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Literature summary extracted from

  • Sudhamsu, J.; Crane, B.R.
    Structure and reactivity of a thermostable prokaryotic nitric-oxide synthase that forms a long-lived oxy-heme complex (2006), J. Biol. Chem., 281, 9623-9632.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.14.14.47 expression in Escherichia coli Geobacillus kaustophilus

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.14.14.47 to 3.2 A resolution. Residue Lys-356 (Bacillus subtilis NOS) is changed to Arg-365 (gsNOS), substitution alters the conformation of a conserved Asp carboxylate, resulting in movement of an Ile residue toward the heme Geobacillus kaustophilus

Protein Variants

EC Number Protein Variants Comment Organism
1.14.14.47 L356R mutation Lys-356 (Bacillus subtilis NOS) to Arg-365 (gsNOS) substitution alters the conformation of a conserved Asp carboxylate, resulting in movement of an Ile residue toward the heme Geobacillus kaustophilus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.14.14.47 86000
-
 gel filtration Geobacillus kaustophilus

Organism

EC Number Organism UniProt Comment Textmining
1.14.14.47 Geobacillus kaustophilus Q5KZC5
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-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.14.47 2 L-arginine + 2 reduced flavodoxin + 2 O2
-
 Geobacillus kaustophilus 2 Nomega-hydroxy-L-arginine + 2 oxidized flavodoxin + 2 H2O
-
 ?
1.14.14.47 2 Nomega-hydroxy-L-arginine + reduced flavodoxin + 2 O2
-
 Geobacillus kaustophilus 2 L-citrulline + 2 nitric oxide + oxidized flavodoxin + 2 H2O in single turnover experiments with Nomega-hydroxy-L-arginine, NO forms only in the presence of (6R)-tetrahydro-L-biopterin ?
1.14.14.47 additional information addition of oxygen to ferrous NOS results in long-lived heme-oxy complexes in the presence (Soret peak 427 nm) and absence (Soret peak 413 nm) of substrates L-arginine and Nomega-hydroxy-L-arginine. The substrate-induced red shift correlates with hydrogen bonding between substrate and heme-bound oxygen resulting in conversion to a ferric heme-superoxy species Geobacillus kaustophilus ?
-
 ?

Subunits

EC Number Subunits Comment Organism
1.14.14.47 dimer 2 * 43000, calculated Geobacillus kaustophilus

Synonyms

EC Number Synonyms Comment Organism
1.14.14.47 GK1676
-
 Geobacillus kaustophilus

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.14.14.47 80
-
 melting temperature Geobacillus kaustophilus

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.14.47 tetrahydrobiopterin (6R)-tetrahydro-L-biopterin Geobacillus kaustophilus