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Literature summary for 3.5.1.3 extracted from

  • Cobzaru, C.; Ganas, P.; Mihasan, M.; Schleberger, P.; Brandsch, R.
    Homologous gene clusters of nicotine catabolism, including a new omega-amidase for alpha-ketoglutaramate, in species of three genera of Gram-positive bacteria (2011), Res. Microbiol., 162, 285-291.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
gene nit, the gene is encoded in the nic-gene cluster located on plasmid pAO1 and flanked by mobile elements Paenarthrobacter nicotinovorans
the gene is encoded in the nic-gene cluster on the chromosome Rhodococcus opacus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2-oxoglutaramate + H2O Rhodococcus opacus
-
2-oxoglutarate + NH3
-
?
2-oxoglutaramate + H2O Nocardioides sp.
-
2-oxoglutarate + NH3
-
?
2-oxoglutaramate + H2O Paenarthrobacter nicotinovorans
-
2-oxoglutarate + NH3
-
?
2-oxoglutaramate + H2O Nocardioides sp. JS614 / ATCC BAA-499
-
2-oxoglutarate + NH3
-
?

Organism

Organism UniProt Comment Textmining
Nocardioides sp.
-
-
-
Nocardioides sp. JS614 / ATCC BAA-499
-
-
-
Paenarthrobacter nicotinovorans
-
gene nit
-
Rhodococcus opacus
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-oxoglutaramate + H2O
-
Rhodococcus opacus 2-oxoglutarate + NH3
-
?
2-oxoglutaramate + H2O
-
Nocardioides sp. 2-oxoglutarate + NH3
-
?
2-oxoglutaramate + H2O
-
Paenarthrobacter nicotinovorans 2-oxoglutarate + NH3
-
?
2-oxoglutaramate + H2O the conserved Cys-Glu-Lys triad is involved in catalysis Paenarthrobacter nicotinovorans 2-oxoglutarate + NH3
-
?
2-oxoglutaramate + H2O
-
Nocardioides sp. JS614 / ATCC BAA-499 2-oxoglutarate + NH3
-
?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
assay at Rhodococcus opacus
30
-
assay at Nocardioides sp.
30
-
assay at Paenarthrobacter nicotinovorans

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.1
-
assay at Rhodococcus opacus
7.1
-
assay at Nocardioides sp.
7.1
-
assay at Paenarthrobacter nicotinovorans

General Information

General Information Comment Organism
metabolism the omega-amidase is involved in the nicotine catabolism, and encoded in organized clusters of homologous genes for nicotine catabolism. The omega-amidase, together with glutamate dehydrogenase, may form a physiologically relevant enzyme couple, leading to transformation of metabolically inert alpha-oxoglutaramate derived from trihydroxypyridine into glutamate, a central compound of nitrogen metabolism Rhodococcus opacus
metabolism the omega-amidase is involved in the nicotine catabolism, and encoded in organized clusters of homologous genes for nicotine catabolism. The omega-amidase, together with glutamate dehydrogenase, may form a physiologically relevant enzyme couple, leading to transformation of metabolically inert alpha-oxoglutaramate derived from trihydroxypyridine into glutamate, a central compound of nitrogen metabolism Nocardioides sp.
metabolism the omega-amidase is involved in the nicotine catabolism, and encoded in organized clusters of homologous genes for nicotine catabolism. The omega-amidase, together with glutamate dehydrogenase, may form a physiologically relevant enzyme couple, leading to transformation of metabolically inert alpha-oxoglutaramate derived from trihydroxypyridine into glutamate, a central compound of nitrogen metabolism Paenarthrobacter nicotinovorans
physiological function the omega-amidase, together with glutamate dehydrogenase, may form a physiologically relevant enzyme couple, leading to transformation of metabolically inert alpha-oxoglutaramate derived from trihydroxypyridine into glutamate, a central compound of nitrogen metabolism Rhodococcus opacus
physiological function the omega-amidase, together with glutamate dehydrogenase, may form a physiologically relevant enzyme couple, leading to transformation of metabolically inert alpha-oxoglutaramate derived from trihydroxypyridine into glutamate, a central compound of nitrogen metabolism Nocardioides sp.
physiological function the omega-amidase, together with glutamate dehydrogenase, may form a physiologically relevant enzyme couple, leading to transformation of metabolically inert alpha-oxoglutaramate derived from trihydroxypyridine into glutamate, a central compound of nitrogen metabolism Paenarthrobacter nicotinovorans