Information on EC 3.5.99.7 - 1-aminocyclopropane-1-carboxylate deaminase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY
3.5.99.7
-
RECOMMENDED NAME
GeneOntology No.
1-aminocyclopropane-1-carboxylate deaminase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
1-aminocyclopropane-1-carboxylate + H2O = 2-oxobutanoate + NH3
show the reaction diagram
apyridoxal 5-phosphate enzyme. Its introduction has been used to make fruit ripening dependent on externally added ethylene, as it removes the substrate for endogenous ethylene formation
-
-
-
1-aminocyclopropane-1-carboxylate + H2O = 2-oxobutanoate + NH3
show the reaction diagram
ring cleavage is regiospecific and only occurs between the pro-S and the alpha-carbon of 1-aminocyclopropane-1-carboxylate; stereochemistry
-
1-aminocyclopropane-1-carboxylate + H2O = 2-oxobutanoate + NH3
show the reaction diagram
stereochemistry
-
1-aminocyclopropane-1-carboxylate + H2O = 2-oxobutanoate + NH3
show the reaction diagram
ring cleavage of 1-aminocyclopropane-1-carboxylate is a nucleophilic-addition initiated event
-
1-aminocyclopropane-1-carboxylate + H2O = 2-oxobutanoate + NH3
show the reaction diagram
mechanism
-
1-aminocyclopropane-1-carboxylate + H2O = 2-oxobutanoate + NH3
show the reaction diagram
mechanism
-
1-aminocyclopropane-1-carboxylate + H2O = 2-oxobutanoate + NH3
show the reaction diagram
ring cleavage is induced by a nucleophilic attack at the pro-S-beta-methylene carbon of substrate, with Tyr294 as the nucleophile. Alternatively, ring opening is acid-catalyzed and may be facilitated by charge relay through pyridoxal 5-phosphate, with Tyr294 as general acid
Q00740
1-aminocyclopropane-1-carboxylate + H2O = 2-oxobutanoate + NH3
show the reaction diagram
reaction mechanism, detailed overview
-
1-aminocyclopropane-1-carboxylate + H2O = 2-oxobutanoate + NH3
show the reaction diagram
reaction mechanism, detailed overview
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Deamination
-
-
Deamination
Pseudomonas putida UW4
-
-
-
elimination
-
-
of gamma-substituent from alpha amino acid, C-C bond cleavage
-
hydrolysis
Pseudomonas putida UW4
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Propanoate metabolism
-
SYSTEMATIC NAME
IUBMB Comments
1-aminocyclopropane-1-carboxylate aminohydrolase (isomerizing)
A pyridoxal 5'-phosphate enzyme. Its introduction has been used to make fruit ripening dependent on externally added ethylene, as it removes the substrate for endogenous ethylene formation.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
1-aminocyclopropane-1-carboxylate deaminase
-
-
1-aminocyclopropane-1-carboxylate deaminase
Pseudomonas putida UW4, Pseudomonas putida UW4 AcdS+
-
-
-
1-aminocyclopropane-1-carboxylate endolyase (deaminating)
-
-
-
-
1-aminocyclopropane-1-carboxylic acid deaminase
-
-
-
-
1-aminocyclopropane-1-carboxylic acid deaminase
-
-
1-aminocyclopropane-1-carboxylic acid deaminase
Agrobacterium tumefaciens D3, Agrobacterium tumefaciens YH-2
-
-
-
1-aminocyclopropane-1-carboxylic acid deaminase
E0Y9H8
-
1-aminocyclopropane-1-carboxylic acid deaminase
Azospirillum lipoferum AZm5
E0Y9H8
-
-
1-aminocyclopropane-1-carboxylic acid deaminase
-
-
1-aminocyclopropane-1-carboxylic acid deaminase
Pseudomonas putida UW4
-
-
-
1-aminocyclopropane-1-carboxylic acid-deaminase
-
-
ACC deaminase
-
-
-
-
ACC deaminase
Agrobacterium tumefaciens D3, Agrobacterium tumefaciens YH-2
-
-
-
ACC deaminase
-
-
ACC deaminase
E0Y9H8
-
ACC deaminase
Azospirillum lipoferum AZm5
E0Y9H8
-
-
ACC deaminase
B8R7R9
-
ACC deaminase
Burkholderia caledonica LMG 19076
B8R7R9
-
-
ACC deaminase
B8R7T5
-
ACC deaminase
Burkholderia caribensis MWAP64
B8R7T5
-
-
ACC deaminase
-
-
ACC deaminase
Burkholderia caryophylli LMG 2155
-
-
-
ACC deaminase
B4EJA6
-
ACC deaminase
B8R7S1
-
ACC deaminase
B8R7S1
-
-
ACC deaminase
B8R7T6
-
ACC deaminase
Burkholderia fungorum LMG 16225
B8R7T6
-
-
ACC deaminase
B8R7S2
-
ACC deaminase
Burkholderia graminis C4D1
B8R7S2
-
-
ACC deaminase
B8R7S3
-
ACC deaminase
Burkholderia phenoliruptrix LMG 22037
B8R7S3
-
-
ACC deaminase
B2JYI5
-
ACC deaminase
B2JYI5
-
-
ACC deaminase
B2TBV3
-
ACC deaminase
B8R7S5
-
ACC deaminase
B8R7T9
-
ACC deaminase
Burkholderia stabilis LMG 14294
B8R7T9
-
-
ACC deaminase
B8R7S7
-
ACC deaminase
Burkholderia terricola LMG 20594
B8R7S7
-
-
ACC deaminase
-
-
ACC deaminase
-
-
-
ACC deaminase
B8R7S8
-
ACC deaminase
B8R7S9
-
ACC deaminase
B8R7T2
-
ACC deaminase
-
-
ACC deaminase
-
-
ACC deaminase
Enterobacter cancerogenus MSA2
-
-
-
ACC deaminase
-
-
ACC deaminase
Enterobacter cloacae MSA1
-
-
-
ACC deaminase
-
-
-
ACC deaminase
B9W0P4
-
ACC deaminase
Methylobacterium radiotolerans COLR1
B9W0P4
-
-
ACC deaminase
-
-
ACC deaminase
Methylobacterium sp. WP1
-
-
-
ACC deaminase
G5AFQ7
-
ACC deaminase
-
-
ACC deaminase
-
-
ACC deaminase
C3VP48
-
ACC deaminase
Pseudomonas entomophila PS-PJH
C3VP48
-
-
ACC deaminase
Pseudomonas fluorescens Pf1
-
-
-
ACC deaminase
Pseudomonas putida UW4, Pseudomonas putida UW4 AcdS+
-
-
-
ACC deaminase
-
-
ACC deaminase
-
;
-
ACC deaminase
-
-
ACC deaminase
-
-
ACC deaminase
D3U2Q8
-
ACC deaminase
Trichoderma asperellum T203
D3U2Q8
-
-
ACC-deaminase
-
-
ACC-deaminase
-
-
ACC-deaminase
Enterobacter cancerogenus MSA2
-
-
-
ACC-deaminase
-
-
ACC-deaminase
Enterobacter cloacae MSA1
-
-
-
ACC-deaminase
-
-
ACC-deaminase
Enterobacter gergoviae J107
-
-
-
ACC-deaminase
Pseudomonas fluorescens AM3, Pseudomonas fluorescens J108
-
-
-
ACC-deaminase
-
-
ACC-deaminase
-
-
ACCD
Methylobacterium radiotolerans COLR1
B9W0P4
-
-
ACCD
Methylobacterium sp. WP1
-
-
-
ACCD
G5AFQ7
-
ACCD
Pseudomonas fluorescens Pf1
-
-
-
ACCD
-
-
-
ACCD
Trichoderma asperellum T203
D3U2Q8
-
-
AcdS
Q1G755
-
-
ACPC deaminase
-
-
-
-
deaminase, 1-aminocyclopropane-1-carboxylate
-
-
-
-
EC 4.1.99.4
-
-
formerly
-
EC 4.1.99.4
-
formerly
EC 4.1.99.4
Pseudomonas putida UW4
-
formerly
-
additional information
-
formerly EC 4.1.99.4
additional information
Enterobacter cancerogenus MSA2
-
formerly EC 4.1.99.4
-
additional information
-
formerly EC 4.1.99.4
additional information
Enterobacter cloacae MSA1
-
formerly EC 4.1.99.4
-
CAS REGISTRY NUMBER
COMMENTARY
69553-48-6
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
an avirulent strain, gene acdS
-
-
Manually annotated by BRENDA team
Agrobacterium tumefaciens D3
an avirulent strain, gene acdS
-
-
Manually annotated by BRENDA team
Agrobacterium tumefaciens YH-2
-
-
-
Manually annotated by BRENDA team
strain 4B, gene acdS
SwissProt
Manually annotated by BRENDA team
strain 4B, gene acdS
SwissProt
Manually annotated by BRENDA team
Azospirillum lipoferum AZm5
-
UniProt
Manually annotated by BRENDA team
Burkholderia caledonica LMG 19076
-
UniProt
Manually annotated by BRENDA team
Burkholderia caribensis MWAP64
-
UniProt
Manually annotated by BRENDA team
Burkholderia caryophylli LMG 2155
-
-
-
Manually annotated by BRENDA team
Burkholderia fungorum LMG 16225
-
UniProt
Manually annotated by BRENDA team
Burkholderia graminis C4D1
-
UniProt
Manually annotated by BRENDA team
Burkholderia phenoliruptrix LMG 22037
-
UniProt
Manually annotated by BRENDA team
isolated from surface-sterilized onion roots, strain shows high enzyme activity and is able to establish rhizosphere and endophytic populations associated with various plants
-
-
Manually annotated by BRENDA team
Burkholderia stabilis LMG 14294
-
UniProt
Manually annotated by BRENDA team
Burkholderia terricola LMG 20594
-
UniProt
Manually annotated by BRENDA team
isolated from West Coast soil of Yellow Sea, Incheon, South Korea
-
-
Manually annotated by BRENDA team
strain J120
-
-
Manually annotated by BRENDA team
recovered from the rhizosphere of Jatropha sp., gene acdS
-
-
Manually annotated by BRENDA team
Enterobacter cancerogenus MSA2
recovered from the rhizosphere of Jatropha sp., gene acdS
-
-
Manually annotated by BRENDA team
expression in Lycopersicon esculentum
-
-
Manually annotated by BRENDA team
recovered from the rhizosphere of Jatropha sp., gene acdS
-
-
Manually annotated by BRENDA team
strain CAL2 and strain UW4
-
-
Manually annotated by BRENDA team
strain CAL3
-
-
Manually annotated by BRENDA team
strain UW4
-
-
Manually annotated by BRENDA team
Enterobacter cloacae CAL3
strain CAL3
-
-
Manually annotated by BRENDA team
Enterobacter cloacae MSA1
recovered from the rhizosphere of Jatropha sp., gene acdS
-
-
Manually annotated by BRENDA team
Enterobacter cloacae UW4
strain UW4
-
-
Manually annotated by BRENDA team
Enterobacter gergoviae J107
-
-
-
Manually annotated by BRENDA team
inoculation of Brassica campestris
-
-
Manually annotated by BRENDA team
strain CBMB20, DSM 18207
-
-
Manually annotated by BRENDA team
strain CBMB20, DSM 18207, isolated from stem tissues of Oryza sativa
-
-
Manually annotated by BRENDA team
strain CBMB20, DSM 18207
-
-
Manually annotated by BRENDA team
strain CBMB20, DSM 18207, isolated from stem tissues of Oryza sativa
-
-
Manually annotated by BRENDA team
Methylobacterium radiotolerans COLR1
-
B9W0P4
UniProt
Manually annotated by BRENDA team
Methylobacterium sp. WP1
-
-
-
Manually annotated by BRENDA team
no activity in Agrobacterium tumefaciens
-
-
-
Manually annotated by BRENDA team
no activity in Azospirillum brasilense
-
-
-
Manually annotated by BRENDA team
no activity in Burkholderia ambifaria
-
-
-
Manually annotated by BRENDA team
no activity in Burkholderia tropica
-
-
-
Manually annotated by BRENDA team
no activity in Methylobacterium sp.
strain CBMB120
-
-
Manually annotated by BRENDA team
no activity in Methylobacterium sp. CBMB120
strain CBMB120
-
-
Manually annotated by BRENDA team
inoculation of Pisum sativum
-
-
Manually annotated by BRENDA team
several strains, e.g. the phytopathogenic strain 520-1 or strain Am3, i.e. T8-1
-
-
Manually annotated by BRENDA team
Pseudomonas entomophila PS-PJH
-
UniProt
Manually annotated by BRENDA team
Pseudomonas fluorescens AM3
strain AM3
-
-
Manually annotated by BRENDA team
Pseudomonas fluorescens J108
-
-
-
Manually annotated by BRENDA team
Pseudomonas fluorescens Pf1
-
-
-
Manually annotated by BRENDA team
inoculation of Pisum sativum
-
-
Manually annotated by BRENDA team
biotype A
-
-
Manually annotated by BRENDA team
biotype A, A7
-
-
Manually annotated by BRENDA team
expression in Brassica napus
-
-
Manually annotated by BRENDA team
GR12-2; strain UW3, strain UW1
-
-
Manually annotated by BRENDA team
strain N21
-
-
Manually annotated by BRENDA team
strain UW4 AcdS+
-
-
Manually annotated by BRENDA team
strains Bm3, Am2
-
-
Manually annotated by BRENDA team
strains GR12-2, ATCC 17399
-
-
Manually annotated by BRENDA team
Pseudomonas putida GR12-2
GR12-2
-
-
Manually annotated by BRENDA team
Pseudomonas putida UW4
-
-
-
Manually annotated by BRENDA team
Pseudomonas putida UW4
strain UW4
-
-
Manually annotated by BRENDA team
Pseudomonas putida UW4 AcdS+
strain UW4 AcdS+
-
-
Manually annotated by BRENDA team
strain 3F2
-
-
Manually annotated by BRENDA team
strain ACP
Uniprot
Manually annotated by BRENDA team
strain ACP
-
-
Manually annotated by BRENDA team
Pseudomonas sp. 3F2
strain 3F2
-
-
Manually annotated by BRENDA team
strain ACP
Uniprot
Manually annotated by BRENDA team
strain ACP
-
-
Manually annotated by BRENDA team
Rhizobium spp.
-
-
-
Manually annotated by BRENDA team
Rhizobium spp.
enzyme can be induced by the substrate
-
-
Manually annotated by BRENDA team
strain Fp2, inoculation of Pisum sativum
-
-
Manually annotated by BRENDA team
strain Fp2, inoculation of Pisum sativum
-
-
Manually annotated by BRENDA team
tomato, isoenzyme LeACS2
-
-
Manually annotated by BRENDA team
Trichoderma asperellum T203
-
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
malfunction
D3U2Q8, -
RNAi silencing of the ACCD gene in Trichoderma asperellum shows decreased ability of the mutants to promote root elongation of Brassica napus seedlings
malfunction
-
the acdS and lrpL double mutant strain Agrobacterium tumefaciens D3-1 has lost the ability to promote plant root elongation
malfunction
Agrobacterium tumefaciens D3
-
the acdS and lrpL double mutant strain Agrobacterium tumefaciens D3-1 has lost the ability to promote plant root elongation
-
physiological function
-
inoculation of wheat seedlings with rhizobacteria containing ACC-deaminase increases the plant height significantly under salt-stressed conditions, significantly affects the 100-grain weight of wheat at high and low salinity levels, increases the grain yield, and significantly improves the K+/Na+ at all salinity levels compared to control
physiological function
-
inoculation of Mesorhizobium ciceri with the bacterial isolate exhibiting ACC-deaminase activity results in an increase in root weight, shoot weight, number of pods and grain yield
physiological function
D3U2Q8, -
ACCD is involved in the induction of plant growth promotion by Trichoderma asperellum
physiological function
-
the presence of active ACC deaminase in Agrobacterium tumefaciens reduces ethylene levels produced by plant tissues during the process of infection and cocultivation, and significantly increases the transformation efficiency of three commercial Brassica napus cultivars (Westar, Hyola 401 and 4414RR). ACC deaminase has no effect on the growth of Agrobacterium tumefaciens during the cocultivation process
physiological function
-
the presence of active Pseudomonas putida UW4 ACC deaminase in Agrobacterium tumefaciens reduces ethylene levels produced by plant tissues during the process of infection and cocultivation, and significantly increases the transformation efficiency of three commercial Brassica napus cultivars (Westar, Hyola 401 and 4414RR). ACC deaminase has no effect on the growth of Agrobacterium tumefaciens during the cocultivation process
physiological function
C3VP48, -
ACC deaminase cleaves the ethylene precursor 1-aminocyclopropane-1-carboxylate into 2-oxobutanoate and ammonia. The decreased level of ethylene allows the plant to be more resistant to a wide environmental stress including plant pathogens
physiological function
-
ACC deaminase producing bacterial inoculants enhance shoot and root length of rice
physiological function
B9W0P4
ACC deaminase producing bacterial inoculants enhance shoot and root length of rice
physiological function
-
ACC deaminase producing bacterial inoculants enhance shoot and root length of rice
physiological function
-
ACC deaminase breaks down ACC, the direct precursor of ethylene biosynthesis in all higher plants, into ammonia and 2-oxobutyrate and, as a result, reduces stress ethylene levels in plants caused by a wide range of biotic and abiotic stresses. ACC deaminase from strain D3 can inhibit crown gall development induced by Agrobacterium tumefaciens strain C58 and can partially protect plants from this disease. Under gnotobiotic conditions, wild-type strain D3 is able to promote plant root elongation
physiological function
Agrobacterium tumefaciens D3
-
ACC deaminase breaks down ACC, the direct precursor of ethylene biosynthesis in all higher plants, into ammonia and 2-oxobutyrate and, as a result, reduces stress ethylene levels in plants caused by a wide range of biotic and abiotic stresses. ACC deaminase from strain D3 can inhibit crown gall development induced by Agrobacterium tumefaciens strain C58 and can partially protect plants from this disease. Under gnotobiotic conditions, wild-type strain D3 is able to promote plant root elongation
-
physiological function
Agrobacterium tumefaciens YH-2
-
the presence of active ACC deaminase in Agrobacterium tumefaciens reduces ethylene levels produced by plant tissues during the process of infection and cocultivation, and significantly increases the transformation efficiency of three commercial Brassica napus cultivars (Westar, Hyola 401 and 4414RR). ACC deaminase has no effect on the growth of Agrobacterium tumefaciens during the cocultivation process
-
physiological function
Enterobacter gergoviae J107
-
inoculation of Mesorhizobium ciceri with the bacterial isolate exhibiting ACC-deaminase activity results in an increase in root weight, shoot weight, number of pods and grain yield
-
physiological function
Methylobacterium oryzae CBMB20, Methylobacterium radiotolerans COLR1, Methylobacterium sp. WP1
-
ACC deaminase producing bacterial inoculants enhance shoot and root length of rice
-
physiological function
Pseudomonas entomophila PS-PJH
-
ACC deaminase cleaves the ethylene precursor 1-aminocyclopropane-1-carboxylate into 2-oxobutanoate and ammonia. The decreased level of ethylene allows the plant to be more resistant to a wide environmental stress including plant pathogens
-
physiological function
Pseudomonas fluorescens J108
-
inoculation of Mesorhizobium ciceri with the bacterial isolate exhibiting ACC-deaminase activity results in an increase in root weight, shoot weight, number of pods and grain yield
-
physiological function
Pseudomonas fluorescens Pf1
-
ACC deaminase producing bacterial inoculants enhance shoot and root length of rice
-
physiological function
Pseudomonas putida UW4
-
the presence of active Pseudomonas putida UW4 ACC deaminase in Agrobacterium tumefaciens reduces ethylene levels produced by plant tissues during the process of infection and cocultivation, and significantly increases the transformation efficiency of three commercial Brassica napus cultivars (Westar, Hyola 401 and 4414RR). ACC deaminase has no effect on the growth of Agrobacterium tumefaciens during the cocultivation process
-
physiological function
Trichoderma asperellum T203
-
ACCD is involved in the induction of plant growth promotion by Trichoderma asperellum
-
malfunction
Trichoderma asperellum T203
-
RNAi silencing of the ACCD gene in Trichoderma asperellum shows decreased ability of the mutants to promote root elongation of Brassica napus seedlings
-
additional information
G5AFQ7, -
phylogenetic analysis, structure modeling, and rigid ligand docking of ACC deaminase, coenzyme-substrate docking, overview
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
-
ir
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
-
ir
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
Rhizobium spp.
-
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
Q93AG0
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
B8R7S3
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
B8R7T6
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
B8R7S2
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
B8R7S7
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
B2TBV3
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
B8R7T9
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
B4EJA6
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
B8R7S1
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
B8R7T7
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
D3U2Q8, -
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
B8R7R9
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
C3VP48, -
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
E0Y9H8
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
B8R7S8
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
B9W0P4
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
B8R7T2
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
B8R7S5
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
B2JYI5
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
B8R7S9
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
B8R7T5
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
Q93AG0
enzyme enhances nodulation of Pisum sativum, likely by modulating ethylene levels in the plant roots during the early stages of nodule development
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
-
the enzyme is thought to be intimately involved in the mechanism that the bacterium uses to promote root elongation in developing Canola seedlings. The enzyme is inducible by 1-aminocyclopropane-1-carboxylate and contains a basal level of constitutively expressed enzyme activity
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
-
effective induction by 1-aminocyclopropane-1-carboxylate and 2-aminobutanoate
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
-
the enzyme catalyzes the hydrolytic cleavage of 1-aminocyclopropane-1-carboxylate, the immediate precursor of ethylene, and is therefore an inhibitor of ethylene biosynthesis
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
-
the plant growth-promoting rhizobacteria stimulate plant growth through the activity of 1-aminocyclopropane-1-carboxylate deaminase
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
-
a precursor for ethylene production in plants
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
-
the pyridoxal 5'-phosphate-dependent enzyme cleaves the cyclopropane ring of ACC, to give 2-oxobutyric acid and ammonia as products. The pKa of the conserved active site residue, Tyr294, is lowered by a hydrogen bonding interaction with a second conserved residue, Tyr268. This allows Tyr294 to deprotonate the incoming amino group of ACC to initiate the aldimine exchange reaction between ACC and the pyridoxal 5'-phosphate coenzyme and also likely helps to activate Tyr294 for a role as a nucleophile to attack and cleave the cyclopropane ring of the substrate. The Calpha-Cbeta bond cleavage step in the chemical mechanism is at least partially rate-limiting under kcat/Km conditions and is likely preceded in the mechanism by a partially rate-limiting step involving the conversion of a stable gem-diamine intermediate into a reactive external aldimine intermediate that is poised for cyclopropane ring cleavage
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
Pseudomonas fluorescens J108
-
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
B8R7S1
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
Enterobacter cancerogenus MSA2
-
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
Enterobacter cloacae MSA1
-
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
Enterobacter gergoviae J107
-
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
Azospirillum lipoferum AZm5
E0Y9H8
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
Pseudomonas fluorescens Pf1
-
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
Pseudomonas putida GR12-2
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
Pseudomonas putida GR12-2
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
Pseudomonas putida GR12-2
-
the enzyme is thought to be intimately involved in the mechanism that the bacterium uses to promote root elongation in developing Canola seedlings. The enzyme is inducible by 1-aminocyclopropane-1-carboxylate and contains a basal level of constitutively expressed enzyme activity
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
Burkholderia stabilis LMG 14294
B8R7T9
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
Agrobacterium tumefaciens YH-2
-
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
Pseudomonas putida UW4
-
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
Pseudomonas entomophila PS-PJH
C3VP48
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
Burkholderia phenoliruptrix LMG 22037
B8R7S3
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
Methylobacterium radiotolerans COLR1
B9W0P4
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
Burkholderia terricola LMG 20594
B8R7S7
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
B2JYI5
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
Burkholderia caryophylli LMG 2155
-
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
Burkholderia fungorum LMG 16225
B8R7T6
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
Trichoderma asperellum T203
D3U2Q8
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
Pseudomonas sp. 3F2
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
Pseudomonas sp. 3F2
-
the enzyme catalyzes the hydrolytic cleavage of 1-aminocyclopropane-1-carboxylate, the immediate precursor of ethylene, and is therefore an inhibitor of ethylene biosynthesis
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
Methylobacterium sp. WP1
-
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
-
-, the pyridoxal 5'-phosphate-dependent enzyme cleaves the cyclopropane ring of ACC, to give 2-oxobutyric acid and ammonia as products. The pKa of the conserved active site residue, Tyr294, is lowered by a hydrogen bonding interaction with a second conserved residue, Tyr268. This allows Tyr294 to deprotonate the incoming amino group of ACC to initiate the aldimine exchange reaction between ACC and the pyridoxal 5'-phosphate coenzyme and also likely helps to activate Tyr294 for a role as a nucleophile to attack and cleave the cyclopropane ring of the substrate. The Calpha-Cbeta bond cleavage step in the chemical mechanism is at least partially rate-limiting under kcat/Km conditions and is likely preceded in the mechanism by a partially rate-limiting step involving the conversion of a stable gem-diamine intermediate into a reactive external aldimine intermediate that is poised for cyclopropane ring cleavage
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
Burkholderia caribensis MWAP64
B8R7T5
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
Burkholderia graminis C4D1
B8R7S2
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
Burkholderia caledonica LMG 19076
B8R7R9
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutyrate + NH3
show the reaction diagram
-
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutyrate + NH3
show the reaction diagram
-
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutyrate + NH3
show the reaction diagram
-
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutyrate + NH3
show the reaction diagram
-
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutyrate + NH3
show the reaction diagram
-
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutyrate + NH3
show the reaction diagram
Q1G755
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutyrate + NH3
show the reaction diagram
-
ACC deaminase activity is an important trait of plant growth-promoting rhizobacteria, PGPR, that stimulates root growth in infected plants, e.g. in soil-grown tomato Lycopersicon esculentum cv. Ailsa Craig. All the Pseudomonas brassicacearum strains studied cause pith necrosis when stems or fruits are inoculated with a bacterial suspension, as does the causal organism of this disease Pseudomonas corrugata strain 176, but the non-pathogenic strain Pseudomonas sp. Dp2 does not
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutyrate + NH3
show the reaction diagram
Q1G755
deamination of the ethylene precursor in plants, regulation of enzyme activity involving the lrp-like leucine-responsive regulatory gene, called acdR, overview
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutyrate + NH3
show the reaction diagram
-
the enzyme converts the precursor of ethylene production to 2-oxobutanoate and abolishes the response to ethylene in etiolated pea seedlings, which occurs after application of 1-aminocyclopropane-1-carboxylate in absence of the ACC deaminase, overview
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutyrate + NH3
show the reaction diagram
-
the substrate is the direct precursor of ethylene, which is a key component in regulation of root elongation in plants, e.g. Brassica campestris, inoculation of ACC deaminase-containing Methylobacterium oryzae sequesters 1-aminocyclopropane-1-carboxylate exuded from roots. The inhibitory actions of exogenous additions of auxins cannot be ameliorated by bacterial inoculation that reduces ethylene concentration in canola seedlings, overview
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutyrate + NH3
show the reaction diagram
Pseudomonas fluorescens AM3
-
-, the enzyme converts the precursor of ethylene production to 2-oxobutanoate and abolishes the response to ethylene in etiolated pea seedlings, which occurs after application of 1-aminocyclopropane-1-carboxylate in absence of the ACC deaminase, overview
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutyrate + NH3
show the reaction diagram
-
-, the substrate is the direct precursor of ethylene, which is a key component in regulation of root elongation in plants, e.g. Brassica campestris, inoculation of ACC deaminase-containing Methylobacterium oryzae sequesters 1-aminocyclopropane-1-carboxylate exuded from roots. The inhibitory actions of exogenous additions of auxins cannot be ameliorated by bacterial inoculation that reduces ethylene concentration in canola seedlings, overview
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutyrate + NH3
show the reaction diagram
-
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutyrate + NH3
show the reaction diagram
Q1G755
-, deamination of the ethylene precursor in plants, regulation of enzyme activity involving the lrp-like leucine-responsive regulatory gene, called acdR, overview
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutyrate + NH3
show the reaction diagram
-
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
alpha-ketobutyrate + NH3
show the reaction diagram
-
ACC deaminase-producing bacteria play an important role in the alleviation of different types of stress in plants, including the effect of heavy metals
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
alpha-ketobutyrate + NH3
show the reaction diagram
-
ACC is the immediate precursor of the plant hormone ethylene, an important mediator of plant growth and development
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
alpha-ketobutyrate + NH3
show the reaction diagram
-
activity of the mutants, immediate precursor of ethylene in plants
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
alpha-ketobutyrate + NH3
show the reaction diagram
-
lowering the phytohormone ethylene levels in plants
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
alpha-ketobutyrate + NH3
show the reaction diagram
Pseudomonas putida UW4
-
ACC is the immediate precursor of the plant hormone ethylene, an important mediator of plant growth and development
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
alpha-ketobutyrate + NH3
show the reaction diagram
Pseudomonas putida UW4
-
activity of the mutants, immediate precursor of ethylene in plants
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
alpha-ketobutyrate + NH3
show the reaction diagram
Pseudomonas putida UW4 AcdS+
-
lowering the phytohormone ethylene levels in plants
-
-
?
2-vinyl-1-aminocyclopropane-1-carboxylate + H2O
2-keto-5-hexenoate + NH3
show the reaction diagram
-
-
-
?
coronamic acid + H2O
2-oxobutanoate + NH3
show the reaction diagram
-
D-coronamic acid
-
-
?
coronamic acid + H2O
2-oxobutanoate + NH3
show the reaction diagram
-
DL-coronamic acid
-
-
-
coronamic acid + H2O
2-oxobutanoate + NH3
show the reaction diagram
-
l-coronamic acid and DL-allocoronamic acid are inactive as substrates
-
-
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
show the reaction diagram
Pseudomonas putida, Pseudomonas putida UW4
-
-
-
-
?
D-Ser + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
the enzyme improves the growth of canola plants after infection with Pseudomonas putida strain UW4 conferring salt tolerance to the plants, overview
-
-
-
additional information
?
-
-
ACC deaminase stimulates root growth of plants in a coordinated fashion. Bacterial isolates with ACC deaminase activity reduce seed germination and root length in Canola cultivars under stress by treatment with the bacterial suspension.
-
-
-
additional information
?
-
-
ACC deaminase-producing bacteria are able to inhibit the effect of ethylene on the auxin transduction pathway
-
-
-
additional information
?
-
-
Canola plants inoculating with the HS-2 strain produce an increase in plant biomass as well as in nickeln uptake by shoots and roots.
-
-
-
additional information
?
-
-
leucine-responsive regulatory protein is a potential regulator of ACC deaminase transcription
-
-
-
additional information
?
-
-
mycorrhizal colonization, as well as arbuscule abundance, is significantly stimulated by Pseudomonas putida UW4 AcdS+, but not by the AcdS mutant, on cucumber.
-
-
-
additional information
?
-
-
Site-directed mutagenesis shows that altering two amino acid residues at the same positions within the predicted active site serves to change the enzyme from D-cysteine desulfhydrase to deaminase from Pseudomonas putida UW4 the enzyme is converted into D-cysteine desulfhydrase.
-
-
-
additional information
?
-
-
The presence of the ACC deaminase gene in the transgenic plant as well as the inoculation with Pseudomonas putida strain HS-2 improves the percentage emergence of the plants in the presence of the high nickel concentration (2.9 mg Ni/g dry soil) of this soil.
-
-
-
additional information
?
-
Pseudomonas putida UW4
-
the enzyme improves the growth of canola plants after infection with Pseudomonas putida strain UW4 conferring salt tolerance to the plants, overview
-
-
-
additional information
?
-
Pseudomonas putida UW4
-
leucine-responsive regulatory protein is a potential regulator of ACC deaminase transcription
-
-
-
additional information
?
-
Pseudomonas putida UW4
-
Site-directed mutagenesis shows that altering two amino acid residues at the same positions within the predicted active site serves to change the enzyme from D-cysteine desulfhydrase to deaminase from Pseudomonas putida UW4 the enzyme is converted into D-cysteine desulfhydrase.
-
-
-
additional information
?
-
Pseudomonas putida UW4 AcdS+
-
mycorrhizal colonization, as well as arbuscule abundance, is significantly stimulated by Pseudomonas putida UW4 AcdS+, but not by the AcdS mutant, on cucumber.
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
Q93AG0
enzyme enhances nodulation of Pisum sativum, likely by modulating ethylene levels in the plant roots during the early stages of nodule development
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
-
the enzyme is thought to be intimately involved in the mechanism that the bacterium uses to promote root elongation in developing Canola seedlings. The enzyme is inducible by 1-aminocyclopropane-1-carboxylate and contains a basal level of constitutively expressed enzyme activity
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
-
effective induction by 1-aminocyclopropane-1-carboxylate and 2-aminobutanoate
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
-
the enzyme catalyzes the hydrolytic cleavage of 1-aminocyclopropane-1-carboxylate, the immediate precursor of ethylene, and is therefore an inhibitor of ethylene biosynthesis
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
-
the plant growth-promoting rhizobacteria stimulate plant growth through the activity of 1-aminocyclopropane-1-carboxylate deaminase
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
-
a precursor for ethylene production in plants
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutyrate + NH3
show the reaction diagram
-
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutyrate + NH3
show the reaction diagram
-
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutyrate + NH3
show the reaction diagram
-
ACC deaminase activity is an important trait of plant growth-promoting rhizobacteria, PGPR, that stimulates root growth in infected plants, e.g. in soil-grown tomato Lycopersicon esculentum cv. Ailsa Craig. All the Pseudomonas brassicacearum strains studied cause pith necrosis when stems or fruits are inoculated with a bacterial suspension, as does the causal organism of this disease Pseudomonas corrugata strain 176, but the non-pathogenic strain Pseudomonas sp. Dp2 does not
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutyrate + NH3
show the reaction diagram
Q1G755
deamination of the ethylene precursor in plants, regulation of enzyme activity involving the lrp-like leucine-responsive regulatory gene, called acdR, overview
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutyrate + NH3
show the reaction diagram
-
the enzyme converts the precursor of ethylene production to 2-oxobutanoate and abolishes the response to ethylene in etiolated pea seedlings, which occurs after application of 1-aminocyclopropane-1-carboxylate in absence of the ACC deaminase, overview
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutyrate + NH3
show the reaction diagram
-
the substrate is the direct precursor of ethylene, which is a key component in regulation of root elongation in plants, e.g. Brassica campestris, inoculation of ACC deaminase-containing Methylobacterium oryzae sequesters 1-aminocyclopropane-1-carboxylate exuded from roots. The inhibitory actions of exogenous additions of auxins cannot be ameliorated by bacterial inoculation that reduces ethylene concentration in canola seedlings, overview
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
alpha-ketobutyrate + NH3
show the reaction diagram
-
ACC deaminase-producing bacteria play an important role in the alleviation of different types of stress in plants, including the effect of heavy metals
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
alpha-ketobutyrate + NH3
show the reaction diagram
-
ACC is the immediate precursor of the plant hormone ethylene, an important mediator of plant growth and development
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
alpha-ketobutyrate + NH3
show the reaction diagram
-
activity of the mutants, immediate precursor of ethylene in plants
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
alpha-ketobutyrate + NH3
show the reaction diagram
-
lowering the phytohormone ethylene levels in plants
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutyrate + NH3
show the reaction diagram
Pseudomonas fluorescens AM3
-
the enzyme converts the precursor of ethylene production to 2-oxobutanoate and abolishes the response to ethylene in etiolated pea seedlings, which occurs after application of 1-aminocyclopropane-1-carboxylate in absence of the ACC deaminase, overview
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
Enterobacter cancerogenus MSA2
-
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutyrate + NH3
show the reaction diagram
-
the substrate is the direct precursor of ethylene, which is a key component in regulation of root elongation in plants, e.g. Brassica campestris, inoculation of ACC deaminase-containing Methylobacterium oryzae sequesters 1-aminocyclopropane-1-carboxylate exuded from roots. The inhibitory actions of exogenous additions of auxins cannot be ameliorated by bacterial inoculation that reduces ethylene concentration in canola seedlings, overview
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutyrate + NH3
show the reaction diagram
-
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
Enterobacter cloacae MSA1
-
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
Pseudomonas putida GR12-2
-
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
Pseudomonas putida GR12-2
-
the enzyme is thought to be intimately involved in the mechanism that the bacterium uses to promote root elongation in developing Canola seedlings. The enzyme is inducible by 1-aminocyclopropane-1-carboxylate and contains a basal level of constitutively expressed enzyme activity
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
alpha-ketobutyrate + NH3
show the reaction diagram
Pseudomonas putida UW4
-
ACC is the immediate precursor of the plant hormone ethylene, an important mediator of plant growth and development
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
alpha-ketobutyrate + NH3
show the reaction diagram
Pseudomonas putida UW4
-
activity of the mutants, immediate precursor of ethylene in plants
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutyrate + NH3
show the reaction diagram
Q1G755
deamination of the ethylene precursor in plants, regulation of enzyme activity involving the lrp-like leucine-responsive regulatory gene, called acdR, overview
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
Pseudomonas sp. 3F2
-
the enzyme catalyzes the hydrolytic cleavage of 1-aminocyclopropane-1-carboxylate, the immediate precursor of ethylene, and is therefore an inhibitor of ethylene biosynthesis
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
alpha-ketobutyrate + NH3
show the reaction diagram
Pseudomonas putida UW4 AcdS+
-
lowering the phytohormone ethylene levels in plants
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
show the reaction diagram
-
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutyrate + NH3
show the reaction diagram
-
-
-
-
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
show the reaction diagram
Pseudomonas putida, Pseudomonas putida UW4
-
-
-
-
?
additional information
?
-
-
the enzyme improves the growth of canola plants after infection with Pseudomonas putida strain UW4 conferring salt tolerance to the plants, overview
-
-
-
additional information
?
-
-
ACC deaminase stimulates root growth of plants in a coordinated fashion. Bacterial isolates with ACC deaminase activity reduce seed germination and root length in Canola cultivars under stress by treatment with the bacterial suspension.
-
-
-
additional information
?
-
-
ACC deaminase-producing bacteria are able to inhibit the effect of ethylene on the auxin transduction pathway
-
-
-
additional information
?
-
-
Canola plants inoculating with the HS-2 strain produce an increase in plant biomass as well as in nickeln uptake by shoots and roots.
-
-
-
additional information
?
-
-
leucine-responsive regulatory protein is a potential regulator of ACC deaminase transcription
-
-
-
additional information
?
-
-
mycorrhizal colonization, as well as arbuscule abundance, is significantly stimulated by Pseudomonas putida UW4 AcdS+, but not by the AcdS mutant, on cucumber.
-
-
-
additional information
?
-
-
Site-directed mutagenesis shows that altering two amino acid residues at the same positions within the predicted active site serves to change the enzyme from D-cysteine desulfhydrase to deaminase from Pseudomonas putida UW4 the enzyme is converted into D-cysteine desulfhydrase.
-
-
-
additional information
?
-
-
The presence of the ACC deaminase gene in the transgenic plant as well as the inoculation with Pseudomonas putida strain HS-2 improves the percentage emergence of the plants in the presence of the high nickel concentration (2.9 mg Ni/g dry soil) of this soil.
-
-
-
additional information
?
-
Pseudomonas putida UW4
-
the enzyme improves the growth of canola plants after infection with Pseudomonas putida strain UW4 conferring salt tolerance to the plants, overview
-
-
-
additional information
?
-
Pseudomonas putida UW4
-
leucine-responsive regulatory protein is a potential regulator of ACC deaminase transcription
-
-
-
additional information
?
-
Pseudomonas putida UW4
-
Site-directed mutagenesis shows that altering two amino acid residues at the same positions within the predicted active site serves to change the enzyme from D-cysteine desulfhydrase to deaminase from Pseudomonas putida UW4 the enzyme is converted into D-cysteine desulfhydrase.
-
-
-
additional information
?
-
Pseudomonas putida UW4 AcdS+
-
mycorrhizal colonization, as well as arbuscule abundance, is significantly stimulated by Pseudomonas putida UW4 AcdS+, but not by the AcdS mutant, on cucumber.
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
one mol of subunit contains one mol of pyridoxal 5'-phosphate; pyridoxal 5'-phosphate dependent enzyme
pyridoxal 5'-phosphate
-
2.8 mol of tightly bound pyridoxal 5'-phosphate per mol of enzyme; pyridoxal 5'-phosphate dependent enzyme
pyridoxal 5'-phosphate
-
pyridoxal 5'-phosphate dependent enzyme
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
ACC deaminase binds one pyridoxal phosphate (PLP) molecule at each subunit via a conserved lysine residue.
pyridoxal 5'-phosphate
B8R7R9
-
pyridoxal 5'-phosphate
B8R7T5
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
B4EJA6
-
pyridoxal 5'-phosphate
B8R7S1
-
pyridoxal 5'-phosphate
B8R7T6
-
pyridoxal 5'-phosphate
B8R7S2
-
pyridoxal 5'-phosphate
B8R7S3
-
pyridoxal 5'-phosphate
B2JYI5
-
pyridoxal 5'-phosphate
B2TBV3
-
pyridoxal 5'-phosphate
B8R7S5
-
pyridoxal 5'-phosphate
B8R7T9
-
pyridoxal 5'-phosphate
B8R7S7
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
B8R7S8
-
pyridoxal 5'-phosphate
B8R7S9
-
pyridoxal 5'-phosphate
B8R7T2
-
pyridoxal 5'-phosphate
-
dependent on
pyridoxal 5'-phosphate
-
tightly bound to the enzyme in the amount of approximately one molecule per subunit
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
K2HPO4
-
results in highest activity
Ni2+
-
examined strains are tolerant nickel concentrations of up to 13.2 mM in the culture medium
MgSO4
-
results in highest activity
additional information
-
The bacteria are able to utilize 1-aminocyclopropane-1-carboxylate as the sole N-source, at a concentration of 5 g/l of NaCl
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1-amino-2-methylenecyclopopropane-1-carboxylic acid
-
irreversible
1-aminocyclopropanephosphonate
-
-
5,5'-dithiobis(2-nitrobenzoic acid)
-
-
aminooxyacetic acid
-
0.005-1 mM, enzymatic activity is progressively inhibited as the aminooxyacetic acid concentration is increased
beta-chloro-Ala
-
mechanism-based inhibition
beta-chloro-Ala
-
-
beta-fluoro-D-Ala
-
-
cyclohexylhydrazine
-
-
D-Ser
-
slow inactivation
L-2-aminobutanoate
-
-
L-2-aminobutanoate
-
-
L-Ser
-
competitive
L-serine
-
5 mM L-serine results in at least a 50% decrease of measurable ACD activity
Monoiodoacetamide
-
-
NH2CONH-NH2
-
-
O-acetyl-D-Ser
-
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
additional information
-
inoculation with Brevibacterium iodinum strain RS16, Bacillus licheniformis strain RS656, and Zhihengliuela alba strain RS111 for two h exposure of 100, 150 and 200 mM NaCl stress on 8 day old red pepper seedlings show a significant increase in ethylene productions, phenotypes, overview
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1.5
-
1-aminocyclopropane-1-carboxylate
-
-
2.08
-
1-aminocyclopropane-1-carboxylate
-
pH 7.5, 30C
2.6
-
1-aminocyclopropane-1-carboxylate
-
-
3.4
-
1-aminocyclopropane-1-carboxylate
-
pH 8.0, 22C
9.2
-
1-aminocyclopropane-1-carboxylate
-
-
12.5
-
1-aminocyclopropane-1-carboxylate
-
pH 7.5, 30C
4
-
2-vinyl-1-aminocyclopropane-1-carboxylate
-
-
0.34
-
D-Cysteine
-
double mutant Pseudomonas putida E295S+L322T
97
-
D-vinylglycine
-
-
additional information
-
additional information
-
steady-state kinetics and pH-dependence, overview
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
4.83
-
1-aminocyclopropane-1-carboxylate
-
37C, pH 8.5
146
-
1-aminocyclopropane-1-carboxylate
-
pH 8.0, 22C
5.17
-
2-vinyl-1-aminocyclopropane-1-carboxylate
-
37C, pH 8.5
654
-
D-Cysteine
-
double mutant Pseudomonas putida E295S+L322T
0.6
-
D-vinylglycine
-
37C, pH 8.5
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.00017
-
-
activity in strain 520-1
0.001594
-
-
D-cysteine desulfhydrase activity in wild-type enzyme
0.005
-
-
pH and temperature not specified in the publication
0.0054
-
-
pH and temperature not specified in the publication
0.0057
-
B9W0P4
pH and temperature not specified in the publication
0.0074
-
-
pH and temperature not specified in the publication
0.00819
-
-
ACC deaminase activity in mutant E295S
0.0183
-
-
strain FT-4
0.0317
-
-
strain HS-2
0.0356
-
-
D-cysteine desulfhydrase activity in mutant E295S
0.0483
-
-
strain FT-1
0.0578
-
-
strain FT-3
0.1475
-
-
D-cysteine desulfhydrase activity in double mutant E295S+L322T
0.36
-
-
expressed in delayed ripening tomatoes, 37C
2.812
-
-
ACC deaminase activity in wild-type enzyme
3.49
-
-
-
additional information
-
-
-
additional information
-
Q1G755
semi-quantitative expression analysis of gene acdS
additional information
-
-
enzyme activity in different strain of Pseudomonas brassicacearum, highest activity in strain 520-1, and root elongation assay, overview
additional information
-
-
quantitative determination of ethylene and 1-aminocyclopropane-1-carboxylate content in roots of Brassica campestris
additional information
-
-
2.092, ACC deaminase acitivity in strain 196 (micromol alpha-keto butyrate/mg/h); 2.726, ACC deaminase acitivity in strain 79 (micromol alpha-keto butyrate/mg/h); 3.508, ACC deaminase acitivity in strain 169 (micromol alpha-keto butyrate/mg/h)
additional information
-
-
2.305, ACC deaminase acitivity in strain 4 (micromol alpha-keto butyrate/mg/h); 2.409 , ACC deaminase acitivity in strain 11 (micromol alpha-keto butyrate/mg/h); 2.981, ACC deaminase acitivity in strain 159 (micromol alpha-keto butyrate/mg/h); 5.030, ACC deaminase acitivity in strain 108 (micromol alpha-keto butyrate/mg/h)
additional information
-
-
activity below detection, ACC deaminase activity in double mutant E295S/L322T
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.5
-
-
assay at for wild-type enzyme and mutants E295D and Y294F
8
-
-
assay at
8.8
-
-
assay at for mutant Y268F
additional information
-
-
steady-state kinetics and pH-dependence, overview
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.5
-
-
no activity below
7.5
9.5
-
pH 7.5: about 45% of maximal activity, pH 9.5: 20% of maximal activity
7.5
9.7
-
about 65% of maximal activity at pH 7.5 and at pH 9.7
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
-
-
assay at
37
-
-
assay at
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
15
-
-
15C: about 50% of maximal activity, 40C: about 35% of maximal activity
25
50
-
activity range, optimum activity at 28C, rapid decrease in activity above 30C, no activity at 60C
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
four different morphotypes of biovar B, strain HS-2 and the strain UW4 as control strain
Manually annotated by BRENDA team
-
strain UW4 AcdS+ (ability to synthesize ACC deaminase and indole acetic acid) and its mutant strain AcdS-
Manually annotated by BRENDA team
Pseudomonas putida UW4
-
strain UW4
-
Manually annotated by BRENDA team
Pseudomonas putida UW4 AcdS+
-
strain UW4 AcdS+ (ability to synthesize ACC deaminase and indole acetic acid) and its mutant strain AcdS-
-
Manually annotated by BRENDA team
-
fruits exhibit ACC deaminase activity during ripening
Manually annotated by BRENDA team
additional information
-
1-aminocyclopropane-1-carboxylate serves as sole nitrogen source
Manually annotated by BRENDA team
additional information
-
no activity is detected in the developing xylem
Manually annotated by BRENDA team
additional information
-
1-aminocyclopropane-1-carboxylate serves as sole nitrogen source
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Pseudomonas putida GR12-2
-
-
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Pseudomonas sp. (strain ACP)
Pseudomonas sp. (strain ACP)
Pseudomonas sp. (strain ACP)
Pseudomonas sp. (strain ACP)
Pseudomonas sp. (strain ACP)
Pseudomonas sp. (strain ACP)
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
69000
-
-
gel filtration, disc gel electrophoresis
104000
-
-
gel filtration
105000
-
-
gel filtration
110000
-
-
-
112000
-
-
disc gel electrophoresis
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 36500
?
-
x * 36500, enzyme expressed in Escherichia coli, SDS-PAGE; x * 36800, calculation from amino acid composition
?
-
x * 42000, SDS-PAGE, x * 41848, mass spectroscopy, x * 41842, calculated
?
Pseudomonas putida UW4
-
x * 42000, SDS-PAGE, x * 41848, mass spectroscopy, x * 41842, calculated
-
multimer
-
x * 35000-42000, SDS-PAGE
multimer
Enterobacter cancerogenus MSA2, Enterobacter cloacae MSA1
-
x * 35000-42000, SDS-PAGE
-
trimer
-
3 * 36500, SDS-PAGE
trimer
-
3 * 35000, SDS-PAGE
trimer
Pseudomonas putida GR12-2
-
3 * 35000, SDS-PAGE
-
dimer
-
2 * 40000, SDS-PAGE
additional information
G5AFQ7, -
ACCD consists of mixed alpha/beta motifs and probable loops, computational structural modeling and rigid ligand docking of ACC deaminase, overview. The catalytic site is located in a homotetrameric structure open to opposite directions separated by about 37.97 A distance arranged around central axis
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
no modification
-
the enzyme expressed in Escherichia coli and in delayed ripening tomatoes is not glycosylated
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
mutants K51T and Y295F in complex with substrate
Q7M523
in complex with substrate 1-aminocyclopropane-1-carboxylate, inhibitor 1-aminocyclopropane-1-phosphonate, product alpha-ketobutanoate, and two D-amino acids
Q00740
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
60
-
-
melting temperature
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-80C, pH 7.5, 8 mg/ml protein, stable for at least 6 months
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
native enzyme by ammonium sulfate fractionation, and anion exchange chromatography
-
expressed in delayed ripening tomato plants
-
Recombinant protein expressed with an N-terminal 6xHis-tag is purified under native/non-denaturing conditions using Ni-NTA Superflow resin.
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
ACC-deaminase encoding gene acdS, and a regulator gene lrp, i.e. acdR
-
expressed in Escherichia coli strain DH5alphaPRO
-
expressed in Escherichia coli DH5alpha cells
E0Y9H8
gene acdS, DNA and amino acid sequence determination and analysis, gene mapping and phylogenetic analysis, fate of the acdS/acdR locus during phenotypic variation in Azospirillum lipoferum 4B
Q1G755
subcloned into pET-11d and expressed in Escherichia coli
-
gene acdS, DNA and amino acid sequence determination, phylogenetic analysis using 16S RNA genetic sequence
-
expression in Escherichia coli
-
gene acdS, DNA and amino acid sequence determination, phylogenetic analysis using 16S RNA genetic sequence
-
DNA and amino acid sequence determination and analysis, phylogenetic analysis
-
DNA and amino acid sequence determination and analysis, sequence compariosn and phylogenetic analysis
G5AFQ7, -
cloning and genotype of Pseudomonas brassicacearum strains, overview
-
expression in Escherichia coli and in delayed ripening tomato
-
expressed in Escherichia coli strain DH5alpha
-
An ACC deaminase minus mutant (AcdS) is constructed by the insertion of a tetracycline resistance gene into the coding region of the bacterial ACC deaminase gene.
-
Pseudomonas putida UW4 ACC deaminase is cloned into the pET30a (+) vector at the EcoRV/HindIII sites. All single and double mutants are constructed using a Phusion Site Directed Mutagenesis Kit.
-
Using non-transformed canola (Brassica napus) or canola transformed with the ACC deaminase gene from Pseudomonas putida UW4. The transformed canola line has two copies of the ACC deaminase gene under the control of the rootspecific Agrobacterium rhizogenes promoter. This homozygous line is created through Agrobacterium tumefaciens transformation of canola callus culture.
-
enzyme expression in Agrobacterium tumefaciens strain C58 leading to increased gene transfer of the recombinant bacterium in transfected plant cells, overview
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wild-type enzyme and mutants Y268F and Y294F as His6-tagged proteins in Escherichia coli
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expressed in Escherichia coli JM109 cells
D3U2Q8, -
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
during the immature green stage in tomato development ACC deaminase activity is low. This activity increases significantly during the late breaker stage, just prior to the orange/red stage of development, and then decreases during later stages of tomato ripening
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ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
K51T
Q7M523
crystal structure in complex with substrate
Y295F
Q7M523
crystal structure in complex with substrate
E295S
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by site-directed mutagenesis, the Pseudomonas putida UW4 single mutant is constructed using pET30a (+) with the full-length ACC deaminase as the template
E295S/L322T
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the double mutant is constructed using the E295S mutant as the template
E295S
Pseudomonas putida UW4
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by site-directed mutagenesis, the Pseudomonas putida UW4 single mutant is constructed using pET30a (+) with the full-length ACC deaminase as the template
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E295S/L322T
Pseudomonas putida UW4
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the double mutant is constructed using the E295S mutant as the template
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Y268F
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site-directed mutagesis, mutant kinetics compared to the wild-type, overview
Y294F
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site-directed mutagesis, mutant kinetics compared to the wild-type, overview
Y268F
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site-directed mutagesis, mutant kinetics compared to the wild-type, overview
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additional information
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construction and complementation of acdS and lrpL mutant strains with wild-type strain D3 ACC deaminase, phenotypes, overview
additional information
Agrobacterium tumefaciens D3
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construction and complementation of acdS and lrpL mutant strains with wild-type strain D3 ACC deaminase, phenotypes, overview
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G44D
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completely inactive, CD spectrum is identical to wild-type
additional information
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construction of a disruption mutant deficient of enzyme activity by insertion of a tetracycline resistance gene into the the coding region of the chromosomal copy of the ACC deaminase gene
G44D
Pseudomonas putida UW4
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completely inactive, CD spectrum is identical to wild-type
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additional information
Pseudomonas putida UW4
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construction of a disruption mutant deficient of enzyme activity by insertion of a tetracycline resistance gene into the the coding region of the chromosomal copy of the ACC deaminase gene
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E295D
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site-directed mutagesis, mutant kinetics compared to the wild-type, overview
additional information
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ACC deaminase enhances Agrobacterium tumefaciens-mediated gene transfer into plant cells, e.g. of Cucumis melo var. cantaloupensis or Arabidopsis thaliana, by converting the direct precursor for ethylene, which inhibits gene transfer, into 2-oxobutanoate, overview
E295D
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site-directed mutagesis, mutant kinetics compared to the wild-type, overview
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additional information
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ACC deaminase enhances Agrobacterium tumefaciens-mediated gene transfer into plant cells, e.g. of Cucumis melo var. cantaloupensis or Arabidopsis thaliana, by converting the direct precursor for ethylene, which inhibits gene transfer, into 2-oxobutanoate, overview
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Y294F
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site-directed mutagesis, mutant kinetics compared to the wild-type, overview
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additional information
Q93AG0
gene-disruption mutant, decreased nodulation efficiency with Pisum sativum
additional information
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random mutagenesis generating a library of mutants for the the elucidation of structure-function relationships
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
agriculture
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increase of root elongation by 1-aminocyclopropane-1-carboxylic acid using bacteria depends significantly on nutrient status of the plant
agriculture
E0Y9H8
Azospirillum lipoferum strain AZm5 containing ACC deaminase activity improves the growth and physiology of tomato (Solanum lycopersicum) plants under a deficiency of and medium doses of nitrogenous fertilizers
agriculture
Azospirillum lipoferum AZm5
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Azospirillum lipoferum strain AZm5 containing ACC deaminase activity improves the growth and physiology of tomato (Solanum lycopersicum) plants under a deficiency of and medium doses of nitrogenous fertilizers
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agriculture
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Burkholderia phytofirmans sp. nov. isolated from surface-sterilized onion roots, shows high enzyme activity and is able to establish rhizosphere and endophytic populations associated with various plants
agriculture
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ability of transgenic tomato plants expressing the enzyme under different promoters to grow in the presence of metal ions
agriculture
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in presence of enzyme-containing bacteria, growth of canola seedlings is enhanced and the 1-aminocyclopropane-1-carboxylic acid levels in these roots are lowered
agriculture
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agriculture
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expression of enzyme in Lycopersicon esculentum yields plant showing a very healthy and more productive phenotype compared to wild-type. Transgenic plants have a higher chlorophyll content, and transgenic fruits show higher lycopene and beta-carotene content. Expression using promoters rolD or 35S is most effective, leading to larger roots, higher chlorophyll leaf and protein content, and increased average fruit weight
agriculture
Enterobacter cloacae CAL3
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in presence of enzyme-containing bacteria, growth of canola seedlings is enhanced and the 1-aminocyclopropane-1-carboxylic acid levels in these roots are lowered
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agriculture
Enterobacter cloacae UW4
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agriculture
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inoculation of Brassica campestris with Methylobacterium fujisawaense results in lower levels of 1-aminocyclopropane-1-carboxylate in the tissues of seeds due to bacterial enzyme activity. Activity of plant 1-aminocyclopropane-1-carboxylate remains lower in treated seedlings leading to lowered ethylene in plants and preventing ethylene inhibition of root elongation
agriculture
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inoculation of Pisum sativum with bacteria expressing enzyme increases shoot biomass in non-polluted soil and root and shoot biomass in non-polluted and Cd-supplemented soils, depending on genotype of host plant
agriculture
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development of tomato plants with delayed fruit ripening by Agrobacterium tumefaciens mediated transfer of a gene encoding 1-aminocyclopropane-1-carboxylic acid deaminase, the enzyme delays fruit ripening by decreasing ethylene synthesis
agriculture
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inoculation of Zea mays or Vigna radiata with isolate of Pseudomonas fluorescens showing high enzymic activity results in 1.6fold increase in fresh biomass of seedling, root and shoot growth as well as nodulation are promoted
agriculture
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inoculation of Pisum sativum with bacteria expressing enzyme stimulates root growth and increases shoot biomass in non-polluted and Cd-supplemented soils, depending on genotype of host plant
agriculture
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in presence of enzyme-containing bacteria, growth of canola seedlings is enhanced and the 1-aminocyclopropane-1-carboxylic acid levels in these roots are lowered
agriculture
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increase of root elongation by 1-aminocyclopropane-1-carboxylic acid using bacteria depends significantly on nutrient status of the plant
agriculture
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inoculation of Zea mays or Vigna radiata with isolate of Pseudomonas putida showing high enzymic activity results in 2fold increase in fresh biomass of seedling, root and shoot growth as well as nodulation are promoted
agriculture
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expression of enzyme in Brassica napus provides the transgenic calona lines with tolerance to the inhibitory effects of salt stress, with the root-specific promoter rolD being the most effective. Improved salt tolerance is most likely due to decreased synthesis of stress ethylene
agriculture
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bacterial strains that contain ACC deaminase confer salt tolerance to plants by lowering salt induced ethylene synthesis
agriculture
Pseudomonas putida UW4
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bacterial strains that contain ACC deaminase confer salt tolerance to plants by lowering salt induced ethylene synthesis
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agriculture
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increase of root elongation by 1-aminocyclopropane-1-carboxylic acid using bacteria depends significantly on nutrient status of the plant
agriculture
Rhizobium spp.
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rapid procedure for isolation of the 1-aminocyclopropane-1-carboxylic acid deaminase-containig bacteria
agriculture
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expression of enzyme in Pisum sativum stimulates root growth and increases root and shoot biomass in non-polluted soils, depending on genotype of host plant. No effect in presence of Cd2+
agriculture
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expression of enzyme in Pisum sativum stimulates root growth and increases root and shoot biomass in non-polluted soils, depending on genotype of host plant. No effect in presence of Cd2+
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