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
P23279
biosynthesis of ethylene: plant hormone
-
-
-
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
-
biosynthesis of ethylene: plant hormone
-
-
-
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
-
-
-
-
?
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
-
-
-
?
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
-
-
-
?
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
-
-
-
?
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
-
-
-
?
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
-
-
-
?
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
-
-
-
?
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
-
rate-determining step in the biosynthesis of ethylene
-
?
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
-
biosynthesis of ethylene: plant hormone
-
-
-
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
-
-
-
?
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
-
-
-
?
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
-
-
-
?
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
-
-
-
?
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
-
-
-
?
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
Q6U5H3
-
-
?
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
-
-
-
?
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
-
-
-
?
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
-
-
-
?
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
-
biosynthesis of ethylene: plant hormone
-
-
-
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
-
-
-
?
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
-
-
-
?
S-adenosyl-L-methionine
1-aminocyclopropane-1-carboxylate + methylthioadenosine
-
biosynthesis of ethylene: plant hormone
-
-
-
additional information
?
-
-
enzyme activity may affect net photosynthetic rate through ethylene-induced changes on foliar gas exchange and leaf growth
-
-
-
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
?
-
-
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
?
-
-
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
?
-
Q94LA1
ACS6 is involved in system-1 ethylene production in preclimacteric fruit
-
-
-
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
-
-
-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
-
pyridoxal 5'-phosphate
-
-
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
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(2E,3E)-4-(2-aminoethoxy)-2-[([3-hydroxy-2-methyl-5[(phosphonooxy)methyl]pyridin-4-yl]methyl)imino] but-3-enoic acid
-
1-aminoethoxyvinyl glycine
-
1-methylcyclopropene
completely inhibits the ethylene-associated transcription of isozyme ACS1 in the whole fruit; completely inhibits the ethylene-associated transcription of isozyme ACS4 in the whole fruit
2-(cyclopentylamino)-7,7-dimethyl-7,8-dihydroquinazolin-5(6H)-one
inhibition of ethylene biosynthesis at the step of converting S-adenosylmethionine to 1-aminocyclopropane-1-carboxylic acid by ACC synthase
2-(cyclopentylamino)-7-(4-methylphenyl)-7,8-dihydroquinazolin-5(6H)-one
inhibition of ethylene biosynthesis at the step of converting S-adenosylmethionine to 1-aminocyclopropane-1-carboxylic acid by ACC synthase
2-aminooxyisobutyric acid
-
75% inhibition at 1.1 mM. The compound's action resembles aminooxyacetic acid. The inhibitor significantly increases the vase life of cut flowers by highly reducing the ethylene production through inhibition of the enzyme
2-[(3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl)-imino]-5-phosphonopent-3-enoic acid
-
7-(4-methoxyphenyl)-2-(phenylamino)-7,8-dihydroquinazolin-5(6H)-one
inhibition of ethylene biosynthesis at the step of converting S-adenosylmethionine to 1-aminocyclopropane-1-carboxylic acid by ACC synthase
EOL1
-
also named ETO1-LIKE 1, directs the degradation of type-2 ACS proteins (ACS4, ACS5 and ACS9) but not of type-1 or type-3 ACSs
-
ethylene
ACS6 is negatively regulated by endogenous and exogenous ethylene
S-methyl-L-methionine
-
covalent inactivation after elimination of dimethylsulfide
(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
-
(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
-
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
-
strong binding capacity
-
2-[(3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl)-imino]-5-phosphonopent-3-enoic acid
-
strong binding capacity
-
L-Vinylglycine
-
approx. 60% loss of activity after 5 min, approx. 90% loss of activity after 40 min, biphasic inativation, mechanism based inhibition
S-adenosyl-L-methionine
-
inactivation during catalytic action, (+) and (+/-) isomer
sinefungin
-
naturally occuring antifungal antibiotic isolated from Streptomyces griseus
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1-naphthyl acetic acid
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 butyric acid
plant tissues treated with 3-indole butyric acid exhibit dramatic increases in isozyme ACS1 level; plant tissues treated with 3-indole butyric acid exhibit dramatic increases in isozyme ACS3 level; plant tissues treated with 3-indole butyric acid exhibit dramatic increases in isozyme ACS5 level
abscisic acid
-
exogenous treatment with abscisic acid increases the promoter activity of ACS4
cytokinin
a dramatic increase in ACS1 transcript levels is detected with increasing cytokinin concentrations (0.004-0.04 mM)
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
0.05 mM
jasmonic acid
-
exogenous treatment with jasmonic acid increases the promoter activity of ACS4
1-aminocyclopropane-1-carboxylate
-
the expression of ACS7 is enhanced by 0.02 mM 1-aminocyclopropane-1-carboxylate
1-aminocyclopropane-1-carboxylate
expression of ACS1 is up-regulated by exogenous treatment with 0.1 mM 1-aminocyclopropane-1-carboxylate
3-indole acetic acid
-
exogenous treatment with 3-indole acetic acid increases the promoter activity of ACS4
3-indole acetic acid
3-indole acetic acid applied to the cotyledons of seedlings causes a clear increase of ACS mRNA
3-indole acetic acid
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
auxin
expression of ACS1 is up-regulated by exogenous treatment with auxin
ethylene
-
ethylene enhances the promoter activities of ACS4 and ACS7 genes but exhibits no obvious impacts on that of ACS5
ethylene
activates transcription of isozyme ACS1; activates transcription of isozyme ACS4
gibberellin
expression of ACS1 is up-regulated by exogenous treatment with 0.5 mM gibberellin
gibberellin
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
additional information
-
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
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
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
B2XCJ8; B2XCJ9; B2XCK0
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
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
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
-
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
-
additional information
-
scavengers of reactive oxygen species like 1,4-diazabicyclo(2,2,2) octane, superoxide dismutase, n-propyl gallate, catalase have no effect
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.02927
S-adenosyl-L-methionine
-
without chilling in the presence of xanthine–xanthine oxidase and catalase
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
0.03977
S-adenosyl-L-methionine
-
8 h after chilling in the presence of catalase; 8 h after chilling in the presence of n-propyl gallate
0.04056
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
0.04136
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
0.05712
S-adenosyl-L-methionine
-
without chilling in the presence of H2O2
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000015
7-(4-methoxyphenyl)-2-(phenylamino)-7,8-dihydroquinazolin-5(6H)-one
pH 8.0, 25°C
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0079
2-(cyclopentylamino)-7,7-dimethyl-7,8-dihydroquinazolin-5(6H)-one
Arabidopsis thaliana
Q37001
pH 8.0, 25°C
0.0014
2-(cyclopentylamino)-7-(4-methylphenyl)-7,8-dihydroquinazolin-5(6H)-one
Arabidopsis thaliana
Q37001
pH 8.0, 25°C
0.0005
7-(4-methoxyphenyl)-2-(phenylamino)-7,8-dihydroquinazolin-5(6H)-one
Arabidopsis thaliana
Q37001
pH 8.0, 25°C
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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
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.5
9.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 10
7.5 - 9.5
-
pH 7.5: about 50% of maximal activity, pH 9.5: about 60% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.7
6.4
7.5
8.2
5.7
A0A0U1ZAV5, A0A0U1ZDW5, A0A0U1ZF86
calculated from sequence; calculated from sequence
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Ruby Eyes ‘Golden Star’ and its mericlone mutant, non-high-temperature-induced necrosis (nhn) mutant that is tolerant of high temperatures
SwissProt
brenda
isozyme ACS1; Japanese morning glory, formerly Pharbitis nil, cultivar Violet
UniProt
brenda
brassinosteroid enhances the expression of the auxin-responsive ACC synthase 4
SwissProt
brenda
isozyme ACS1; variant lanatus
B2WR79
UniProt
brenda
isozyme ACS2, fragment; variant lanatus
UniProt
brenda
isozyme ACS3; variant lanatus
UniProt
brenda
isozyme ACS4, fragment; variant lanatus
UniProt
brenda
L. var sativus cv Beit Alpha monoecious ffMM and gynoecious FFMM
SWISSPROT
brenda
ACS is encoded by a multigen family, consisting of at least five members
-
-
brenda
isozyme ACS3, fragments; cultivars Early Golden and Shiro
B2XCJ8; B2XCJ9; B2XCK0
UniProt
brenda
isozyme ACS4, fragment; cultivars Early Golden and Shiro
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
newly elongated internode shoots prior to needle elongation
brenda
-
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
brenda
wounded bark; wounded bark; wounded bark
brenda
the highest ACS1 transcript level is detected in tendrils
brenda
additional information
24 h after wounding; 24 h after wounding; 24 h after wounding
brenda
-
brenda
-
brenda
ripening-specific; ripening-specific; ripening-specific
brenda
maximum expression in ripe fruit pulp, very low expression in ripe fruit peel
brenda
-
Pp-ACS1 is suppressed during fruit ripening in stony hard peaches
brenda
-
isoforms ACS1 and ACS4 show ripening-related increased expression during fruit development and ripening in cultivar CN13. The expression of isoform ACS5 decreases during fruit development
brenda
transcript accumulation of ACS1 is detected at a low level only in the later stage of fruit ripening
brenda
immature green, mature green, turning, pink, red, full ripe; immature green, mature green, turning, pink, red, full ripe
brenda
-
brenda
-
brenda
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; 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; 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
brenda
-
brenda
-
flower stem, expression pattern of the three different genes of 1-aminocyclopropane-1-carboxylate synthase in gravistimulated stems
brenda
ACS1 is not expressed in stem
brenda
additional information
B2WR79
not detecte in flower, leaf, shoot, stem, tendril, root, and cotyledon
brenda
additional information
not detecte in flower, leaf, shoot, stem, tendril, root, and cotyledon
brenda
additional information
not detecte in flower, leaf, shoot, stem, tendril, root, and cotyledon
brenda
additional information
not detecte in flower, leaf, shoot, stem, tendril, root, and cotyledon
brenda
additional information
mRNA is not detected in root, stem and leaf tissues
brenda
additional information
constitutively expressed in all tested organs
brenda
additional information
-
constitutively expressed in all tested organs
brenda
additional information
the enzyme expression levels in young tissues are higher than that in other tissues
brenda
additional information
no activity in root and petals, expression profiling, overview
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
the enzyme belongs to type-1 subfamily of plant 1-aminocyclopropane-1-carboxylate synthases
metabolism
physiological function
additional information
-
14-3-3 proteins interact with multiple 1-aminocyclopropane-1-carboxylate synthase isoforms in Arabidopsis thaliana, 14-3-3 likely acts on all three classes of enzyme proteins
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
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
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
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
metabolism
-
abscisic acid, auxin, gibberellic acid, methyl jasmonic acid, and salicylic acid differentially regulate the stability of ACS proteins, with distinct effects on various isoforms. Heterodimerization between ACS isoforms from distinct subclades results in increased stability of the shorter-lived partner, i.e. isoform ACS7 has a regulatory function to influence the stability of type-1 and type-2 ACS proteins through the formation of heterodimers
physiological function
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; ethylene overproduction in protein phosphatase 2A-deficient plants requires isoforms ACS2 and ACS6
physiological function
the enzyme might be involved in fruit ripening and in response to salicylic acid, indole-3-acetic acid, and disease
physiological function
transgenic Arabidopsis thaliana plants expressing Lycopersicum esculentum gamma-glutamyl-cysteine synthetase exhibit remarkable upregulation of isoforms ACS2, ACS6, and ACO1 at transcript as well as protein levels, while they are downregulated in the GSH-depleted phytoalexin deficient2-1 mutant. Presence of enhanced levels of GSH induce ACS2 and ACS6 transcription in a WRKY33-dependent manner, while ACO1 transcription remains unaffected; transgenic Arabidopsis thaliana plants expressing Lycopersicum esculentum gamma-glutamyl-cysteine synthetase exhibit remarkable upregulation of isoforms ACS2, ACS6, and ACO1 at transcript as well as protein levels, while they are downregulated in the GSH-depleted phytoalexin deficient2-1 mutant. Presence of enhanced levels of GSH induce ACS2 and ACS6 transcription in a WRKY33-dependent manner, while ACO1 transcription remains unaffected
physiological function
ethylene production is associated with ACS1 transcription
physiological function
-
lack of isoform ACS1 expression is solely responsible for low levels of ethylene production in cultivar CN16
Show AA Sequence and Transmembrane Helices (213 entries)
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Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
48000
50000
53800
54100
54600
55000
55800
57000
100000
160000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
?
-
x * 53800, iosenzymes ACS4 and ACS5; x * 54600, iosenzyme ACS1; x * 55600, iosenzyme ACS2
?
A0A0U1ZAV5, A0A0U1ZDW5, A0A0U1ZF86
x * 49180, calculated from sequence; x * 49250, calculated from sequence; x * 52660, calculated from sequence; x * 54050, calculated from sequence; x * 54200, calculated from sequence; x * 54430, calculated from sequence; x * 54600, calculated from sequence
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
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
additional information
phosphoprotein
RCN1-containing protein phosphatase 2A complexes specifically dephosphorylate a C-terminal ACS6 phosphopeptide
phosphoprotein
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
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
additional information
-
posttranslational regulation of ethylene biosynthesis
additional information
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
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CRYSTALLIZATION/commentary
ORGANISM
UNIPROT
LITERATURE
crystal structure of ACC synthase in complex with the substrate analogue [2-(aminooxy)ethyl](5'deoxyadenosin-5'-yl)(methyl)sulfonium at 2.01 A resolution, crystals are obtained with the sitting drop method, 0.001 ml of protein solution, consisting of 20 mg/ml ACC synthase, 10 mM [2-(aminooxy)ethyl](5'deoxyadenosin-5'-yl)(methyl)sulfonium, 50 mM HEPES, pH 7.9, 0.01 mM pyridoxal 5'-phosphate, 1 mM dithiothreitol, is mixed with 0.001 ml of precipitating solution containing 30% 2-methyl-2-4-pentanediol and 50 mM MES, pH 6.5
-
recombinant enzyme, cocrystals of the enzyme-L-vinylglycine complex are obtained by sitting drop method. The crystals belong to space group C2 with cell constants a = 103.3 A, b = 59.4 A, c = 79.0 A, beta = 124.2°. The crystal structure of the covalent adduct of the inactivated enzyme is determined at 2.25 A resolution
-
to 1.35 A resolution. The internal aldimine Schiff base linking the C4' atom of the pyridoxal 5'-phosphate cofactor and the side chain nitrogen of K273 in the N'-pyridoxyl-lysine-5'-monophosphate adduct coexists with a small portion, about 20%, of free K273. Modeling of the mutation A46V, corresponding to A57V in Cucumis melo, which results in andromonoecious plants. The mutation changes the structure of the neighbouring active site residues only marginally. The mutation may cause an improper orientation of SAM in the active site
in silico three-dimensional modelling. The overall structure of the modelled binding site for pyridoxal 5'-phosphate and aminoethylvinylglycine in ACS1 is very similar to the known structure for the binding site in apple and tomato ACC synthase. The structures show good conservation of the catalytic residues
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
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
S460G/S478A/S481A/S486A
level of CPK1 phosphorylation is significantly decreased
S478A/S481A/S486A
CPK1 phosphorylation efficiency does not significantly change compared to wild-type
A46V
modeling of the mutation, corresponding to A57V in Cucumis melo, which results in andromonoecious plants. The mutation changes the structure of the neighbouring active site residues only marginally. The mutation may cause an improper orientation of SAM in the active site
Y233F
Y85A
Y233F
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24-fold increase in the Km for S-adenosyl-L-methionine and no change in kcat
R286L
additional information
R286L
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low affinity for pyridoxal 5' phosphate and S-adenosylmethionine
R286L
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low affinity for both pyridoxal 5'-phosphate and S-adenosyl-L-methionine, 8000fold decrease in overall catalytic activity, i.e. kcat/Km
additional information
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
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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
additional information
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deletion of 11 amino acids through Glu-23 from the N-terminus results in a substantial reduction of in vitro activity; deletion of residues 2-12 from the non-conserved N-terminus leads to slight increase in activity in vitro; deletion of residues 3 through 27, from the N-terminus abolished enzyme activity completely
additional information
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deleltion of 46-52 amino acids from the COOH terminus results in an nine times higher affinity for S-adenosylmehtionine; deletion of the COOH terminus through Arg429 results in complete inactivation
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
by centrifugation and Sephadex G-25 column chromatography
isoenzyme LeACS2 and five ACC synthase mutants (Y151F, Y151G, Y152F, Y152G and Y151F/Y152F) in Escherichia coli
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partial
recombinant ACC synthase
by centrifugation and Sephadex G-25 column chromatography
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CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
cloning of LE-ACS1A into the two-hybrid vector pACT2 in yeast; cloning of LE-ACS2 into the two-hybrid vector pACT2 in yeast; cloning of LE-ACS3 into the two-hybrid vector pACT2 in yeast, the C-terminus of LE-ACS3 is fused to the C-terminus of green fluorescent protein GFP and transformed into rice calli and Arabidopsis by Agrobacterium-mediated transformation; cloning of LE-ACS4 into the two-hybrid vector pACT2 in yeast; cloning of LE-ACS6 into the two-hybrid vector pACT2 in yeast
coexpression of HA-tagged EOL2, HA-tagged isozyme ACS5, and increasing levels of HA-tagged 14-3-3omega protein in Arabidospis thaliana protoplasts, seedling phenotypes, overview
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DNA and amino acid sequence determination and analysis, genomic structure, sequence comparions and phylogenetic analysis
expressed in Escherichia coli BL21(DE3); expressed in Escherichia coli BL21(DE3); expressed in Escherichia coli BL21(DE3)
expression in Escherichia coli
expression in Escherichia coli and Saccharomyces cerevisiae
five clones from one gene existing as a single copy in Carica papaya Sinta genome
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gene PpACS1a, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, real-time quantitative PCR expression analysis
into Escherichia coli, pCR2.1-TOPO vector for sequencing; into Escherichia coli, pCR2.1-TOPO vector for sequencing; into Escherichia coli, pCR2.1-TOPO vector for sequencing
into Escherichia coli, pCR2.1-TOPO vector for sequencing; into Escherichia coli, pCR2.1-TOPO vector for sequencing; into Escherichia coli, pCR2.1-TOPO vector for sequencing; into Escherichia coli, pCR2.1-TOPO vector for sequencing; into Escherichia coli, pCR2.1-TOPO vector for sequencing
overexpression of isoenzyme LeACS2 and five ACC synthase mutants (Y151F, Y151G, Y152F, Y152G and Y151F/Y152F) in Escherichia coli
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
ethylene is not a regulatory factor of RiEXPA1 expression in raspberry fruit
expression in fruit skin 116 days after full bloom; expression in fruit skin 16 and 37 days after full bloom
isoforms ACS1 and ACS4 show ripening-related increased expression during fruit development and ripening in cultivar CN13. The expression of isoform ACS5 decreases during fruit development
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presence of oligogalacturonic acids upregulates expression of both ACC synthase ACS2 and ACC oxidase ACO1
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the PpACS1a gene expression is regulated by salicylic acid and indole-3-acetic acid in fruits and during fruit ripening
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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
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
food industry
agriculture
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
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
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
agriculture
UV-B radiation influences ethylene biosynthesis by changes in the expression of the ACC synthase
agriculture
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
expression of CyACS1 is involved in high-temperature induced necrosis of plant tissue
agriculture
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
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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
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; 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
the enzyme regulates ethylene production in conifers, ethylene signalling induces chemical defenses against insects or pathogens; the enzyme regulates ethylene production in conifers, ethylene signalling induces chemical defenses against insects or pathogens; the enzyme regulates ethylene production in conifers, ethylene signalling induces chemical defenses against insects or pathogens; the enzyme regulates ethylene production in conifers, ethylene signalling induces chemical defenses against insects or pathogens; 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; the enzyme regulates ethylene production in conifers, ethylene signalling induces chemical defenses against insects or pathogens; the enzyme regulates ethylene production in conifers, ethylene signalling induces chemical defenses against insects or pathogens
agriculture
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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
agriculture
identification of compounds inhibiting ethylene biosynthesis at the step of converting S-adenosylmethionine to 1-aminocyclopropane-1-carboxylic acid by ACC synthase
agriculture
ethylene overproduction in protein phosphatase 2A-deficient plants requires isoforms ACS2 and ACS6; ethylene overproduction in protein phosphatase 2A-deficient plants requires isoforms ACS2 and ACS6
agriculture
-
oligogalacturonic acids promote tomato fruit ripening by inducing ethylene synthesis through the regulation of isoform ACS2 at transcriptional and post-translational levels
agriculture
-
the enzyme regulates ethylene production in conifers, ethylene signalling induces chemical defenses against insects or pathogens
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food industry
Diospyros sp.
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wounding and pre-treatment with 1-methylcyclopropene promotes ethylene production by inducing expression of the ACC synthase, which accelerates persimmon fruit softening
food industry
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silencing of the ACACS2 gene using genetic engineering techniques can be used to control natural flowering in commercial situations
food industry
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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
food industry
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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
-
chilling stress induces increased ethylene production, O2 – is involved in the chilling induced increases in ACS activity, but not H2O2
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