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1-amino-2-vinylcyclopropane-1-carboxylic acid + H2O
?
-
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutyrate + NH3
1-aminocyclopropane-1-carboxylate + H2O
alpha-ketobutyrate + NH3
2-vinyl-1-aminocyclopropane-1-carboxylate + H2O
2-keto-5-hexenoate + NH3
-
-
-
?
5-nitroanthranilate + H2O
5-nitrosalicylate + NH3
-
-
-
-
?
beta,beta-dichloro-D-alanine + H2O
?
-
-
-
-
?
beta,beta-difluoro-D-alanine + H2O
?
-
-
-
-
?
beta-chloro-D-alanine + H2O
?
-
-
-
-
?
beta-fluoro-D-alanine + H2O
?
-
-
-
-
?
coronamic acid + H2O
2-oxobutanoate + NH3
D-cysteine + H2O
sulfide + NH3 + pyruvate
D-erythro-2-amino-3-chlorobutyrate + H2O
?
-
-
-
-
?
D-threo-2-amino-3-fluorobutyrate + H2O
?
-
-
-
-
?
D-vinylglycine + H2O
?
-
-
-
-
?
DL-coronamic acid + H2O
?
L-serine + H2O
?
-
-
-
-
?
O-acetyl-D-serine + H2O
?
-
-
-
-
?
additional information
?
-
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
-
-
-
-
?
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
-
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
high substrate specificity of enzyme ACCD
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
high substrate specificity of enzyme ACCD
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
-
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
-
-
-
-
ir
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
-
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
-
-
-
-
?
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
-
-
-
?
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
-
-
-
-
?
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
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
-
?
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
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
-
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
-
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
-
-
-
-
ir
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
-
-
-
?
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
-
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
-
a precursor for ethylene production in plants
-
-
?
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
-
-
-
?
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-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
-
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
-
-
-
?
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
-
-
-
-
?
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
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
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
Rhizobium spp.
-
-
-
-
?
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
-
-
-
?
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
-
-
-
-
?
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-oxobutyrate + NH3
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutyrate + NH3
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
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutyrate + NH3
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
-
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutyrate + NH3
-
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
-
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutyrate + NH3
-
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
-
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutyrate + NH3
-
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutyrate + NH3
-
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
-
-
-
-
?
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-oxobutyrate + 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-oxobutyrate + 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-oxobutyrate + NH3
-
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutyrate + NH3
-
-
-
-
?
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
-
-
?
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
-
-
?
coronamic acid + H2O
2-oxobutanoate + NH3
-
DL-coronamic acid
-
-
?
coronamic acid + H2O
2-oxobutanoate + NH3
-
D-coronamic acid
-
-
?
coronamic acid + H2O
2-oxobutanoate + NH3
-
l-coronamic acid and DL-allocoronamic acid are inactive as substrates
-
-
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
-
-
-
-
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
-
-
-
-
?
D-cystine + H2O
?
-
-
-
-
?
D-cystine + H2O
?
-
-
-
-
?
D-cystine + H2O
?
-
-
-
-
?
D-cystine + H2O
?
-
-
-
-
?
D-cystine + H2O
?
-
-
-
?
D-cystine + H2O
?
-
-
-
?
D-serine + H2O
?
-
-
-
?
D-serine + H2O
?
-
-
-
-
?
D-serine + H2O
?
-
-
-
-
?
D-serine + H2O
?
-
-
-
-
?
DL-coronamic acid + H2O
?
-
-
-
-
?
DL-coronamic acid + H2O
?
-
-
-
-
?
DL-coronamic acid + H2O
?
-
-
-
-
?
L-cystine + H2O
?
-
-
-
-
?
L-cystine + H2O
?
-
-
-
-
?
additional information
?
-
ACC deaminase activity is detected by the following three methods: 2-oxobutyrate production in the coupled reaction with lactate dehydrogenase and NADH, 2-oxobutyrate production by the colorimetric method, and production of ammonium ions in the coupled reaction with glutamate dehydrogenase
-
-
-
additional information
?
-
ACC deaminase activity is detected by the following three methods: 2-oxobutyrate production in the coupled reaction with lactate dehydrogenase and NADH, 2-oxobutyrate production by the colorimetric method, and production of ammonium ions in the coupled reaction with glutamate dehydrogenase
-
-
-
additional information
?
-
beta-chloro-D-alanine is not a functional substrate
-
-
?
additional information
?
-
beta-chloro-D-alanine is not a functional substrate
-
-
?
additional information
?
-
-
beta-chloro-D-alanine and O-acetyl-D-serine are not a functional substrate
-
-
?
additional information
?
-
-
1H NMR spectroscopy for determination of reaction products and metabolites
-
-
-
additional information
?
-
-
DL-allocoronamic acid and dimethyl-1-aminocyclopropane-1-carboxylic acid are not a functional substrate
-
-
?
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
?
-
-
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
?
-
-
the enzyme improves the growth of canola plants after infection with Pseudomonas putida strain UW4 conferring salt tolerance to the plants, overview
-
-
?
additional information
?
-
-
leucine-responsive regulatory protein is a potential regulator of ACC deaminase transcription
-
-
?
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
?
-
-
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
?
-
-
1-aminocyclopentane-1-carboxylate, L-homoserine, L-Thr, L-Tryp, L-Met, L-Tyr, L-Cys, and L-aminobutyrate are not a functional substrate
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutyrate + NH3
1-aminocyclopropane-1-carboxylate + H2O
alpha-ketobutyrate + NH3
5-nitroanthranilate + H2O
5-nitrosalicylate + NH3
-
-
-
-
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
additional information
?
-
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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 plant growth-promoting rhizobacteria stimulate plant growth through the activity of 1-aminocyclopropane-1-carboxylate deaminase
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
a precursor for ethylene production in plants
-
-
?
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-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
-
-
-
?
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 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
-
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
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
-
-
-
-
?
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
-
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
-
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutanoate + NH3
-
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutyrate + NH3
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
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
-
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutyrate + NH3
-
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
-
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
-
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutyrate + NH3
-
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
-
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
-
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
-
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
-
-
-
-
?
1-aminocyclopropane-1-carboxylate + H2O
2-oxobutyrate + NH3
-
-
-
-
?
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
-
-
?
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
-
-
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
-
-
-
-
?
D-cysteine + H2O
sulfide + NH3 + pyruvate
-
-
-
-
?
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
?
-
-
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
?
-
-
the enzyme improves the growth of canola plants after infection with Pseudomonas putida strain UW4 conferring salt tolerance to the plants, overview
-
-
?
additional information
?
-
-
leucine-responsive regulatory protein is a potential regulator of ACC deaminase transcription
-
-
?
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
?
-
-
mycorrhizal colonization, as well as arbuscule abundance, is significantly stimulated by Pseudomonas putida UW4 AcdS+, but not by the AcdS mutant, on cucumber.
-
-
?
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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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
evolution
comparative analysis of 1-aminocyclopropane-1-carboxylate (ACC) deaminase in selected plant growth promoting rhizobacteria (PGPR). The sequence and phylogenetic analysis of ACCD producing PGPR species represents the common conserved domain belonging to the tryptophan synthase beta subunit-like PLP-dependent enzymes superfamily and closely related to each other. The predicted homology models of ACCD of PGPR have similar protein structure with similar folds often share similar function. This analysis represents the evolutionary conservation and same biochemical function of ACCD producing plant growth-promoting rhizobacteria
evolution
comparative analysis of 1-aminocyclopropane-1-carboxylate (ACC) deaminase in selected plant growth promoting rhizobacteria (PGPR). The sequence and phylogenetic analysis of ACCD producing PGPR species represents the common conserved domain belonging to the tryptophan synthase beta subunit-like PLP-dependent enzymes superfamily and closely related to each other. The predicted homology models of ACCD of PGPR have similar protein structure with similar folds often share similar function. This analysis represents the evolutionary conservation and same biochemical function of ACCD producing plant growth-promoting rhizobacteria
evolution
comparative analysis of 1-aminocyclopropane-1-carboxylate (ACC) deaminase in selected plant growth promoting rhizobacteria (PGPR). The sequence and phylogenetic analysis of ACCD producing PGPR species represents the common conserved domain belonging to the tryptophan synthase beta subunit-like PLP-dependent enzymes superfamily and closely related to each other. The predicted homology models of ACCD of PGPR have similar protein structure with similar folds often share similar function. This analysis represents the evolutionary conservation and same biochemical function of ACCD producing plant growth-promoting rhizobacteria
evolution
comparative analysis of 1-aminocyclopropane-1-carboxylate (ACC) deaminase in selected plant growth promoting rhizobacteria (PGPR). The sequence and phylogenetic analysis of ACCD producing PGPR species represents the common conserved domain belonging to the tryptophan synthase beta subunit-like PLP-dependent enzymes superfamily and closely related to each other. The predicted homology models of ACCD of PGPR have similar protein structure with similar folds often share similar function. This analysis represents the evolutionary conservation and same biochemical function of ACCD producing plant growth-promoting rhizobacteria
evolution
comparative analysis of 1-aminocyclopropane-1-carboxylate (ACC) deaminase in selected plant growth promoting rhizobacteria (PGPR). The sequence and phylogenetic analysis of ACCD producing PGPR species represents the common conserved domain belonging to the tryptophan synthase beta subunit-like PLP-dependent enzymes superfamily and closely related to each other. The predicted homology models of ACCD of PGPR have similar protein structure with similar folds often share similar function. This analysis represents the evolutionary conservation and same biochemical function of ACCD producing plant growth-promoting rhizobacteria
evolution
distribution of 1-aminocyclopropane-1-carboxylate deaminase genes among type species of the genus Methylobacterium, overview
evolution
distribution of 1-aminocyclopropane-1-carboxylate deaminase genes among type species of the genus Methylobacterium, overview
evolution
distribution of 1-aminocyclopropane-1-carboxylate deaminase genes among type species of the genus Methylobacterium, overview
evolution
distribution of 1-aminocyclopropane-1-carboxylate deaminase genes among type species of the genus Methylobacterium, overview
evolution
distribution of 1-aminocyclopropane-1-carboxylate deaminase genes among type species of the genus Methylobacterium, overview
evolution
distribution of 1-aminocyclopropane-1-carboxylate deaminase genes among type species of the genus Methylobacterium, overview
evolution
distribution of 1-aminocyclopropane-1-carboxylate deaminase genes among type species of the genus Methylobacterium, overview
evolution
distribution of 1-aminocyclopropane-1-carboxylate deaminase genes among type species of the genus Methylobacterium, overview
evolution
distribution of 1-aminocyclopropane-1-carboxylate deaminase genes among type species of the genus Methylobacterium, overview
evolution
-
library screening and genotyping of rhizosphere soli isolates, sequence comparisons and phylogenetic analysis, overview
evolution
-
phylogenetic, chemotaxonomic, phenotypic and genomic characterisation indicates that the detected strains belong to a distinct genus and species of the order Oceanospirillales for which the names Pokkaliibacter gen.nov., and Pokkaliibacter plantistimulans sp. nov., are proposed with L1E11 / DSM 28732 / MCC 2992 as the type strain. The isolate is found in association with plants grown in brackish environments and possesses plant growth promotion traits such asACC deaminase, siderophore production and phosphate solubilisation. The type species of the genus is Pokkaliibacter plantistimulans
evolution
-
comparative analysis of 1-aminocyclopropane-1-carboxylate (ACC) deaminase in selected plant growth promoting rhizobacteria (PGPR). The sequence and phylogenetic analysis of ACCD producing PGPR species represents the common conserved domain belonging to the tryptophan synthase beta subunit-like PLP-dependent enzymes superfamily and closely related to each other. The predicted homology models of ACCD of PGPR have similar protein structure with similar folds often share similar function. This analysis represents the evolutionary conservation and same biochemical function of ACCD producing plant growth-promoting rhizobacteria
-
evolution
-
comparative analysis of 1-aminocyclopropane-1-carboxylate (ACC) deaminase in selected plant growth promoting rhizobacteria (PGPR). The sequence and phylogenetic analysis of ACCD producing PGPR species represents the common conserved domain belonging to the tryptophan synthase beta subunit-like PLP-dependent enzymes superfamily and closely related to each other. The predicted homology models of ACCD of PGPR have similar protein structure with similar folds often share similar function. This analysis represents the evolutionary conservation and same biochemical function of ACCD producing plant growth-promoting rhizobacteria
-
evolution
-
comparative analysis of 1-aminocyclopropane-1-carboxylate (ACC) deaminase in selected plant growth promoting rhizobacteria (PGPR). The sequence and phylogenetic analysis of ACCD producing PGPR species represents the common conserved domain belonging to the tryptophan synthase beta subunit-like PLP-dependent enzymes superfamily and closely related to each other. The predicted homology models of ACCD of PGPR have similar protein structure with similar folds often share similar function. This analysis represents the evolutionary conservation and same biochemical function of ACCD producing plant growth-promoting rhizobacteria
-
evolution
-
phylogenetic, chemotaxonomic, phenotypic and genomic characterisation indicates that the detected strains belong to a distinct genus and species of the order Oceanospirillales for which the names Pokkaliibacter gen.nov., and Pokkaliibacter plantistimulans sp. nov., are proposed with L1E11 / DSM 28732 / MCC 2992 as the type strain. The isolate is found in association with plants grown in brackish environments and possesses plant growth promotion traits such asACC deaminase, siderophore production and phosphate solubilisation. The type species of the genus is Pokkaliibacter plantistimulans
-
evolution
-
comparative analysis of 1-aminocyclopropane-1-carboxylate (ACC) deaminase in selected plant growth promoting rhizobacteria (PGPR). The sequence and phylogenetic analysis of ACCD producing PGPR species represents the common conserved domain belonging to the tryptophan synthase beta subunit-like PLP-dependent enzymes superfamily and closely related to each other. The predicted homology models of ACCD of PGPR have similar protein structure with similar folds often share similar function. This analysis represents the evolutionary conservation and same biochemical function of ACCD producing plant growth-promoting rhizobacteria
-
evolution
-
distribution of 1-aminocyclopropane-1-carboxylate deaminase genes among type species of the genus Methylobacterium, overview
-
evolution
-
distribution of 1-aminocyclopropane-1-carboxylate deaminase genes among type species of the genus Methylobacterium, overview
-
evolution
-
comparative analysis of 1-aminocyclopropane-1-carboxylate (ACC) deaminase in selected plant growth promoting rhizobacteria (PGPR). The sequence and phylogenetic analysis of ACCD producing PGPR species represents the common conserved domain belonging to the tryptophan synthase beta subunit-like PLP-dependent enzymes superfamily and closely related to each other. The predicted homology models of ACCD of PGPR have similar protein structure with similar folds often share similar function. This analysis represents the evolutionary conservation and same biochemical function of ACCD producing plant growth-promoting rhizobacteria
-
evolution
-
distribution of 1-aminocyclopropane-1-carboxylate deaminase genes among type species of the genus Methylobacterium, overview
-
evolution
-
distribution of 1-aminocyclopropane-1-carboxylate deaminase genes among type species of the genus Methylobacterium, overview
-
evolution
-
phylogenetic, chemotaxonomic, phenotypic and genomic characterisation indicates that the detected strains belong to a distinct genus and species of the order Oceanospirillales for which the names Pokkaliibacter gen.nov., and Pokkaliibacter plantistimulans sp. nov., are proposed with L1E11 / DSM 28732 / MCC 2992 as the type strain. The isolate is found in association with plants grown in brackish environments and possesses plant growth promotion traits such asACC deaminase, siderophore production and phosphate solubilisation. The type species of the genus is Pokkaliibacter plantistimulans
-
evolution
-
phylogenetic, chemotaxonomic, phenotypic and genomic characterisation indicates that the detected strains belong to a distinct genus and species of the order Oceanospirillales for which the names Pokkaliibacter gen.nov., and Pokkaliibacter plantistimulans sp. nov., are proposed with L1E11 / DSM 28732 / MCC 2992 as the type strain. The isolate is found in association with plants grown in brackish environments and possesses plant growth promotion traits such asACC deaminase, siderophore production and phosphate solubilisation. The type species of the genus is Pokkaliibacter plantistimulans
-
evolution
-
comparative analysis of 1-aminocyclopropane-1-carboxylate (ACC) deaminase in selected plant growth promoting rhizobacteria (PGPR). The sequence and phylogenetic analysis of ACCD producing PGPR species represents the common conserved domain belonging to the tryptophan synthase beta subunit-like PLP-dependent enzymes superfamily and closely related to each other. The predicted homology models of ACCD of PGPR have similar protein structure with similar folds often share similar function. This analysis represents the evolutionary conservation and same biochemical function of ACCD producing plant growth-promoting rhizobacteria
-
evolution
-
distribution of 1-aminocyclopropane-1-carboxylate deaminase genes among type species of the genus Methylobacterium, overview
-
evolution
-
phylogenetic, chemotaxonomic, phenotypic and genomic characterisation indicates that the detected strains belong to a distinct genus and species of the order Oceanospirillales for which the names Pokkaliibacter gen.nov., and Pokkaliibacter plantistimulans sp. nov., are proposed with L1E11 / DSM 28732 / MCC 2992 as the type strain. The isolate is found in association with plants grown in brackish environments and possesses plant growth promotion traits such asACC deaminase, siderophore production and phosphate solubilisation. The type species of the genus is Pokkaliibacter plantistimulans
-
evolution
-
comparative analysis of 1-aminocyclopropane-1-carboxylate (ACC) deaminase in selected plant growth promoting rhizobacteria (PGPR). The sequence and phylogenetic analysis of ACCD producing PGPR species represents the common conserved domain belonging to the tryptophan synthase beta subunit-like PLP-dependent enzymes superfamily and closely related to each other. The predicted homology models of ACCD of PGPR have similar protein structure with similar folds often share similar function. This analysis represents the evolutionary conservation and same biochemical function of ACCD producing plant growth-promoting rhizobacteria
-
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.
-
evolution
-
distribution of 1-aminocyclopropane-1-carboxylate deaminase genes among type species of the genus Methylobacterium, overview
-
evolution
-
phylogenetic, chemotaxonomic, phenotypic and genomic characterisation indicates that the detected strains belong to a distinct genus and species of the order Oceanospirillales for which the names Pokkaliibacter gen.nov., and Pokkaliibacter plantistimulans sp. nov., are proposed with L1E11 / DSM 28732 / MCC 2992 as the type strain. The isolate is found in association with plants grown in brackish environments and possesses plant growth promotion traits such asACC deaminase, siderophore production and phosphate solubilisation. The type species of the genus is Pokkaliibacter plantistimulans
-
evolution
-
distribution of 1-aminocyclopropane-1-carboxylate deaminase genes among type species of the genus Methylobacterium, overview
-
evolution
-
distribution of 1-aminocyclopropane-1-carboxylate deaminase genes among type species of the genus Methylobacterium, overview
-
malfunction
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
compared with the wild-type A1501, the acdS mutant A1815 is more sensitive to the environmental stresses of salt and heavy metal shock. The survival rate of A1815 is lowered by 1-2 orders of magnitude compared with the wild-type when exposed to 1.0 M NaCl treatment for 3 h and by 2-3 orders of magnitude when exposed to 13.2 mM NiCl2 for 3 h
malfunction
Sinorhizobium sp. BL3-enhancing ACC deaminase activity (BL3+) and defective mutant (BL3-) strains are constructed, modulation competitiveness is weaker in BL3- than in the wild-type, but is stronger in BL3+. The inoculation of BL3- into mung bean results in less plant growth, a lower nodule dry weight, and smaller nodule number than those in the wild-type, whereas the inoculation of BL3+ has no marked effects
malfunction
-
compared with the wild-type A1501, the acdS mutant A1815 is more sensitive to the environmental stresses of salt and heavy metal shock. The survival rate of A1815 is lowered by 1-2 orders of magnitude compared with the wild-type when exposed to 1.0 M NaCl treatment for 3 h and by 2-3 orders of magnitude when exposed to 13.2 mM NiCl2 for 3 h
-
malfunction
-
the acdS and lrpL double mutant strain Agrobacterium tumefaciens D3-1 has lost the ability to promote plant root elongation
-
malfunction
-
RNAi silencing of the ACCD gene in Trichoderma asperellum shows decreased ability of the mutants to promote root elongation of Brassica napus seedlings
-
metabolism
-
all the PGPR isolates register phosphate and zinc solubilization accompanied by drop in pH of the medium
metabolism
-
all the PGPR isolates register phosphate and zinc solubilization accompanied by drop in pH of the medium
metabolism
-
all the PGPR isolates register phosphate and zinc solubilization accompanied by drop in pH of the medium
metabolism
-
all the PGPR isolates register phosphate and zinc solubilization accompanied by drop in pH of the medium
metabolism
-
all the PGPR isolates register phosphate and zinc solubilization accompanied by drop in pH of the medium
metabolism
-
all the PGPR isolates register phosphate and zinc solubilization accompanied by drop in pH of the medium
metabolism
-
all the PGPR isolates register phosphate and zinc solubilization accompanied by drop in pH of the medium
metabolism
-
all the PGPR isolates register phosphate and zinc solubilization accompanied by drop in pH of the medium
metabolism
-
all the PGPR isolates register phosphate and zinc solubilization accompanied by drop in pH of the medium
metabolism
-
all the PGPR isolates register phosphate and zinc solubilization accompanied by drop in pH of the medium
metabolism
-
all the PGPR isolates register phosphate and zinc solubilization accompanied by drop in pH of the medium
metabolism
-
all the PGPR isolates register phosphate and zinc solubilization accompanied by drop in pH of the medium
metabolism
-
all the PGPR isolates register phosphate and zinc solubilization accompanied by drop in pH of the medium
metabolism
-
all the PGPR isolates register phosphate and zinc solubilization accompanied by drop in pH of the medium
metabolism
-
all the PGPR isolates register phosphate and zinc solubilization accompanied by drop in pH of the medium
metabolism
-
all the PGPR isolates register phosphate and zinc solubilization accompanied by drop in pH of the medium
metabolism
-
all the PGPR isolates register phosphate and zinc solubilization accompanied by drop in pH of the medium
metabolism
all the PGPR isolates register phosphate and zinc solubilization accompanied by drop in pH of the medium
metabolism
all the PGPR isolates register phosphate and zinc solubilization accompanied by drop in pH of the medium
metabolism
all the PGPR isolates register phosphate and zinc solubilization accompanied by drop in pH of the medium
metabolism
-
all the PGPR isolates register phosphate and zinc solubilization accompanied by drop in pH of the medium
metabolism
-
all the PGPR isolates register phosphate and zinc solubilization accompanied by drop in pH of the medium
metabolism
-
all the PGPR isolates register phosphate and zinc solubilization accompanied by drop in pH of the medium
metabolism
impact of gene acdS on the sensitivity and nitrogenase activity under environmental stresses
metabolism
-
impact of gene acdS on the sensitivity and nitrogenase activity under environmental stresses
-
metabolism
-
all the PGPR isolates register phosphate and zinc solubilization accompanied by drop in pH of the medium
-
physiological function
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
-
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 producing bacterial inoculants enhance shoot and root length of rice
physiological function
ACCD is involved in the induction of plant growth promotion by Trichoderma asperellum
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
-
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
-
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
-
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
-
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 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 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 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
-
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
1-aminocyclopropane-1-carboxylate (ACC) deaminase promotes plant growth by sequestering and cleaving the ethylene precursor ACC to 2-oxobutyrate and ammonium. Many plant growth promoting rhizobacteria producing 1-aminocyclopropane-1-carboxylate (ACC) deaminase as a source of nitrogen has an eminent role in plant nutrition
physiological function
1-aminocyclopropane-1-carboxylate (ACC) deaminase promotes plant growth by sequestering and cleaving the ethylene precursor ACC to 2-oxobutyrate and ammonium. Many plant growth promoting rhizobacteria producing 1-aminocyclopropane-1-carboxylate (ACC) deaminase as a source of nitrogen has an eminent role in plant nutrition
physiological function
1-aminocyclopropane-1-carboxylate (ACC) deaminase promotes plant growth by sequestering and cleaving the ethylene precursor ACC to 2-oxobutyrate and ammonium. Many plant growth promoting rhizobacteria producing 1-aminocyclopropane-1-carboxylate (ACC) deaminase as a source of nitrogen has an eminent role in plant nutrition
physiological function
1-aminocyclopropane-1-carboxylate (ACC) deaminase promotes plant growth by sequestering and cleaving the ethylene precursor ACC to 2-oxobutyrate and ammonium. Many plant growth promoting rhizobacteria producing 1-aminocyclopropane-1-carboxylate (ACC) deaminase as a source of nitrogen has an eminent role in plant nutrition
physiological function
1-aminocyclopropane-1-carboxylate (ACC) deaminase promotes plant growth by sequestering and cleaving the ethylene precursor ACC to 2-oxobutyrate and ammonium. Many plant growth promoting rhizobacteria producing 1-aminocyclopropane-1-carboxylate (ACC) deaminase as a source of nitrogen has an eminent role in plant nutrition
physiological function
-
1-aminocyclopropane-1-carboxylate deaminase (ACCD)-producing endophytic Streptomyces sp. GMKU 336 and its ACCD-deficient mutant are inoculated into Thai jasmine rice Khao Dok Mali 105 cultivar (Oryza sativa cv. KDML105) under salt stress (150 mM NaCl) conditions. The results clearly indicate that Streptomyces sp. GMKU 336 significantly increases plant growth, chlorophyll, proline, K+, Ca+, and water contents, but decreases ethylene, reactive oxygen species (ROS), Na+, and Na+/K+ ratio when compared to plants not inoculated and those inoculated with the ACCD-deficient mutant. Genes involved in the ethylene pathway, ACO1 and EREBP1, are significantly downregulated, while acdS encoding ACCD in Streptomyces sp. GMKU 336 is upregulated in vivo. Effects of ACCD-producing Streptomyces sp. GMKU 336 on the rice plants, detailed overview
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
one of the key mechanisms of the effect of bacteria on plant growth and development is their ability to reduce the level of ethylene due to the activity of 1-aminocyclopropanex021-carboxylate deaminase (ACCD). This enzyme catalyzes the hydrolysis of 1-aminocyclopropanex021-carboxylate (ACC), which is an immediate precursor in ethylene biosynthesis, to 2-oxobutyrate and ammonium ions. ACCDx02possessing bacteria contribute to the enhancement of plant resistance to such negative impacts as drought, soil salinity, heavy metal pollution, and the presence of phytopathogens. Amycolatopsis methanolica is a freex02living soil bacterium, apparently not directly associated with plant surface
physiological function
plant growth-promoting effects of Pseudomonas stutzeri wild-type strain A1501 and of A1815 mutant strain on rice plants, overview. Importance of the acdS gene for the plant growth-promoting effect
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
Sinorhizobium sp. BL3 forms symbiotic interactions with mung bean (Vigna radiata cv. SUT1) and contains lrpL-acdS genes, which encode the 1-aminocyclopropane-1-carboxylate (ACC) deaminase enzyme that cleaves ACC, a precursor of plant ethylene synthesis. Detection of ACC deaminase expression by RT-PCR of acdS, and ACC deaminase activity from nodules of mung bean (Vigna radiata cv. SUT1) on the 3rd, 5th, and 7th week after the inoculation with BL3, BL3+, and BL3-. Requirement of ACC deaminase activity in Sinorhizobium sp. BL3 for nodulation competitiveness in mung bean. ACC deaminase activities direct the changing of biochemical molecules
physiological function
the 1-aminocyclopropane-1-carboxylate (ACC) deaminase-expressing endophyte Pseudomonas migulae strain 8R6 increases Catharanthus roseus plant resistance to flavescence Doree phytoplasma infection. Flavescence doree is an epidemic yellows disease of grapevine, caused by a phytoplasma (FDP). Pseudomonas migulae strain 8R6 cells are found in the shoot, while they are completely absent or under the detection limit in leaves and roots. The bacterial strain 8R6, as well as its mutant lacking the ACC deaminase activity, does not promote the growth of either the infected or uninfected plants
physiological function
-
the phytostimulatory effects of the detetcted strain are checked on inoculated pokkali rice variety (Oryzsa sativa VTL-6)
physiological function
-
the phytostimulatory effects of the detetcted strain are checked on inoculated pokkali rice variety (Oryzsa sativa VTL-6). Initial treatment of VTL-6seeds with strain L1E11 does not have any negative effect on the seed germination. Increased root length and fresh weight in L1E11-treated seeds is observed as compared to non-treated pokkali seeds after 14 days of incubation. Strain L1E11 is able to promote rice growth. L1E11-treated rice plants are able to resist 200 mM NaCl stress better as compared to the uninoculated control plants. L1E11 can mediate growth and protect its host plant from saline stress by modulating the stress ethylene levels as like other ACCd producing plant beneficial rhizobacteria functions
physiological function
-
the rhizosphere bacterium containing 1-aminocyclopropane-1-carboxylate deaminase increases growth and photosynthesis of pea (Pisum sativum cv. Alderman) plants under salt stress by limiting Na+ accumulation. When pea is grown with 70 and 130 mM NaCl, the ACC-deaminase containing rhizobacterium Variovorax paradoxus strain 5C-2 increases total biomass by 25 and 54% respectively. Nutrient flow modelling shows that Variovorax paradoxus strain 5C-2 increases K uptake and root to shoot K flow, but decreases Na flow and increases Na deposition in roots. Thus, shoot K+:Na+ ratio increases following Variovorax paradoxus 5C-2 inoculation. At 70 and 130 mM NaCl, rhizobacterial inoculation decreases stomatal resistance by 14 and 31%and decreases xylem balancing pressure by 7 and 21%, respectively. Furthermore, rhizobacterial inoculation improves photosynthetic efficiency (Fv/Fm) by 12 and 19% and increases maximal electron transport rate (ETR) by 18 and 22% at 70 and 130 mM NaCl, respectively
physiological function
-
1-aminocyclopropane-1-carboxylate (ACC) deaminase promotes plant growth by sequestering and cleaving the ethylene precursor ACC to 2-oxobutyrate and ammonium. Many plant growth promoting rhizobacteria producing 1-aminocyclopropane-1-carboxylate (ACC) deaminase as a source of nitrogen has an eminent role in plant nutrition
-
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
-
1-aminocyclopropane-1-carboxylate (ACC) deaminase promotes plant growth by sequestering and cleaving the ethylene precursor ACC to 2-oxobutyrate and ammonium. Many plant growth promoting rhizobacteria producing 1-aminocyclopropane-1-carboxylate (ACC) deaminase as a source of nitrogen has an eminent role in plant nutrition
-
physiological function
-
1-aminocyclopropane-1-carboxylate (ACC) deaminase promotes plant growth by sequestering and cleaving the ethylene precursor ACC to 2-oxobutyrate and ammonium. Many plant growth promoting rhizobacteria producing 1-aminocyclopropane-1-carboxylate (ACC) deaminase as a source of nitrogen has an eminent role in plant nutrition
-
physiological function
-
ACC deaminase producing bacterial inoculants enhance shoot and root length of rice
-
physiological function
-
the phytostimulatory effects of the detetcted strain are checked on inoculated pokkali rice variety (Oryzsa sativa VTL-6)
-
physiological function
-
the phytostimulatory effects of the detetcted strain are checked on inoculated pokkali rice variety (Oryzsa sativa VTL-6). Initial treatment of VTL-6seeds with strain L1E11 does not have any negative effect on the seed germination. Increased root length and fresh weight in L1E11-treated seeds is observed as compared to non-treated pokkali seeds after 14 days of incubation. Strain L1E11 is able to promote rice growth. L1E11-treated rice plants are able to resist 200 mM NaCl stress better as compared to the uninoculated control plants. L1E11 can mediate growth and protect its host plant from saline stress by modulating the stress ethylene levels as like other ACCd producing plant beneficial rhizobacteria functions
-
physiological function
-
ACC deaminase producing bacterial inoculants enhance shoot and root length of rice
-
physiological function
-
1-aminocyclopropane-1-carboxylate (ACC) deaminase promotes plant growth by sequestering and cleaving the ethylene precursor ACC to 2-oxobutyrate and ammonium. Many plant growth promoting rhizobacteria producing 1-aminocyclopropane-1-carboxylate (ACC) deaminase as a source of nitrogen has an eminent role in plant nutrition
-
physiological function
-
plant growth-promoting effects of Pseudomonas stutzeri wild-type strain A1501 and of A1815 mutant strain on rice plants, overview. Importance of the acdS gene for the plant growth-promoting effect
-
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
-
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
-
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
-
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
-
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
-
1-aminocyclopropane-1-carboxylate (ACC) deaminase promotes plant growth by sequestering and cleaving the ethylene precursor ACC to 2-oxobutyrate and ammonium. Many plant growth promoting rhizobacteria producing 1-aminocyclopropane-1-carboxylate (ACC) deaminase as a source of nitrogen has an eminent role in plant nutrition
-
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
-
the phytostimulatory effects of the detetcted strain are checked on inoculated pokkali rice variety (Oryzsa sativa VTL-6)
-
physiological function
-
the phytostimulatory effects of the detetcted strain are checked on inoculated pokkali rice variety (Oryzsa sativa VTL-6). Initial treatment of VTL-6seeds with strain L1E11 does not have any negative effect on the seed germination. Increased root length and fresh weight in L1E11-treated seeds is observed as compared to non-treated pokkali seeds after 14 days of incubation. Strain L1E11 is able to promote rice growth. L1E11-treated rice plants are able to resist 200 mM NaCl stress better as compared to the uninoculated control plants. L1E11 can mediate growth and protect its host plant from saline stress by modulating the stress ethylene levels as like other ACCd producing plant beneficial rhizobacteria functions
-
physiological function
-
ACC deaminase producing bacterial inoculants enhance shoot and root length of rice
-
physiological function
-
the phytostimulatory effects of the detetcted strain are checked on inoculated pokkali rice variety (Oryzsa sativa VTL-6)
-
physiological function
-
the phytostimulatory effects of the detetcted strain are checked on inoculated pokkali rice variety (Oryzsa sativa VTL-6). Initial treatment of VTL-6seeds with strain L1E11 does not have any negative effect on the seed germination. Increased root length and fresh weight in L1E11-treated seeds is observed as compared to non-treated pokkali seeds after 14 days of incubation. Strain L1E11 is able to promote rice growth. L1E11-treated rice plants are able to resist 200 mM NaCl stress better as compared to the uninoculated control plants. L1E11 can mediate growth and protect its host plant from saline stress by modulating the stress ethylene levels as like other ACCd producing plant beneficial rhizobacteria functions
-
physiological function
-
1-aminocyclopropane-1-carboxylate (ACC) deaminase promotes plant growth by sequestering and cleaving the ethylene precursor ACC to 2-oxobutyrate and ammonium. Many plant growth promoting rhizobacteria producing 1-aminocyclopropane-1-carboxylate (ACC) deaminase as a source of nitrogen has an eminent role in plant nutrition
-
physiological function
-
the phytostimulatory effects of the detetcted strain are checked on inoculated pokkali rice variety (Oryzsa sativa VTL-6)
-
physiological function
-
the phytostimulatory effects of the detetcted strain are checked on inoculated pokkali rice variety (Oryzsa sativa VTL-6). Initial treatment of VTL-6seeds with strain L1E11 does not have any negative effect on the seed germination. Increased root length and fresh weight in L1E11-treated seeds is observed as compared to non-treated pokkali seeds after 14 days of incubation. Strain L1E11 is able to promote rice growth. L1E11-treated rice plants are able to resist 200 mM NaCl stress better as compared to the uninoculated control plants. L1E11 can mediate growth and protect its host plant from saline stress by modulating the stress ethylene levels as like other ACCd producing plant beneficial rhizobacteria functions
-
physiological function
-
ACCD is involved in the induction of plant growth promotion by Trichoderma asperellum
-
physiological function
-
the 1-aminocyclopropane-1-carboxylate (ACC) deaminase-expressing endophyte Pseudomonas migulae strain 8R6 increases Catharanthus roseus plant resistance to flavescence Doree phytoplasma infection. Flavescence doree is an epidemic yellows disease of grapevine, caused by a phytoplasma (FDP). Pseudomonas migulae strain 8R6 cells are found in the shoot, while they are completely absent or under the detection limit in leaves and roots. The bacterial strain 8R6, as well as its mutant lacking the ACC deaminase activity, does not promote the growth of either the infected or uninfected plants
-
physiological function
-
the rhizosphere bacterium containing 1-aminocyclopropane-1-carboxylate deaminase increases growth and photosynthesis of pea (Pisum sativum cv. Alderman) plants under salt stress by limiting Na+ accumulation. When pea is grown with 70 and 130 mM NaCl, the ACC-deaminase containing rhizobacterium Variovorax paradoxus strain 5C-2 increases total biomass by 25 and 54% respectively. Nutrient flow modelling shows that Variovorax paradoxus strain 5C-2 increases K uptake and root to shoot K flow, but decreases Na flow and increases Na deposition in roots. Thus, shoot K+:Na+ ratio increases following Variovorax paradoxus 5C-2 inoculation. At 70 and 130 mM NaCl, rhizobacterial inoculation decreases stomatal resistance by 14 and 31%and decreases xylem balancing pressure by 7 and 21%, respectively. Furthermore, rhizobacterial inoculation improves photosynthetic efficiency (Fv/Fm) by 12 and 19% and increases maximal electron transport rate (ETR) by 18 and 22% at 70 and 130 mM NaCl, respectively
-
physiological function
-
one of the key mechanisms of the effect of bacteria on plant growth and development is their ability to reduce the level of ethylene due to the activity of 1-aminocyclopropanex021-carboxylate deaminase (ACCD). This enzyme catalyzes the hydrolysis of 1-aminocyclopropanex021-carboxylate (ACC), which is an immediate precursor in ethylene biosynthesis, to 2-oxobutyrate and ammonium ions. ACCDx02possessing bacteria contribute to the enhancement of plant resistance to such negative impacts as drought, soil salinity, heavy metal pollution, and the presence of phytopathogens. Amycolatopsis methanolica is a freex02living soil bacterium, apparently not directly associated with plant surface
-
physiological function
-
1-aminocyclopropane-1-carboxylate (ACC) deaminase promotes plant growth by sequestering and cleaving the ethylene precursor ACC to 2-oxobutyrate and ammonium. Many plant growth promoting rhizobacteria producing 1-aminocyclopropane-1-carboxylate (ACC) deaminase as a source of nitrogen has an eminent role in plant nutrition
-
physiological function
-
ACC deaminase producing bacterial inoculants enhance shoot and root length of rice
-
physiological function
-
the phytostimulatory effects of the detetcted strain are checked on inoculated pokkali rice variety (Oryzsa sativa VTL-6)
-
physiological function
-
the phytostimulatory effects of the detetcted strain are checked on inoculated pokkali rice variety (Oryzsa sativa VTL-6). Initial treatment of VTL-6seeds with strain L1E11 does not have any negative effect on the seed germination. Increased root length and fresh weight in L1E11-treated seeds is observed as compared to non-treated pokkali seeds after 14 days of incubation. Strain L1E11 is able to promote rice growth. L1E11-treated rice plants are able to resist 200 mM NaCl stress better as compared to the uninoculated control plants. L1E11 can mediate growth and protect its host plant from saline stress by modulating the stress ethylene levels as like other ACCd producing plant beneficial rhizobacteria functions
-
additional information
phylogenetic analysis, structure modeling, and rigid ligand docking of ACC deaminase, coenzyme-substrate docking, overview
additional information
-
phylogenetic analysis, structure modeling, and rigid ligand docking of ACC deaminase, coenzyme-substrate docking, overview
additional information
-
identification of a specific ACC deaminase domain region (ACCD-DR) that, when PCR amplified from the soil, produces a variant pool that can be swapped into functional plasmids carrying ACC deaminase-encoding genes. Functional clones of ACC deaminase are selected for in a competition assay based on their capacity to provide nitrogen to Escherichia coli in vitro. Structure-function analysis
additional information
predicted secondary structure and structure homology modelling using the structure of Cyberlindnera saturnus (PDB ID 1f2d) as template
additional information
predicted secondary structure and structure homology modelling using the structure of Cyberlindnera saturnus (PDB ID 1j0d) as template
additional information
predicted secondary structure and structure homology modelling using the structure of Cyberlindnera saturnus (PDB ID 1j0d) as template
additional information
predicted secondary structure and structure homology modelling using the structure of Pseudomonas sp. ACP (PDB ID 1tzm) as template
additional information
predicted secondary structure and structure homology modelling using the structure of Salmonella enterica subsp. enterica serovar Typhimurium (PDB ID 4d92) as template
additional information
-
using ACC deaminase-producing bacteria in association with plants subjected to a wide range of different kinds of biotic and abiotic stresses can enhance plant tolerance to the stresses
additional information
-
predicted secondary structure and structure homology modelling using the structure of Cyberlindnera saturnus (PDB ID 1j0d) as template
-
additional information
-
using ACC deaminase-producing bacteria in association with plants subjected to a wide range of different kinds of biotic and abiotic stresses can enhance plant tolerance to the stresses
-
additional information
-
predicted secondary structure and structure homology modelling using the structure of Salmonella enterica subsp. enterica serovar Typhimurium (PDB ID 4d92) as template
-
additional information
-
predicted secondary structure and structure homology modelling using the structure of Cyberlindnera saturnus (PDB ID 1j0d) as template
-
additional information
-
predicted secondary structure and structure homology modelling using the structure of Cyberlindnera saturnus (PDB ID 1j0d) as template
-
additional information
-
predicted secondary structure and structure homology modelling using the structure of Cyberlindnera saturnus (PDB ID 1j0d) as template
-
additional information
-
using ACC deaminase-producing bacteria in association with plants subjected to a wide range of different kinds of biotic and abiotic stresses can enhance plant tolerance to the stresses
-
additional information
-
predicted secondary structure and structure homology modelling using the structure of Cyberlindnera saturnus (PDB ID 1j0d) as template
-
additional information
-
predicted secondary structure and structure homology modelling using the structure of Cyberlindnera saturnus (PDB ID 1j0d) as template
-
additional information
-
using ACC deaminase-producing bacteria in association with plants subjected to a wide range of different kinds of biotic and abiotic stresses can enhance plant tolerance to the stresses
-
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ACC-deaminase encoding gene acdS, and a regulator gene lrp, i.e. acdR
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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 and analysis, genotyping
gene acdS, DNA and amino acid sequence determination and analysis, genotyping and phylogenetic analysis
gene acdS, DNA and amino acid sequence determination and analysis, genotyping, phylogenetic analysis and tree
-
gene acdS, DNA and amino acid sequence determination, phylogenetic analysis using 16S RNA genetic sequence
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, phylogenetic analysis
-
gene acdS, phylogenetic tree, recombinant expression of His-tagged enzyme in Escherichia coli strain Rosetta
gene acdS, recombinant expression of His6-tagged ACCD in Escherichia coli strain BL21(DE3)
-
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
gene acdS, RT-PCR enzyme expression analysis
gene acdS, semi-quantitative RT-PCR expression analysis
-
gene acdS, sequence comparisons and phylogenetic analysis
gene PST_1815 or acdS, DNA and amino acid sequence determination and analysis, sequence comparisons, quntitative RT-PCR expression analysis, transcriptional organization of the three consecutive genes, PST1814-16, in the genome of Pseudomonas stutzeri strain A1501, overview
identification of a specific ACC deaminase domain region (ACCD-DR) that, when PCR amplified from the soil, produces a variant pool that can be swapped into functional plasmids carrying ACC deaminase-encoding genes. The ACC deaminase domain regions are recombinantly expressed in Escherichia coli. Functional clones of ACC deaminase are selected for in a competition assay based on their capacity to provide nitrogen to Escherichia coli in vitro, DNA and amino acid sequence determination and analysis
-
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
-
-
-
expressed in Escherichia coli Rosetta(DE3) cells
expressed in Escherichia coli Rosetta(DE3) cells
gene acdS, DNA and amino acid sequence determination and analysis, genotyping
-
gene acdS, DNA and amino acid sequence determination and analysis, genotyping
-
gene acdS, DNA and amino acid sequence determination and analysis, genotyping
-
gene acdS, DNA and amino acid sequence determination and analysis, genotyping
-
gene acdS, DNA and amino acid sequence determination and analysis, genotyping
-
gene acdS, DNA and amino acid sequence determination and analysis, genotyping
-
gene acdS, DNA and amino acid sequence determination and analysis, genotyping
-
gene acdS, DNA and amino acid sequence determination and analysis, genotyping
-
gene acdS, DNA and amino acid sequence determination and analysis, genotyping
-
gene acdS, DNA and amino acid sequence determination and analysis, genotyping
-
gene acdS, DNA and amino acid sequence determination and analysis, genotyping
-
gene acdS, DNA and amino acid sequence determination and analysis, genotyping
-
gene acdS, DNA and amino acid sequence determination and analysis, genotyping
-
gene acdS, DNA and amino acid sequence determination and analysis, genotyping
-
gene acdS, DNA and amino acid sequence determination and analysis, genotyping
-
gene acdS, DNA and amino acid sequence determination and analysis, genotyping
-
gene acdS, DNA and amino acid sequence determination and analysis, genotyping
-
gene acdS, DNA and amino acid sequence determination and analysis, genotyping
gene acdS, DNA and amino acid sequence determination and analysis, genotyping
gene acdS, DNA and amino acid sequence determination and analysis, genotyping
gene acdS, DNA and amino acid sequence determination and analysis, genotyping
-
gene acdS, DNA and amino acid sequence determination and analysis, genotyping
-
gene acdS, DNA and amino acid sequence determination and analysis, genotyping
-
gene acdS, DNA and amino acid sequence determination and analysis, genotyping and phylogenetic analysis
gene acdS, DNA and amino acid sequence determination and analysis, genotyping and phylogenetic analysis
gene acdS, DNA and amino acid sequence determination and analysis, genotyping and phylogenetic analysis
gene acdS, DNA and amino acid sequence determination and analysis, genotyping and phylogenetic analysis
gene acdS, DNA and amino acid sequence determination and analysis, genotyping and phylogenetic analysis
gene acdS, DNA and amino acid sequence determination and analysis, genotyping and phylogenetic analysis
gene acdS, DNA and amino acid sequence determination and analysis, genotyping and phylogenetic analysis
gene acdS, DNA and amino acid sequence determination and analysis, genotyping and phylogenetic analysis
gene acdS, DNA and amino acid sequence determination and analysis, genotyping and phylogenetic analysis
gene acdS, DNA and amino acid sequence determination, phylogenetic analysis using 16S RNA genetic sequence
-
gene acdS, DNA and amino acid sequence determination, phylogenetic analysis using 16S RNA genetic sequence
-
gene acdS, sequence comparisons and phylogenetic analysis
gene acdS, sequence comparisons and phylogenetic analysis
gene acdS, sequence comparisons and phylogenetic analysis
gene acdS, sequence comparisons and phylogenetic analysis
gene acdS, sequence comparisons and phylogenetic analysis
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Tarun, A.S.; Lee, J.S.; Theologis, A.
Random mutagenesis of 1-aminocyclopropane-1-carboxylate synthase: a key enzyme in ethylene biosynthesis
Proc. Natl. Acad. Sci. USA
95
9796-9801
1998
Solanum lycopersicum
brenda
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
brenda
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.
brenda
Honma, M.
Reaction of 1-aminocyclopropane-1-carboxylate deaminase with beta-chloro-D-alanine
Agric. Biol. Chem.
50
3189-3190
1986
Pseudomonas sp.
-
brenda
Honma, M.
Chemically reactive sulfhydryl groups of 1-aminocyclopropane-1-carboxylate deaminase
Agric. Biol. Chem.
49
567-571
1985
Pseudomonas sp.
-
brenda
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.
-
brenda
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.
-
brenda
Honma, M.
Enzymatic determination of 1-aminocyclopropane-1-carboxylic acid
Agric. Biol. Chem.
47
617-618
1983
Pseudomonas sp.
-
brenda
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.
brenda
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.
-
brenda
Honma, M.; Shimomura, T.
Metabolism of 1-aminocyclopropane-1-carboxylic acid
Agric. Biol. Chem.
42
1825-1831
1978
Cyberlindnera saturnus, Pseudomonas sp.
-
brenda
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.
-
brenda
Yao, M.; Horiuchi, A.; Tanaka, I.; Honma, M.
Crystallization of 1-aminocyclopropane-1-carboxylic acid deaminase from yeast
Protein Pept. Lett.
2
305-306
1995
Cyberlindnera saturnus
-
brenda
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
-
brenda
Reed, A.J.; Magin, K.M.; Anderson, J.S.; Austin, G.D.; Rangwala, T.; Linde, D.C.; Love, J.N.; Rogers, S.G.; Fuchs, R.L.
Delayed ripening tomato plants expressing the enzyme 1-aminocyclopropane-1-carboxylic acid deaminase. 1. Molecular characterization, enzyme expression, and fruit ripening traits
J. Agric. Food Chem.
43
1954-1962
1995
Pseudomonas chlororaphis
brenda
Finn, R.F.; Leimgruber, R.M.; Boyle, D.M.; Jennings, M.G.; Kimack, N.M.; Smith, C.E.; Bishop, B.F.; Frazier, R.B.; Magin, K.M.; Fuchs, R.L.; Reed, A.J.
Purification and biochemical comparison of 1-aminocyclopropane-1-carboxylic acid deaminase proteins expressed in delayed ripening tomato and Escherichia coli: studies for a food safety assessment
J. Agric. Food Chem.
44
381-387
1996
Pseudomonas chlororaphis
brenda
Minami, R.; Uchiyama, K.; Murakami, T.; Kawai, J.; Mikami, K.; Yamada, T.; Yokoi, D.; Ito, H.; Matsui, H.; Honma, M.
Properties, sequence, and synthesis in Escherichia coli of 1-aminocyclopropane-1-carboxylate deaminase from Hansenula saturnus
J. Biochem.
123
1112-1118
1998
Cyberlindnera saturnus
brenda
Shah, S.; Li, J.; Moffatt, B.A.; Glick, B.R.
Isolation and characterization of ACC deaminase genes from two different plant growth-promoting rhizobacteria
Can. J. Microbiol.
44
833-843
1998
Enterobacter cloacae
brenda
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
brenda
Ma, W.; Sebestianova, S.B.; Sebestian, J.; Burd, G.I.; Guinel, F.C.; Glick, B.R.
Prevalence of 1-aminocyclopropane-1-carboxylate deaminase in Rhizobium spp
Antonie van Leeuwenhoek
83
285-291
2003
Rhizobium spp.
brenda
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
brenda
Penrose, D.M.; Glick, B.R.
Methods for isolating and characterizing ACC deaminase-containing plant growth-promoting rhizobacteria
Physiol. Plant.
118
10-15
2003
Rhizobium spp.
brenda
Jia, Y.J.; Ito, H.; Matsui, H.; Honma, M.
1-Aminocyclopropane-1-carboxylate (ACC) deaminase induced by ACC synthesized and accumulated in Penicillium citrinum intracellular spaces
Biosci. Biotechnol. Biochem.
64
299-305
2000
Penicillium citrinum
brenda
Ma, W.; Guinel, F.C.; Glick, B.R.
Rhizobium leguminosarum biovar viciae 1-aminocyclopropane-1-carboxylate deaminase promotes nodulation of pea plants
Appl. Environ. Microbiol.
69
4396-4402
2003
Rhizobium leguminosarum (Q93AG0), Rhizobium leguminosarum
brenda
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.
brenda
Yao, M.; Ose, T.; Sugimoto, H.; Horiuchi, A.; Nakagawa, A.; Wakatsuki, S.; Yokoi, D.; Murakami, T.; Honma, M.; Tanaka, I.
Crystal structure of 1-aminocyclopropane-1-carboxylate deaminase from Hansenula saturnus
J. Biol. Chem.
275
34557-34565
2000
Cyberlindnera saturnus
brenda
Ose, T.; Fujino, A.; Yao, M.; Watanabe, N.; Honma, M.; Tanaka, I.
Reaction intermediate structures of 1-aminocyclopropane-1-carboxylate deaminase: insight into PLP-dependent cyclopropane ring-opening reaction
J. Biol. Chem.
278
41069-41076
2003
Cyberlindnera saturnus (Q7M523)
brenda
Grichko, V.P.; Filby, B.; Glick, B.R.
Increased ability of transgenic plants expressing the bacterial enzyme ACC deaminase to accumulate Cd, Co, Cu, Ni, Pb, and Zn
J. Biotechnol.
81
45-53
2000
Enterobacter cloacae, Cyberlindnera saturnus, Enterobacter cloacae UW4
brenda
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)
brenda
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
brenda
Safronova, V.I.; Stepanok, V.V.; Engqvist, G.L.; Alekseyev, Y.V.; Belimov, A.A.
Root-associated bacteria containing 1-aminocyclopropane-1-carboxylate deaminase improve growth and nutrient uptake by pea genotypes cultivated in cadmium supplemented soil
Biol. Fertil. Soils
42
267-272
2006
Pseudomonas marginalis, Rhodococcus sp., Pseudomonas brassicacearum, Rhodococcus sp. Fp2
brenda
Sessitsch, A.; Coenye, T.; Sturz, A.V.; Vandamme, P.; Barka, E.A.; Salles, J.F.; Van Elsas, J.D.; Faure, D.; Reiter, B.; Glick, B.R.; Wang-Pruski, G.; Nowak, J.
Burkholderia phytofirmans sp. nov., a novel plant-associated bacterium with plant-beneficial properties
Int. J. Syst. Evol. Microbiol.
55
1187-1192
2005
Paraburkholderia phytofirmans
brenda
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
brenda
Madhaiyan, M.; Poonguzhali, S.; Ryu, J.; Sa, T.
Regulation of ethylene levels in canola (Brassica campestris) by 1-aminocyclopropane-1-carboxylate deaminase-containing Methylobacterium fujisawaense
Planta
224
268-278
2006
Methylobacterium fujisawaense
brenda
Grichko, V.P.; Glick, B.R.; Grishko, V.I.; Pauls, K.P.
Evaluation of tomato plants with constitutive, root-specific, and stress-induced ACC deaminase gene expression
Russ. J. Plant Physiol.
52
359-364
2005
Enterobacter cloacae
-
brenda
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
brenda
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
brenda
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
brenda
Prigent-Combaret, C. ; Blaha, D.; Pothier, J.F. ; Vial, L.; Poirier, M.-A. ; Wisniewski-Dye, F.; Moenne-Loccoz, Y.
Physical organization and phylogenetic analysis of acdR as leucine responsive regulator of the 1-aminocyclopropane-1-carboxylate deaminase gene acdS in phytobeneficial Azospirillum lipoferum 4B and other Proteobacteria
FEMS Microbiol. Ecol.
2008
1-18
2008
Azospirillum lipoferum (Q1G755), Azospirillum lipoferum 4B (Q1G755)
-
brenda
Madhaiyan, M.; Kim, B.-Y.; Poonguzhali, S.; Kwon,S.-W.; Song, M.-H.; Ryu, J.-H.; Go, S.-J.; Koo, B.-S.; Sa, T.-M.
Methylobacterium oryzae sp. nov., an aerobic, pink-pigmented, facultatively methylotrophic, 1-aminocyclopropane-1-carboxylate deaminase-producing bacterium isolated from rice
Int. J. Syst. Evol. Microbiol.
57
326-331
2007
Methylobacterium oryzae, Methylobacterium oryzae CBMB20 / DSM 18207
brenda
Belimov, A.A.; Dodd, I.C.; Safronova, V.I.; Hontzeas, N.; Davies, W.J.
Pseudomonas brassicacearum strain Am3 containing 1-aminocyclopropane-1-carboxylate deaminase can show both pathogenic and growth-promoting properties in its interaction with tomato
J. Exp. Bot.
58
1485-1495
2007
Pseudomonas brassicacearum
brenda
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
brenda
Madhaiyan, M.; Poonguzhali, S.; Sa, T.
Characterization of 1-aminocyclopropane-1-carboxylate (ACC) deaminase containing Methylobacterium oryzae and interactions with auxins and ACC regulation of ethylene in canola (Brassica campestris)
Planta
226
867-876
2007
Methylobacterium oryzae, no activity in Methylobacterium sp., Methylobacterium oryzae CBMB20 / DSM 18207, no activity in Methylobacterium sp. CBMB120
brenda
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
brenda
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
brenda
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+
brenda
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
brenda
Todorovic, B.; Glick, B.R.
The interconversion of ACC deaminase and D-cysteine desulfhydrase by diected mutagenesis
Planta
229
193-205
2008
Pseudomonas putida
brenda
Onofre-Lemus, J.; Hernandez-Lucas, I.; Girard, L.; Caballero-Mellado, J.
ACC (1-aminocyclopropane-1-carboxylate) deaminase activity, a widespread trait in Burkholderia species, and its growth-promoting effect on tomato plants
Appl. Environ. Microbiol.
75
6581-6590
2009
Burkholderia cenocepacia (B4EJA6), Burkholderia cepacia (B8R7S1), Burkholderia cepacia ATCC 25416 (B8R7S1), Burkholderia stabilis (B8R7T9), Burkholderia stabilis LMG 14294 (B8R7T9), Burkholderia vietnamiensis (B8R7S9), no activity in Burkholderia ambifaria, no activity in Burkholderia tropica, Paraburkholderia caledonica (B8R7R9), Paraburkholderia caledonica LMG 19076 (B8R7R9), Paraburkholderia caribensis (B8R7T5), Paraburkholderia caribensis MWAP64 (B8R7T5), Paraburkholderia fungorum (B8R7T6), Paraburkholderia fungorum LMG 16225 (B8R7T6), Paraburkholderia graminis (B8R7S2), Paraburkholderia graminis C4D1 (B8R7S2), Paraburkholderia kururiensis subsp. kururiensis (B8R7T7), Paraburkholderia phenoliruptrix (B8R7S3), Paraburkholderia phenoliruptrix LMG 22037 (B8R7S3), Paraburkholderia phymatum (B2JYI5), Paraburkholderia phymatum STM815 (B2JYI5), Paraburkholderia phytofirmans (B2TBV3), Paraburkholderia phytofirmans PsJN (B2TBV3), Paraburkholderia silvatlantica (B8R7S5), Paraburkholderia terricola (B8R7S7), Paraburkholderia terricola LMG 20594 (B8R7S7), Paraburkholderia tuberum, Paraburkholderia tuberum STM678, Paraburkholderia unamae (B8R7S8), Paraburkholderia unamae, Paraburkholderia xenovorans (B8R7T2), Trinickia caryophylli, Trinickia caryophylli LMG 2155
brenda
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
brenda
Farajzadeh, D.; Aliasgharzad, N.; Sokhandan Bashir, N.; Yakhchali, B.
Cloning and characterization of a plasmid encoded ACC deaminase from an indigenous Pseudomonas fluorescens FY32
Curr. Microbiol.
61
37-43
2010
Pseudomonas fluorescens
brenda
Shahzad, S.; Khalid, A.; Arshad, M.; Tahir, J.; Mahmood, T.
Improving nodulation, growth and yield of Cicer arietinum L. through bacterial ACC-deaminase induced changes in root architecture
Eur. J. Soil Biol.
46
342-347
2010
Citrobacter koseri, Pseudomonas fluorescens, Pluralibacter gergoviae, Serratia proteamaculans, Pseudomonas fluorescens J108, Pluralibacter gergoviae J107
-
brenda
Viterbo, A.; Landau, U.; Kim, S.; Chernin, L.; Chet, I.
Characterization of ACC deaminase from the biocontrol and plant growth-promoting agent Trichoderma asperellum T203
FEMS Microbiol. Lett.
305
42-48
2010
Trichoderma asperellum (D3U2Q8), Trichoderma asperellum, Trichoderma asperellum T203 (D3U2Q8), Trichoderma asperellum T203
brenda
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
brenda
Kamala-Kannan, S.; Lee, K.J.; Park, S.M.; Chae, J.C.; Yun, B.S.; Lee, Y.H.; Park, Y.J.; Oh, B.T.
Characterization of ACC deaminase gene in Pseudomonas entomophila strain PS-PJH isolated from the rhizosphere soil
J. Basic Microbiol.
50
200-205
2010
Pseudomonas entomophila (C3VP48), Pseudomonas entomophila, Pseudomonas entomophila PS-PJH (C3VP48)
brenda
McDonnell, L.; Plett, J.M.; Andersson-Gunneras, S.; Kozela, C.; Dugardeyn, J.; Van Der Straeten, D.; Glick, B.R.; Sundberg, B.; Regan, S.
Ethylene levels are regulated by a plant encoded 1-aminocyclopropane-1-carboxylic acid deaminase
Physiol. Plant.
136
94-109
2009
Arabidopsis thaliana, Populus tremula
brenda
Plett. J.M.; McDonnell, L.; Regan, S.
Plant encoded 1-aminocyclopropane-1-carboxylic acid deaminase activity implicated in different aspects of plant development
Plant Signal. Behav.
4
1186-1189
2009
Solanum lycopersicum
brenda
Esquivel-Cote, R.; Ramrez-Gama, R.; Tsuzuki-Reyes, G.; Orozco-Segovia, A.; Huante, P.
Azospirillum lipoferum strain AZm5 containing 1-aminocyclopropane-1-carboxylic acid deaminase improves early growth of tomato seedlings under nitrogen deficiency
Plant Soil
337
65-75
2010
no activity in Azospirillum brasilense, Azospirillum lipoferum (E0Y9H8), Azospirillum lipoferum AZm5 (E0Y9H8)
-
brenda
Chinnadurai, C.; Balachandar, D.; Sundaram, S.
Characterization of 1-aminocyclopropane-1-carboxylate deaminase producing methylobacteria from phyllosphere of rice and their role in ethylene regulation
World J. Microbiol. Biotechnol.
25
1403-1411
2009
Methylobacterium sp., Pseudomonas fluorescens, Methylobacterium oryzae, Methylobacterium radiotolerans (B9W0P4), Methylobacterium oryzae CBMB20 / DSM 18207, Pseudomonas fluorescens Pf1, Methylobacterium radiotolerans COLR1 (B9W0P4), Methylobacterium sp. WP1
-
brenda
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
brenda
Hao, Y.; Charles, T.C.; Glick, B.R.
ACC deaminase activity in avirulent Agrobacterium tumefaciens D3
Can. J. Microbiol.
57
278-286
2011
Agrobacterium tumefaciens, Agrobacterium tumefaciens D3
brenda
Jha, C.K.; Annapurna, K.; Saraf, M.
Isolation of Rhizobacteria from Jatropha curcas and characterization of produced ACC deaminase
J. Basic Microbiol.
52
285-295
2012
Enterobacter cancerogenus, Enterobacter cancerogenus MSA2, Enterobacter cloacae, Enterobacter cloacae MSA1
brenda
Singh, N.; Kashyap, S.
In silico identification and characterization of 1-aminocyclopropane-1-carboxylate deaminase from Phytophthora sojae
J. Mol. Model.
18
4101-4111
2012
Phytophthora sojae (G5AFQ7), Phytophthora sojae
brenda
Siddikee, M.A.; Glick, B.R.; Chauhan, P.S.; Yim, W.; Sa, T.
Enhancement of growth and salt tolerance of red pepper seedlings (Capsicum annuum L.) by regulating stress ethylene synthesis with halotolerant bacteria containing 1-aminocyclopropane-1-carboxylic acid deaminase activity
Plant Physiol. Biochem.
49
427-434
2011
Capsicum annuum
brenda
Fedorov, D.N.; Ekimova, G.A.; Doronina, N.V.; Trotsenko, Y.A.
1-Aminocyclopropane-1-carboxylate (ACC) deaminases from Methylobacterium radiotolerans and Methylobacterium nodulans with higher specificity for ACC
FEMS Microbiol. Lett.
343
70-76
2013
Methylobacterium nodulans (B8IP05), Methylobacterium nodulans ORS 2060 (B8IP05), Methylobacterium radiotolerans (B1M5C5), Methylobacterium radiotolerans JCM 2831 (B1M5C5)
brenda
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)
brenda
Ekimova, G.; Fedorov, D.; Tani, A.; Doronina, N.; Trotsenko, Y.
Distribution of 1-aminocyclopropane-1-carboxylate deaminase and d-cysteine desulfhydrase genes among type species of the genus Methylobacterium
Antonie van Leeuwenhoek
111
1723-1734
2018
Methylobacterium brachiatum (A0A346M1A9), Methylobacterium brachiatum B0021 (A0A346M1A9), Methylobacterium fujisawaense (A0A346M1B0), Methylobacterium fujisawaense 0-31 (A0A346M1B0), Methylobacterium gnaphalii (A0A512JJT7), Methylobacterium goesingense (A0A2H4NI51), Methylobacterium goesingense iEII3 (A0A2H4NI51), Methylobacterium gregans (A0A2H4NI69), Methylobacterium gregans 002-074 (A0A2H4NI69), Methylobacterium longum (A0A2H4NI68), Methylobacterium longum 440 (A0A2H4NI68), Methylobacterium marchantiae (A0A2H4NI67), Methylobacterium marchantiae JT1 (A0A2H4NI67), Methylobacterium mesophilicum (A0A2H4NI93), Methylobacterium mesophilicum A47 (A0A2H4NI93), Methylobacterium tardum (A0A346M1B1), Methylobacterium tardum RB677 (A0A346M1B1)
brenda
Gao, J.; Yuan, M.; Wang, X.; Qiu, T.; Li, J.; Liu, H.; Li, X.; Chen, J.; Sun, J.
Variovorax guangxiensis sp. nov., an aerobic, 1-aminocyclopropane-1-carboxylate deaminase producing bacterium isolated from banana rhizosphere
Antonie van Leeuwenhoek
107
65-72
2015
Variovorax guangxiensis, Variovorax guangxiensis ACCC 05911, Variovorax guangxiensis DSM 27352, Variovorax guangxiensis GXGD002
brenda
Jin, Z.; Di Rienzi, S.C.; Janzon, A.; Werner, J.J.; Angenent, L.T.; Dangl, J.L.; Fowler, D.M.; Ley, R.E.
Novel rhizosphere soil alleles for the enzyme 1-aminocyclopropane-1-carboxylate deaminase queried for function with an in vivo competition assay
Appl. Environ. Microbiol.
82
1050-1059
2016
uncultured bacterium
brenda
Wang, Q.; Dodd, I.; Belimov, A.; Jiang, F.
Rhizosphere bacteria containing 1-aminocyclopropane-1-carboxylate deaminase increase growth and photosynthesis of pea plants under salt stress by limiting Na+ accumulation
Funct. Plant Biol.
43
161-172
2016
Variovorax paradoxus, Variovorax paradoxus 5C-2
-
brenda
Han, Y.; Wang, R.; Yang, Z.; Zhan, Y.; Ma, Y.; Ping, S.; Zhang, L.; Lin, M.; Yan, Y.
1-Aminocyclopropane-1-carboxylate deaminase from Pseudomonas stutzeri A1501 facilitates the growth of rice in the presence of salt or Hheavy metals
J. Microbiol. Biotechnol.
25
1119-1128
2015
Pseudomonas stutzeri (A4VKI8), Pseudomonas stutzeri, Pseudomonas stutzeri A1501 (A4VKI8), Pseudomonas stutzeri A1501
brenda
Singh, S.; Yadav, S.; Mishra, P.; Maurya, R.; Rana, V.; Yadav, A.; Singh, A.; Ram, G.; Ramteke, P.
Comparative analysis of 1-aminocyclopropane-1-carboxylate (ACC) deaminase in selected plant growth promoting rhizobacteria (PGPR)
J. Pure Appl. Microbiol.
9
1587-1596
2015
Francisella tularensis subsp. holarctica (A0A0B6CW37), Phyllobacterium brassicacearum (A4GXB0), Azospirillum lipoferum (Q1G755), Pseudomonas fluorescens (Q51813), Bacillus cereus (Q81BE9), Bacillus cereus ATCC 14579 (Q81BE9), Francisella tularensis subsp. holarctica OSU18 (A0A0B6CW37), Bacillus cereus NRRL B-3711 (Q81BE9), Bacillus cereus NCIMB 9373 (Q81BE9), Bacillus cereus DSM 31 (Q81BE9), Bacillus cereus NBRC 15305 (Q81BE9), Bacillus cereus JCM 2152 (Q81BE9)
-
brenda
Tittabutr, P.; Sripakdi, S.; Boonkerd, N.; Tanthanuch, W.; Minamisawa, K.; Teaumroong, N.
Possible role of 1-aminocyclopropane-1-carboxylate (ACC) deaminase activity of Sinorhizobium sp. BL3 on symbiosis with mung bean and determinate nodule senescence
Microbes Environ.
30
310-320
2015
Sinorhizobium sp. BL3 (A8VU64)
brenda
Ekimova, G.; Fedorov, D.; Doronina, N.; Trotsenko, Y.
1-Aminocyclopropane-1-carboxylate deaminase of the aerobic facultative methylotrophic actinomycete Amycolatopsis methanolica 239
Microbiology
84
584-586
2015
Amycolatopsis methanolica (A0A076MQB4), Amycolatopsis methanolica 239 (A0A076MQB4)
-
brenda
Liu, C.H.; Wang, S.A.; Ruszczycky, M.W.; Chen, H.; Li, K.; Murakami, K.; Liu, H.W.
Studies of 1-amino-2,2-difluorocyclopropane-1-carboxylic acid mechanism of decomposition and inhibition of 1-aminocyclopropane-1-carboxylic acid deaminase
Org. Lett.
17
3342-3345
2015
Escherichia coli
brenda
Gamalero, E.; Marzachi, C.; Galetto, L.; Veratti, F.; Massa, N.; Bona, E.; Novello, G.; Glick, B.; Ali, S.; Cantamessa, S.; D'Agostino, G.; Berta, G.
An 1-aminocyclopropane-1-carboxylate (ACC) deaminase-expressing endophyte increases plant resistance to flavescence Doree phytoplasma infection
Plant Biosyst.
151
331-340
2017
Pseudomonas migulae (A0A1H5L0M7), Pseudomonas migulae 8R6 (A0A1H5L0M7)
-
brenda
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)
brenda
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)
-
brenda
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)
-
brenda
Jaemsaeng, R.; Jantasuriyarat, C.; Thamchaipenet, A.
Molecular interaction of 1-aminocyclopropane-1-carboxylate deaminase (ACCD)-producing endophytic Streptomyces sp. GMKU 336 towards salt-stress resistance of Oryza sativa L. cv. KDML105
Sci. Rep.
8
1950
2018
Streptomyces sp. GMKU 336
brenda
Krishnan, R.; Lang, E.; Midha, S.; Patil, P.B.; Rameshkumar, N.
Isolation and characterization of a novel 1-aminocyclopropane-1-carboxylate (ACC) deaminase producing plant growth promoting marine Gammaproteobacteria from crops grown in brackish environments. Proposal for Pokkaliibacter plantistimulans gen. nov., sp. n
Syst. Appl. Microbiol.
41
570-580
2018
Pokkaliibacter plantistimulans, Pokkaliibacter plantistimulans MCC 2992, Pokkaliibacter plantistimulans 228, Pokkaliibacter plantistimulans DSM 28732, Pokkaliibacter plantistimulans L1E11, Pokkaliibacter plantistimulans L1E4
brenda