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Literature summary extracted from

  • Li, Y.; Gao, Z.; Hou, H.; Li, L.; Zhang, J.; Yang, H.; Dong, Y.; Tan, H.
    Crystal structure and site-directed mutagenesis of a nitroalkane oxidase from Streptomyces ansochromogenes (2011), Biochem. Biophys. Res. Commun., 405, 344-348.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.13.12.16 expressed in Escherichia coli Streptomyces ansochromogenes

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.7.3.1 wild-type and mutant H179D. Enzyme consists of two domains, a TIM barrel domain bound to FMN and C-terminal domain with a alpha-alpha-alpha-beta-alpha-beta-alpha fold. It shows the typical function as nitroalkane oxidase but its structure is similar to that of 2-nitropropane dioxygenase Streptomyces ansochromogenes
1.13.12.16 crystal structure of NAO from Streptomyces ansochromogenes is determined. It consists of two domains, a TIM barrel domain bound to FMN and C-terminal domain with a novel folding pattern Streptomyces ansochromogenes

Protein Variants

EC Number Protein Variants Comment Organism
1.7.3.1 H179D residue is spatially adjacent to FMN, mutation results in the loss of enzyme activity Streptomyces ansochromogenes
1.7.3.1 H179K residue is spatially adjacent to FMN, mutation results in the loss of enzyme activity Streptomyces ansochromogenes
1.7.3.1 H179V residue is spatially adjacent to FMN, mutation results in the loss of enzyme activity Streptomyces ansochromogenes
1.13.12.16 H179D mutant enzyme shows no activity. Crystal structure of mutant H179D is determined: The structural superimposition of wild-type Sa-NAO and mutant H179D-nitroethane shows no significant structural variation Streptomyces ansochromogenes
1.13.12.16 H179K mutant enzyme shows no activity Streptomyces ansochromogenes
1.13.12.16 H179V mutant enzyme shows no activity Streptomyces ansochromogenes

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.7.3.1 26.8
-
 nitroethane pH 8.0, 28°C Streptomyces ansochromogenes
1.7.3.1 35.7
-
 1-Nitropropane pH 8.0, 28°C Streptomyces ansochromogenes
1.7.3.1 83.5
-
 2-Nitropropane pH 8.0, 28°C Streptomyces ansochromogenes

Organism

EC Number Organism UniProt Comment Textmining
1.7.3.1 Streptomyces ansochromogenes Q9FDD4
-
-
1.13.12.16 Streptomyces ansochromogenes Q9FDD4
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.7.3.1 1-nitropropane + H2O
-
 Streptomyces ansochromogenes propanal + nitrite + H2O2
-
 ?
1.7.3.1 2-nitropropane + H2O
-
 Streptomyces ansochromogenes propanone + nitrite + H2O2
-
 ?
1.7.3.1 additional information enzyme prefers the neutral forms of substrates and only reacts with anionic 2-nitropropane at a low rate Streptomyces ansochromogenes ?
-
 ?
1.7.3.1 nitroethane + H2O
-
 Streptomyces ansochromogenes ethanal + nitrite + H2O2
-
 ?
1.13.12.16 1-nitropropane + O2
-
 Streptomyces ansochromogenes propionaldehyde + HNO2
-
 ?
1.13.12.16 2-nitropropane + O2
-
 Streptomyces ansochromogenes acetone + HNO2
-
 ?
1.13.12.16 nitroethane + O2
-
 Streptomyces ansochromogenes acetaldehyde + HNO2
-
 ?

Subunits

EC Number Subunits Comment Organism
1.7.3.1 dimer crystallization data Streptomyces ansochromogenes

Synonyms

EC Number Synonyms Comment Organism
1.7.3.1 2-npdl
-
 Streptomyces ansochromogenes
1.13.12.16 nitroalkane oxidase
-
 Streptomyces ansochromogenes
1.13.12.16 Sa-NAO
-
 Streptomyces ansochromogenes

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.13.12.16 8
-
 assay at Streptomyces ansochromogenes

Cofactor

EC Number Cofactor Comment Organism Structure
1.7.3.1 FMN
-
 Streptomyces ansochromogenes