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Information on EC 3.5.99.7 - 1-aminocyclopropane-1-carboxylate deaminase and Organism(s) Pseudomonas sp. and UniProt Accession Q00740
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3.5.99.7 1-aminocyclopropane-1-carboxylate deaminaseIUBMB Comments
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.
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Word Map
- 3.5.99.7
-
siderophore
-
growth-promoting
- ethylene
- rhizobacteria
- iaa
-
rhizosphere
-
endophytic
- crop
- seedling
- rrna
- indole
-
indole-3-acetic
-
phytoremediation
- enterobacter
-
uninoculated
-
biocontrol
-
biofertilizer
-
non-inoculated
-
deaminase-producing
- canola
-
plant-microbe
-
plant-growth-promoting
- variovorax
- rhizobia
- hcn
-
co-inoculation
-
indoleacetic
-
plant-associated
- alpha-ketobutyrate
-
phytoextraction
- pantoea
-
gnotobiotic
- agriculture
- paenibacillus
- microbacterium
-
rhizoplane
-
phosphate-solubilizing
-
cd-contaminated
-
p-solubilization
- paradoxus
- phaseolina
-
above-ground
-
bacterization
-
macrophomina
-
metal-contaminated
-
bio-inoculants
- curtobacterium
-
metal-resistant
-
plant-beneficial
-
salt-affected
The taxonomic range for the selected organisms is: Pseudomonas sp.
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
hide(Overall reactions are displayed. Show all >>)
Synonyms
acc deaminase, 1-aminocyclopropane-1-carboxylate deaminase, acc-deaminase, 1-aminocyclopropane-1-carboxylic acid deaminase, 1-aminocyclopropane-1-carboxylic acid-deaminase, acpc deaminase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
1-aminocyclopropane-1-carboxylate endolyase (deaminating)
-
-
-
-
1-aminocyclopropane-1-carboxylic acid deaminase
-
-
-
-
ACC deaminase
ACPC deaminase
-
-
-
-
deaminase, 1-aminocyclopropane-1-carboxylate
-
-
-
-
ACC deaminase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
1-aminocyclopropane-1-carboxylate + H2O = 2-oxobutanoate + NH3
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
1-aminocyclopropane-1-carboxylate + H2O = 2-oxobutanoate + NH3
mechanism
-
1-aminocyclopropane-1-carboxylate + H2O = 2-oxobutanoate + NH3
stereochemistry
-
1-aminocyclopropane-1-carboxylate + H2O = 2-oxobutanoate + NH3
ring cleavage is regiospecific and only occurs between the pro-S and the alpha-carbon of 1-aminocyclopropane-1-carboxylate
-
1-aminocyclopropane-1-carboxylate + H2O = 2-oxobutanoate + NH3
ring cleavage of 1-aminocyclopropane-1-carboxylate is a nucleophilic-addition initiated event
-
1-aminocyclopropane-1-carboxylate + H2O = 2-oxobutanoate + NH3
reaction mechanism, detailed overview
-
PATHWAY SOURCE
PATHWAYS
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
69553-48-6
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-vinyl-1-aminocyclopropane-1-carboxylate + H2O
2-keto-5-hexenoate + NH3
-
-
-
?
additional information
?
-
-
1-aminocyclopentane-1-carboxylate, L-homoserine, L-Thr, L-Tryp, L-Met, L-Tyr, L-Cys, and L-aminobutyrate are not a functional substrate
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
-
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
-
effective induction by 1-aminocyclopropane-1-carboxylate and 2-aminobutanoate
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
-
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
-
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
-
-
?
coronamic acid + H2O
2-oxobutanoate + NH3
-
l-coronamic acid and DL-allocoronamic acid are inactive as substrates
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
-
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
-
effective induction by 1-aminocyclopropane-1-carboxylate and 2-aminobutanoate
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
-
the enzyme catalyzes the hydrolytic cleavage of 1-aminocyclopropane-1-carboxylate, the immediate precursor of ethylene, and is therefore an inhibitor of ethylene biosynthesis
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
pyridoxal 5'-phosphate dependent enzyme
pyridoxal 5'-phosphate
-
one mol of subunit contains one mol of pyridoxal 5'-phosphate
pyridoxal 5'-phosphate
-
2.8 mol of tightly bound pyridoxal 5'-phosphate per mol of enzyme
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4.4
1-amino-2-vinylcyclopropane-1-carboxylic acid
-
pH and temperature not specified in the publication
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
additional information
additional information
-
steady-state kinetics and pH-dependence, overview
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
36500
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with substrate 1-aminocyclopropane-1-carboxylate, inhibitor 1-aminocyclopropane-1-phosphonate, product alpha-ketobutanoate, and two D-amino acids
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
-
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
-
increase of root elongation by 1-aminocyclopropane-1-carboxylic acid using bacteria depends significantly on nutrient status of the plant
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Penrose, D.M.; Glick, B.R.
Enzymes that regulate ethylene levels - 1-aminocyclopropane-1-carboxylic acid (ACC) deaminase, ACC synthase and ACC oxidase
Indian J. Exp. Biol.
35
1-17
1997
Enterobacter cloacae, Penicillium citrinum, Pseudomonas sp., Pseudomonas putida, Pseudomonas chlororaphis, Pseudomonas fluorescens, Pseudomonas putida GR12-2, Pseudomonas sp. 3F2
Erion, M.D.; Walsh, C.T.
1-Aminocyclopropanephosphonate: time-dependent inactivation of 1-aminocyclopropanecarboxylate deaminase and Bacillus stearothermophilus alanine racemase by slow dissociation behavior
Biochemistry
26
3417-3425
1987
Pseudomonas sp.
Honma, M.
Reaction of 1-aminocyclopropane-1-carboxylate deaminase with beta-chloro-D-alanine
Agric. Biol. Chem.
50
3189-3190
1986
Pseudomonas sp.
-
Honma, M.
Chemically reactive sulfhydryl groups of 1-aminocyclopropane-1-carboxylate deaminase
Agric. Biol. Chem.
49
567-571
1985
Pseudomonas sp.
-
Liu, H.W.; Auchus, R.; Walsh, C.T.
Stereochemical studies on the reactions catalyzed by the PLP-dependent enzyme 1-aminocyclopropane-1-carboxylate deaminase
J. Am. Chem. Soc.
106
5335-5348
1984
Pseudomonas sp.
-
Hill, R.K.; Prakash, S.R.
Stereochemistry of the enzymatic ring opening of 1-aminocyclopropanecarboxylic acid
J. Am. Chem. Soc.
106
795-796
1984
Pseudomonas sp.
-
Honma, M.
Enzymatic determination of 1-aminocyclopropane-1-carboxylic acid
Agric. Biol. Chem.
47
617-618
1983
Pseudomonas sp.
-
Walsh, C.T.; Pascal, R.A.; Johnston, M.; Raines, R.; Dikshit, D.; Krantz, A.; Honma, M.
Mechanistic studies on the pyridoxal phosphate enzyme 1-aminocyclopropane-1-carboxylate deaminase from Pseudomonas sp.
Biochemistry
20
7509-7519
1981
Pseudomonas sp.
Honma, M.; Shimomura, T.; Shiraishi, K.; Ichihara, A.; Sakamura, S.
Enzymatic deamination of d-coronamic acid: stereoselectivity of 1-aminocyclopropane-1-carboxylate deaminase
Agric. Biol. Chem.
43
1677-1679
1979
Pseudomonas sp.
-
Honma, M.; Shimomura, T.
Metabolism of 1-aminocyclopropane-1-carboxylic acid
Agric. Biol. Chem.
42
1825-1831
1978
Cyberlindnera saturnus, Pseudomonas sp.
-
Li, K.; Du, W.; Que, N.L.S.; Liu, H.W.
Mechanistic studies of 1-aminocyclopropane-1-carboxylate deaminase: unique covalent catalysis by coenzyme B6
J. Am. Chem. Soc.
118
8763-8764
1996
Pseudomonas sp.
-
Belimov, A.A.; Safronova, V.I.; Mimura, T.
Response of spring rape (Brassica napus var. oleifera L.) to inoculation with plant growth promoting rhizobacteria containing 1-aminocyclopropane-1-carboxylate deaminase depends on nutrient status of the plant
Can. J. Microbiol.
48
189-199
2002
Achromobacter xylosoxidans, Pseudomonas sp., Pseudomonas putida
Zhao, Z.; Chen, H.; Li, K.; Du, W.; He, S.; Liu, H.W.
Reaction of 1-amino-2-methylenecyclopropane-1-carboxylate with 1-aminocyclopropane-1-carboxylate deaminase: analysis and mechanistic implications
Biochemistry
42
2089-2103
2003
Pseudomonas sp.
Karthikeyan, S.; Zhou, Q.; Zhao, Z.; Kao, C.L.; Tao, Z.; Robinson, H.; Liu, H.W.; Zhang, H.
Structural analysis of Pseudomonas 1-aminocyclopropane-1-carboxylate deaminase complexes: insight into the mechanism of a unique pyridoxal-5-phosphate dependent cyclopropane ring-opening reaction
Biochemistry
43
13328-13339
2004
Pseudomonas sp. (Q00740), Pseudomonas sp., Pseudomonas sp. ACP (Q00740)
Nonaka, S.; Sugarawa, M.; Minamisawa, K.; Yuhashi, K.-i.; Ezura, H.
1-Aminocyclopropane-1-carboxylate deaminase enhances Agrobacterium tumefaciens-mediated gene transfer into plant cells
Appl. Environ. Microbiol.
74
2526-2528
2008
Pseudomonas sp., Pseudomonas sp. ACP
Thibodeaux, C.J.; Liu, H.W.
Mechanistic studies of 1-aminocyclopropane-1-carboxylate deaminase: characterization of an unusual pyridoxal 5-phosphate-dependent reaction
Biochemistry
50
1950-1962
2011
Pseudomonas sp., Pseudomonas sp. ACP
Nascimento, F.; Rossi, M.; Soares, C.; McConkey, B.; Glick, B.
New insights into 1-aminocyclopropane-1-carboxylate (ACC) deaminase phylogeny, evolution and ecological significance
PLoS ONE
9
e99168
2014
Arabidopsis thaliana, Cyberlindnera saturnus, Penicillium citrinum, Pseudomonas sp., Methylobacterium radiotolerans, Methylobacterium nodulans, Pseudomonas putida (Q5PWZ8), Bradyrhizobium japonicum (Q89XR6), Bradyrhizobium japonicum USDA 110 (Q89XR6), Pseudomonas putida UW4 (Q5PWZ8)
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