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1-Aminocyclopropane-1-carboxylate (ACC) deaminases from Methylobacterium radiotolerans and Methylobacterium nodulans with higher specificity for ACC

Fedorov, Dmitry N ; Ekimova, Galina A ; Doronina, Nina V ; Trotsenko, Yuri A

FEMS microbiology letters, 2013-06, Vol.343 (1), p.70-76 [Periódico revisado por pares]

Oxford, UK: Blackwell Publishing Ltd

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Título:
1-Aminocyclopropane-1-carboxylate (ACC) deaminases from Methylobacterium radiotolerans and Methylobacterium nodulans with higher specificity for ACC
Autor: Fedorov, Dmitry N ; Ekimova, Galina A ; Doronina, Nina V ; Trotsenko, Yuri A
Assuntos: 1‐aminocylopropane‐1‐carboxylate deaminase ; Carbon-Carbon Lyases - chemistry ; Carbon-Carbon Lyases - genetics ; Carbon-Carbon Lyases - isolation & purification ; Carbon-Carbon Lyases - metabolism ; Chromatography, Gel ; Cloning, Molecular ; Computational Biology ; Electrophoresis, Polyacrylamide Gel ; Enzyme Stability ; Escherichia coli ; Escherichia coli - genetics ; Gene Expression ; heterologous expression ; Hydrogen-Ion Concentration ; Kinetics ; Methylobacterium ; Methylobacterium - enzymology ; Methylobacterium - genetics ; methylotroph ; Microbiology ; Molecular Weight ; plant‐bacterial interactions ; Recombinant Proteins - chemistry ; Recombinant Proteins - genetics ; Recombinant Proteins - isolation & purification ; Recombinant Proteins - metabolism ; Sequence Homology ; Substrate Specificity ; Temperature
É parte de: FEMS microbiology letters, 2013-06, Vol.343 (1), p.70-76
Notas: ObjectType-Article-1
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Descrição: Abstract The 1-aminocyclopropane-1-carboxylate (ACC) deaminases (EC 3.4.99.7), the key enzymes of degradation of the precursor of the phytohormone ethylene, have not been well studied despite their great importance for plant–bacterial interactions. Using blast, the open reading frames encoding ACC deaminases were found in the genomes of epiphytic methylotroph Methylobacterium radiotolerans JCM2831 and nodule-forming endosymbiont Methylobacterium nodulans ORS2060. These genes were named acdS and cloned; recombinant proteins were expressed and purified from Escherichia coli. The enzyme from M. nodulans displayed the highest substrate specificity among all of the characterized ACC deaminases (Km 0.80 ± 0.04 mM), whereas the enzyme from M. radiotolerans had Km 1.8 ± 0.3 mM. The kcat values were 111.8 ± 0.2 and 65.8 ± 2.8 min−1 for the enzymes of M. nodulans and M. radiotolerans, respectively. Both enzymes are homotetramers with a molecular mass of 144 kDa, as was demonstrated by size exclusion chromatography and native PAGE. The purified enzymes displayed the maximum activity at 45–50 °C and pH 8.0. Thus, the priority data have been obtained, extending the knowledge of biochemical properties of bacterial ACC deaminases.
Editor: Oxford, UK: Blackwell Publishing Ltd
Idioma: Inglês;Russo

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1-Aminocyclopropane-1-carboxylate (ACC) deaminases from Methylobacterium radiotolerans and Methylobacterium nodulans with higher specificity for ACC

Fedorov, Dmitry N ; Ekimova, Galina A ; Doronina, Nina V ; Trotsenko, Yuri A

Oxford, UK: Blackwell Publishing Ltd

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