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 hide
3.5.99.7
-
RECOMMENDED NAME
GeneOntology No.
1-aminocyclopropane-1-carboxylate deaminase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
1-aminocyclopropane-1-carboxylate + H2O = 2-oxobutanoate + NH3
show the reaction diagram
1-aminocyclopropane-1-carboxylate = 2-aminobut-2-enoate
show the reaction diagram
(1a)
-
-
-
2-aminobut-2-enoate = 2-iminobutanoate
show the reaction diagram
spontaneous
-
-
-
2-iminobutanoate + H2O = 2-oxobutanoate + NH3
show the reaction diagram
spontaneous
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Deamination
elimination
-
-
of gamma-substituent from alpha amino acid, C-C bond cleavage
-
hydrolysis
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Cysteine and methionine metabolism
-
-
SYSTEMATIC NAME
IUBMB Comments
1-aminocyclopropane-1-carboxylate aminohydrolase (isomerizing)
A pyridoxal 5'-phosphate enzyme. The enzyme, found in certain soil bacteria and fungi, catalyses the ring opening of 1-aminocyclopropane-1-carboxylate, the immediate precursor to ethylene, an important plant hormone that regulates fruit ripening and other processes. The enzyme releases an unstable enamine product that tautomerizes to an imine form, which undergoes a hydrolytic deamination. The latter reaction, which can occur spontaneously, can also be catalysed by EC 3.5.99.10, 2-iminobutanoate/2-iminopropanoate deaminase. The enzyme has been used to make fruit ripening dependent on externally added ethylene, as it removes the substrate for endogenous ethylene formation.
CAS REGISTRY NUMBER
COMMENTARY hide
69553-48-6
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
an avirulent strain, gene acdS
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain 4B, gene acdS
SwissProt
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
Burkholderia caledonica
-
UniProt
Manually annotated by BRENDA team
Burkholderia caledonica LMG 19076
-
UniProt
Manually annotated by BRENDA team
Burkholderia caribensis
-
UniProt
Manually annotated by BRENDA team
Burkholderia caribensis MWAP64
-
UniProt
Manually annotated by BRENDA team
Burkholderia caryophylli
-
-
-
Manually annotated by BRENDA team
Burkholderia caryophylli LMG 2155
-
-
-
Manually annotated by BRENDA team
Burkholderia fungorum
-
UniProt
Manually annotated by BRENDA team
Burkholderia fungorum LMG 16225
-
UniProt
Manually annotated by BRENDA team
Burkholderia graminis
-
UniProt
Manually annotated by BRENDA team
Burkholderia graminis C4D1
-
UniProt
Manually annotated by BRENDA team
Burkholderia kururiensis subsp. kururiensis
-
UniProt
Manually annotated by BRENDA team
Burkholderia phenoliruptrix
-
UniProt
Manually annotated by BRENDA team
Burkholderia phenoliruptrix LMG 22037
-
UniProt
Manually annotated by BRENDA team
Burkholderia phymatum
-
UniProt
Manually annotated by BRENDA team
Burkholderia phymatum STM815
-
UniProt
Manually annotated by BRENDA team
Burkholderia phytofirmans
Burkholderia phytofirmans PsJN
-
UniProt
Manually annotated by BRENDA team
Burkholderia silvatlantica
-
UniProt
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
Burkholderia terricola
-
UniProt
Manually annotated by BRENDA team
Burkholderia terricola LMG 20594
-
UniProt
Manually annotated by BRENDA team
Burkholderia tuberum
-
-
-
Manually annotated by BRENDA team
Burkholderia tuberum STM678
-
-
-
Manually annotated by BRENDA team
Burkholderia unamae
-
UniProt
Manually annotated by BRENDA team
Burkholderia xenovorans
-
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
Cyberlidnera saturnus
-
-
-
Manually annotated by BRENDA team
recovered from the rhizosphere of Jatropha sp., gene acdS
-
-
Manually annotated by BRENDA team
recovered from the rhizosphere of Jatropha sp., gene acdS
-
-
Manually annotated by BRENDA team
strain CAL3
-
-
Manually annotated by BRENDA team
recovered from the rhizosphere of Jatropha sp., gene acdS
-
-
Manually annotated by BRENDA team
strain UW4
-
-
Manually annotated by BRENDA team
inoculation of Brassica campestris
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
-
-
-
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
-
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain N39
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
strain AM3
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
inoculation of Pisum sativum
-
-
Manually annotated by BRENDA team
GR12-2
-
-
Manually annotated by BRENDA team
strain UW4 AcdS+
-
-
Manually annotated by BRENDA team
strain 3F2
-
-
Manually annotated by BRENDA team
Rhizobium spp.
strain Fp2, inoculation of Pisum sativum
-
-
Manually annotated by BRENDA team
strain Fp2, inoculation of Pisum sativum
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1-amino-2-vinylcyclopropane-l-carboxylic acid + H2O
?
show the reaction diagram
-
-
-
-
?
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
alpha-ketobutyrate + NH3
show the reaction diagram
2-vinyl-1-aminocyclopropane-1-carboxylate + H2O
2-keto-5-hexenoate + NH3
show the reaction diagram
-
-
-
?
beta,beta-dichloro-D-alanine + H2O
?
show the reaction diagram
-
-
-
-
?
beta,beta-difluoro-D-alanine + H2O
?
show the reaction diagram
-
-
-
-
?
beta-chloro-D-alanine + H2O
?
show the reaction diagram
-
-
-
-
?
beta-fluoro-D-alanine+ H2O
?
show the reaction diagram
-
-
-
-
?
coronamic acid + H2O
2-oxobutanoate + NH3
show the reaction diagram
D-cysteine + H2O
sulfide + NH3 + pyruvate
show the reaction diagram
D-cystine + H2O
?
show the reaction diagram
D-erythro-2-amino-3-chlorobutyrate + H2O
?
show the reaction diagram
-
-
-
-
?
D-Ser + H2O
?
show the reaction diagram
-
-
-
-
?
D-serine + H2O
?
show the reaction diagram
D-threo-2-amino-3-fluorobutyrate + H2O
?
show the reaction diagram
-
-
-
-
?
D-vinylglycine + H2O
?
show the reaction diagram
-
-
-
-
?
DL-coronamic acid + H2O
?
show the reaction diagram
L-cystine + H2O
?
show the reaction diagram
L-serine + H2O
?
show the reaction diagram
-
-
-
-
?
O-acetyl-D-serine + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
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-oxobutyrate + NH3
show the reaction diagram
1-aminocyclopropane-1-carboxylate + H2O
alpha-ketobutyrate + NH3
show the reaction diagram
D-cysteine + H2O
sulfide + NH3 + pyruvate
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K2HPO4
-
results in highest activity
MgSO4
-
results in highest activity
Ni2+
-
examined strains are tolerant nickel concentrations of up to 13.2 mM in the culture medium
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
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
beta-fluoro-D-Ala
-
-
cyclohexylhydrazine
-
-
homoserine
L-2-aminobutanoate
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
COMMENTARY hide
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]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4.4
1-amino-2-vinylcyclopropane-l-carboxylic acid
-
pH and temperature not specified in the publication
-
0.8 - 12.5
1-aminocyclopropane-1-carboxylate
4
2-vinyl-1-aminocyclopropane-1-carboxylate
-
-
1.1
beta,beta-difluoro-D-alanine
-
pH and temperature not specified in the publication
-
5.4
beta-Chloro-D-alanine
-
pH and temperature not specified in the publication
0.34
D-Cysteine
-
double mutant Pseudomonas putida E295S+L322T
0.25 - 0.34
D-Cystine
97
D-vinylglycine
36.2
DL-coronamic acid
-
pH and temperature not specified in the publication
-
56
O-acetyl-D-serine
-
pH and temperature not specified in the publication
additional information
additional information
-
steady-state kinetics and pH-dependence, overview
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.1 - 146
1-aminocyclopropane-1-carboxylate
5.17
2-vinyl-1-aminocyclopropane-1-carboxylate
Pseudomonas sp.
-
37C, pH 8.5
654
D-Cysteine
Pseudomonas putida
-
double mutant Pseudomonas putida E295S+L322T
0.6
D-vinylglycine
Pseudomonas sp.
-
37C, pH 8.5
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.61 - 2.33
1-aminocyclopropane-1-carboxylate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
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
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
0.44
purified enzyme, at pH 8.0 and 30C
0.74
purified enzyme, at pH 8.0 and 30C
2.812
-
ACC deaminase activity in wild-type enzyme
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.8
-
assay at for mutant Y268F
additional information
-
steady-state kinetics and pH-dependence, overview
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
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 RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
15
-
15C: about 50% of maximal activity, 40C: about 35% of maximal activity
25 - 50
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
fruits exhibit ACC deaminase activity during ripening
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
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
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
69000
-
gel filtration, disc gel electrophoresis
104000
-
gel filtration
105000
-
gel filtration
110000
-
-
112000
-
disc gel electrophoresis
144000
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
2 * 40000, SDS-PAGE
homotetramer
multimer
trimer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
no modification
-
the enzyme expressed in Escherichia coli and in delayed ripening tomatoes is not glycosylated
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
mutants K51T and Y295F in complex with substrate
in complex with substrate 1-aminocyclopropane-1-carboxylate, inhibitor 1-aminocyclopropane-1-phosphonate, product alpha-ketobutanoate, and two D-amino acids
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
-
melting temperature
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80C, pH 7.5, 8 mg/ml protein, stable for at least 6 months
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in delayed ripening tomato plants
-
native enzyme by ammonium sulfate fractionation, and anion exchange chromatography
Ni-NTA agarose column chromatography
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
LITERATURE
ACC-deaminase encoding gene acdS, and a regulator gene lrp, i.e. acdR
-
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.
-
cloning and genotype of Pseudomonas brassicacearum strains, overview
-
DNA and amino acid sequence determination and analysis, phylogenetic analysis
-
DNA and amino acid sequence determination and analysis, sequence compariosn and phylogenetic analysis
enzyme expression in Agrobacterium tumefaciens strain C58 leading to increased gene transfer of the recombinant bacterium in transfected plant cells, overview
-
expressed in Escherichia coli DH5alpha cells
expressed in Escherichia coli JM109 cells
expressed in Escherichia coli Rosetta(DE3) cells
expressed in Escherichia coli strain DH5alpha
-
expressed in Escherichia coli strain DH5alphaPRO
-
expression in Escherichia coli
-
expression in Escherichia coli and in delayed ripening tomato
-
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
gene acdS, DNA and amino acid sequence determination, phylogenetic analysis using 16S RNA genetic sequence
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.
-
subcloned into pET-11d and expressed in Escherichia coli
-
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.
-
wild-type enzyme and mutants Y268F and Y294F as His6-tagged proteins in Escherichia coli
-
EXPRESSION
ORGANISM
UNIPROT
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
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K51T
crystal structure in complex with substrate
Y295F
crystal structure in complex with substrate
E295S
-
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
G44D
-
completely inactive, CD spectrum is identical to wild-type
E295S
-
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
-
the double mutant is constructed using the E295S mutant as the template; the mutations lead to a loss of enzyme activity against 1-aminocyclopropane-1-carboxylate
-
G44D
-
completely inactive, CD spectrum is identical to wild-type
-
E295D
-
site-directed mutagesis, mutant kinetics compared to the wild-type, overview
Y268F
-
site-directed mutagesis, mutant kinetics compared to the wild-type, overview
Y294F
-
site-directed mutagesis, mutant kinetics compared to the wild-type, overview
E295D
-
site-directed mutagesis, mutant kinetics compared to the wild-type, overview
-
Y268F
-
site-directed mutagesis, mutant kinetics compared to the wild-type, overview
-
Y294F
-
site-directed mutagesis, mutant kinetics compared to the wild-type, overview
-
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
agriculture
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