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Information on EC 3.5.99.7 - 1-aminocyclopropane-1-carboxylate deaminase and Organism(s) Pseudomonas putida and UniProt Accession Q5PWZ8
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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 putida
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
-
-
-
-
1-aminocyclopropane-1-carboxylic acid deaminase
-
-
-
-
ACC deaminase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
-
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
-
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
-
a precursor for ethylene production in plants
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutyrate + NH3
-
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
alpha-ketobutyrate + NH3
-
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
-
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
-
activity of the mutants, immediate precursor of ethylene in plants
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
alpha-ketobutyrate + NH3
-
lowering the phytohormone ethylene levels in plants
-
-
?
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.
-
-
?
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-oxobutyrate + NH3
-
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
-
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
-
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
-
a precursor for ethylene production in plants
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
alpha-ketobutyrate + NH3
-
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
-
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
-
activity of the mutants, immediate precursor of ethylene in plants
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
alpha-ketobutyrate + NH3
-
lowering the phytohormone ethylene levels in plants
-
-
?
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.
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
ACC deaminase binds one pyridoxal phosphate (PLP) molecule at each subunit via a conserved lysine residue.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ni2+
-
examined strains are tolerant nickel concentrations of up to 13.2 mM in the culture medium
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
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
aminooxyacetic acid
-
0.005-1 mM, enzymatic activity is progressively inhibited as the aminooxyacetic acid concentration is increased
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3.4
1-aminocyclopropane-1-carboxylate
wild type enzyme, pH and temperature not specified in the publication
0.34
D-Cystine
mutant enzyme E295S/L322T, pH and temperature not specified in the publication
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.056
enzyme in strain UW4, pH and temperature not specified in the publication
additional information
additional information
-
2.305, ACC deaminase acitivity in strain 4 (micromol alpha-keto butyrate/mg/h)
additional information
-
2.409 , ACC deaminase acitivity in strain 11 (micromol alpha-keto butyrate/mg/h)
additional information
-
2.981, ACC deaminase acitivity in strain 159 (micromol alpha-keto butyrate/mg/h)
additional information
-
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
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5 - 9.5
-
pH 7.5: about 45% of maximal activity, pH 9.5: 20% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
15
-
15°C: about 50% of maximal activity, 40°C: about 35% of maximal activity
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
four different morphotypes of biovar B, strain HS-2 and the strain UW4 as control strain
-
strain UW4 AcdS+ (ability to synthesize ACC deaminase and indole acetic acid) and its mutant strain AcdS-
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
evolution
-
ACC deaminase producing plant growth promoting rhizobacteria (PGPR) are isolated from the rhizosphere of Triticum aestivum var. Lok-1 and identified using 16S rRNA gene sequence analysis. Isolates are evaluated for various direct and indirect plant growth promoting (PGP) traits. 38 ACC deaminase producing PGPR are isolated which belonged to 12 distinct genera and falling into four phyla gamma-proteobacteria, beta-proteobacteria, Flavobacteria and Firmicutes. Klebsiella sp. is the most abundant genera and followed by Enterobacter sp.
metabolism
-
all the PGPR isolates register phosphate and zinc solubilization accompanied by drop in pH of the medium
physiological function
physiological function
effect of bacterial ACC deaminase overproduction on Medicago lupulina plants growth and nodulation, overview. The biomass production is significantly increased in the plants inoculated with Sinorhizobium meliloti overexpressing the Pseudomonas putida enzyme (pRKACC) or co-inoculated with wild-type Sinorhizobium meliloti and Pseudomonas putida UW4 in comparison with the plants inoculated with wild-type Sinorhizobium meliloti. The dry weight of aerial parts of plants inoculated with Sinorhizobium meliloti overexpressing the Pseudomonas putida enzyme (pRKACC) are enhanced by 31.6 % in the presence of 200 mg/kg Cu2+, and by 54.4 % in the presence of 400 mg/kg Cu2+, as compared with the plants inoculated with wild-type Sinorhizobium meliloti. The dry weight of roots is also significantly increased by 34.6 and 39.4 % in the pRKACC-strain inoculated plants treated with 200 and 400 mg/kg Cu2+. Similarly, a significant increase is also observed in the biomass production of plants co-inoculated with wild-type Sinorhizobium meliloti and Pseudomonas putida UW4
physiological function
recombinant expression of the exogenous 1-aminocyclopropane-1-carboxylate deaminase gene from Pseudomonas putida in psychrotolerant bacteria, i.e. acdS-deficient Flavobacterium sp. strain OR306 and Pseudomonas frederiksbergensis strain OS211, modulates ethylene metabolism and cold-induced genes in tomato under chilling stress. Physiologically evolved stress ethylene and its transcription factors play a role in regulation of cold-induced genes, e.g. LeCBF1 and LeCBF3
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
-
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
41842
-
x * 42000, SDS-PAGE, x * 41848, mass spectroscopy, x * 41842, calculated
41848
-
x * 42000, SDS-PAGE, x * 41848, mass spectroscopy, x * 41842, calculated
42000
-
x * 42000, SDS-PAGE, x * 41848, mass spectroscopy, x * 41842, calculated
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 42000, SDS-PAGE, x * 41848, mass spectroscopy, x * 41842, calculated
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E295S/L322T
the mutations lead to a loss of enzyme activity against 1-aminocyclopropane-1-carboxylate
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
additional information
additional information
gene acdS expressing mutant strains are generated from ACCD negative psychrotolerant bacterial strains Flavobacterium sp. OR306 and Pseudomonas frederiksbergensis OS211, isolated from agricultural soil during late winter. After transformation with plasmid pRKACC-acdS, both the strains are able to exhibit ACCD activity in vitro. On exposing tomato plants inoculated with both acdS expressing and wild-type bacteria to one week of chilling treatment at 12/10°C, stress ethylene, ACC accumulation and ACO activity, which are markers of ethylene stress, are significantly reduced in plants inoculated with the acdS gene transformed mutants. In case of plants inoculated with strain OS211-acdS, ethylene emission, ACC accumulation and ACO activity are significantly reduced by 52%, 75.9%, and 23.2%, respectively, compared to uninoculated control plants. Expression analysis of cold-induced LeCBF1 and LeCBF3 genes shows that these genes in the plants are significantly induced by the acdS transformed mutant bacteria in addition to observed reduced expression of ethylene-responsive transcription factor 13 (ETF-13) and ACO genes
additional information
-
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
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
gene acdS, functional recombinant expression of the exogenous 1-aminocyclopropane-1-carboxylate deaminase gene from Pseudomonas putida in the psychrotolerant bacteria, acdS negative Flavobacterium sp. strain OR306 and Pseudomonas frederiksbergensis strain OS211
gene acdS, recombinant overexpression in Sinorhizobium meliloti strain CCNWSX0020 (ACCC 19736), a Cu-resistant strain isolated from the root nodules of Medicago lupulina plants growing in lead-zinc mine tailings in China, quantitative real-time PCR analysis
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.
-
gene acdS, DNA and amino acid sequence determination and analysis, genotyping
-
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.
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
agriculture
-
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
-
increase of root elongation by 1-aminocyclopropane-1-carboxylic acid using bacteria depends significantly on nutrient status of the plant
agriculture
-
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
-
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
-
bacterial strains that contain ACC deaminase confer salt tolerance to plants by lowering salt induced ethylene synthesis
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
Jacobson, C.B.; Pasternak, J.J.; Glick, B.R.
Partial purification and characterization of 1-aminocyclopropane-1-carboxylate deaminase from the plant growth promoting rhizobacterium Pseudomonas putida GR12-2
Can. J. Microbiol.
40
1019-1025
1994
Pseudomonas putida, Pseudomonas putida GR12-2
-
Penrose, D.M.; Moffatt, B.A.; Glick, B.R.
Determination of 1-aminocycopropane-1-carboxylic acid (ACC) to assess the effects of ACC deaminase-containing bacteria on roots of canola seedlings
Can. J. Microbiol.
47
77-80
2001
Enterobacter cloacae, Pseudomonas putida, Enterobacter cloacae CAL3
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
Hontzeas, N.; Zoidakis, J.; Glick, B.R.; Abu-Omar, M.M.
Expression and characterization of 1-aminocyclopropane-1-carboxylate deaminase from the rhizobacterium Pseudomonas putida UW4: a key enzyme in bacterial plant growth promotion
Biochim. Biophys. Acta
1703
11-19
2004
Pseudomonas putida, Pseudomonas putida UW4
Shaharoona, B.; Arshad, M.; Zahir, Z.A.
Effect of plant growth promoting rhizobacteria containing ACC-deaminase on maize (Zea mays L.) growth under axenic conditions and on nodulation in mung bean (Vigna radiata L.)
Lett. Appl. Microbiol.
42
155-159
2006
Pseudomonas putida, Pseudomonas fluorescens
Sergeeva, E.; Shah, S.; Glick, B.R.
Growth of transgenic canola (Brassica napus cv. Westar) expressing a bacterial 1-aminocyclopropane-1-carboxylate (ACC) deaminase gene on high concentrations of salt
World J. Microbiol. Biotechnol.
22
277-282
2006
Pseudomonas putida
Cheng, Z.; Park, E.; Glick, B.R.
1-Aminocyclopropane-1-carboxylate deaminase from Pseudomonas putida UW4 facilitates the growth of canola in the presence of salt.
Can. J. Microbiol.
53
912-918
2007
Pseudomonas putida, Pseudomonas putida UW4
Shaharoona, B.; Arshad, M.; Khalid, A.
Differential response of etiolated pea seedlings to inoculation with Rhizobacteria capable of utilizing 1-aminocyclopropane-1-carboxylate or L-methionine
J. Microbiol.
45
15-20
2007
Pseudomonas putida, Pseudomonas fluorescens, Pseudomonas fluorescens AM3
Cheng, Z.; Duncker, B.P.; McConkey, B.J.; Glick, B.R.
Transcriptional regulation of ACC deaminase gene expression in Pseudomonas putida UW4
Can. J. Microbiol.
54
128-136
2008
Pseudomonas putida, Pseudomonas putida UW4
Rodriguez, H.; Vessely, S.; Shah, S.; Glick, B.R.
Effect of a nickel-tolerant ACC deaminase-producing Pseudomonas strain on growth of nontransformed and transgenic canola plants
Curr. Microbiol.
57
170-174
2008
Pseudomonas putida
Gamalero, E.; Berta, G.; Massa, N.; Glick, B.R.; Lingua, G.
Synergistic interactions between the ACC deaminase-producing bacterium Pseudomonas putida UW4 and the AM fungus Gigaspora rosea positively affect cucumber plant growth
FEMS Microbiol. Ecol.
64
459-467
2008
Pseudomonas putida, Pseudomonas putida UW4 AcdS+
Jalili, F.; Khavazi, K.; Pazira, E.; Nejati, A.; Rahmani, H.A.; Sadaghiani, H.R.; Miransari, M.
Isolation and characterization of ACC deaminase-producing fluorescent pseudomonads, to alleviate salinity stress on canola (Brassica napus L.) growth
J. Plant Physiol.
166
667-674
2008
Pseudomonas putida, Pseudomonas fluorescens
Todorovic, B.; Glick, B.R.
The interconversion of ACC deaminase and D-cysteine desulfhydrase by diected mutagenesis
Planta
229
193-205
2008
Pseudomonas putida
Zahir, Z.A.; Ghani, U.; Naveed, M.; Nadeem, S.M.; Asghar, H.N.
Comparative effectiveness of Pseudomonas and Serratia sp. containing ACC-deaminase for improving growth and yield of wheat (Triticum aestivum L.) under salt-stressed conditions
Arch. Microbiol.
191
415-424
2009
Pseudomonas aeruginosa, Pseudomonas putida, Serratia proteamaculans
Hao, Y.; Charles, T.C.; Glick, B.R.
ACC deaminase increases the Agrobacterium tumefaciens-mediated transformation frequency of commercial canola cultivars
FEMS Microbiol. Lett.
307
185-190
2010
Agrobacterium tumefaciens, no activity in Agrobacterium tumefaciens, Pseudomonas putida, Agrobacterium tumefaciens YH-2, Pseudomonas putida UW4
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)
Subramanian, P.; Krishnamoorthy, R.; Chanratana, M.; Kim, K.; Sa, T.
Expression of an exogenous 1-aminocyclopropane-1-carboxylate deaminase gene in psychrotolerant bacteria modulates ethylene metabolism and cold induced genes in tomato under chilling stress
Plant Physiol. Biochem.
89
18-23
2015
Pseudomonas putida (Q5PWZ8), Pseudomonas putida UW4 (Q5PWZ8)
Kong, Z.; Glick, B.; Duan, J.; Ding, S.; Tian, J.; McConkey, B.; Wei, G.
Effects of 1-aminocyclopropane-1-carboxylate (ACC) deaminase-overproducing Sinorhizobium meliloti on plant growth and copper tolerance of Medicago lupulina
Plant Soil
391
383-398
2015
Pseudomonas putida (Q5PWZ8), Pseudomonas putida UW4 (Q5PWZ8)
-
Gontia-Mishra, I.; Sapre, S.; Kachare, S.; Tiwari, S.
Molecular diversity of 1-aminocyclopropane-1-carboxylate (ACC) deaminase producing PGPR from wheat (Triticum aestivum L.) rhizosphere
Plant Soil
414
213-227
2017
Acinetobacter baumannii, Acinetobacter calcoaceticus, Acinetobacter sp., Alcaligenes faecalis, Citrobacter sp., Enterobacter sp., Flavobacterium sp., Klebsiella oxytoca, Klebsiella pneumoniae, Klebsiella sp., Pseudomonas aeruginosa, Pseudomonas putida, Stenotrophomonas maltophilia, Enterobacter asburiae, Chryseobacterium sp., Acinetobacter bereziniae, Klebsiella variicola, Enterobacter ludwigii, Atlantibacter hermannii, Chryseobacterium jejuense, Empedobacter brevis (A0A511NK22), Bacillus cereus (G5DCA6), Enterobacter cloacae (Q9ZHW3), Empedobacter brevis ATCC 43319 (A0A511NK22)
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