Aerobic catabolism of phenylacetic acid in Pseudomonas putida U: biochemical characterization of a specific phenylacetic acid transport system and formal demonstration that phenylacetyl-coenzyme A is a catabolic intermediate.

Abstract Sutter’s arginine dihydrolase medium has been modified to obtain maximum yields of arginine dihydrolase. Bromothymol blue is the indicator for alkalinity in Sutter’s medium. By adding glucose and lowering the pH of the medium, more positive reactions were obtained in 24 hr as well as a sharper color contrast to the base medium which facilitated reading the reactions. The modified Sutter’s medium was included in the routine biochemical schema for speciation of pseudomonads isolated from cosmetic products. Of the 706 strains belonging to the 5 species isolated from cosmetic products, only one false negative reaction was obtained with a strain of Pseudomonas putida. The medium was also used for the biochemical characterization of 122 Pseudomonas sp. isolates.

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II. Phenylacetic acid transport system in Penicillium chrysogenum Wis 54-1255: Molecular specificity of its induction.

The Journal of Antibiotics ◽

10.7164/antibiotics.42.1410 ◽

1989 ◽

Vol 42 (9) ◽

pp. 1410-1415 ◽

Cited By ~ 11

Author(s):

JOSÉ M. FERNÁNDEZ-CAÑÓ ◽

ANGEL REGLERO ◽

HONORINA MARTÍNEZ-BIANCO ◽

MIGUEL A. FERRERO ◽

JOSÉ M. LUENGO

Keyword(s):

Transport System ◽

Penicillium Chrysogenum ◽

Phenylacetic Acid ◽

Acid Transport ◽

Molecular Specificity

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Biochemical characterization of a Rhizobium etli monovalent cation-stimulated acyl-coenzyme A carboxylase with a high substrate specificity constant for propionyl-coenzyme A

Microbiology ◽

10.1099/mic.0.26779-0 ◽

2004 ◽

Vol 150 (2) ◽

pp. 399-406 ◽

Cited By ~ 2

Author(s):

Michael F. Dunn ◽

Gisela Araíza ◽

Jaime Mora

Keyword(s):

Coenzyme A ◽

Biochemical Characterization ◽

Electrophoretic Analysis ◽

Monovalent Cation ◽

Gel Chromatography ◽

Rhizobium Etli ◽

Specificity Constant ◽

Acyl Coenzyme A ◽

Acetyl Coenzyme A Carboxylase

Biotin has a profound effect on the metabolism of rhizobia. It is reported here that the activities of the biotin-dependent enzymes acetyl-coenzyme A carboxylase (ACC; EC 6.4.1.2) and propionyl-coenzyme A carboxylase (PCC; EC 6.4.1.3) are present in all species of the five genera comprising the Rhizobiaceae which were examined. Evidence is presented that the ACC and PCC activities detectable in Rhizobium etli extracts are catalysed by a single acyl-coenzyme A carboxylase. The enzyme from R. etli strain 12-53 was purified 478-fold and displayed its highest activity with propionyl-CoA as substrate, with apparent K m and V max values of 0·064 mM and 2885 nmol min−1 (mg protein)−1, respectively. The enzyme carboxylated acetyl-CoA and butyryl-CoA with apparent K m values of 0·392 and 0·144 mM, respectively, and V max values of 423 and 268 nmol min−1 (mg protein)−1, respectively. K+, or Cs+ markedly activated the enzyme, which was essentially inactive in their absence. Electrophoretic analysis indicated that the acyl-CoA carboxylase was composed of a 74 kDa biotin-containing α subunit and a 45 kDa biotin-free β subunit, and gel chromatography indicated a total molecular mass of 620 000 Da. The strong kinetic preference of the enzyme for propionyl-CoA is consistent with its participation in an anaplerotic pathway utilizing this substrate.

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Clinical and biochemical characterization of short-chain acyl-coenzyme A dehydrogenase deficiency

The Journal of Pediatrics ◽

10.1016/s0022-3476(95)70207-5 ◽

1995 ◽

Vol 126 (6) ◽

pp. 910-915 ◽

Cited By ~ 65

Author(s):

Ajay Bhala ◽

Steven M. Willi ◽

Piero Rinaldo ◽

Michael J. Bennett ◽

Eberhard Schmidt-Sommerfeld ◽

...

Keyword(s):

Dehydrogenase Deficiency ◽

Coenzyme A ◽

Biochemical Characterization ◽

Short Chain ◽

Chain Acyl ◽

Acyl Coenzyme A

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Genetic Characterization of the Phenylacetyl-Coenzyme A Oxygenase from the Aerobic Phenylacetic Acid Degradation Pathway of Escherichia coli

Applied and Environmental Microbiology ◽

10.1128/aem.01550-06 ◽

2006 ◽

Vol 72 (11) ◽

pp. 7422-7426 ◽

Cited By ~ 27

Author(s):

Cristina Fernández ◽

Abel Ferrández ◽

Baltasar Miñambres ◽

Eduardo Díaz ◽

José L. García

Keyword(s):

Escherichia Coli ◽

Primary Structure ◽

Phenylacetic Acid ◽

Coenzyme A ◽

Genetic Characterization ◽

Distinct Group ◽

Degradation Pathway ◽

Acid Degradation

ABSTRACT We show here that the paaABCDE genes of the paa cluster responsible for phenylacetate degradation in Escherichia coli W encode a five-component oxygenase that hydroxylates phenylacetyl-coenzyme A (CoA), the first intermediate of the pathway. The primary structure of the subunits of bacterial phenylacetyl-CoA oxygenases revealed that these enzymes constitute the prototype of a new and distinct group of the large bacterial diiron multicomponent oxygenase family.

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