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Literature summary for 1.14.13.250 extracted from

  • Ng, T.; Rohac, R.; Mitchell, A.; Boal, A.; Balskus, E.
    An N-nitrosating metalloenzyme constructs the pharmacophore of streptozotocin (2019), Nature, 566, 94-99 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.14.13.250

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Streptomyces achromogenes subsp. streptozoticus

Crystallization (Commentary)

Crystallization (Comment) Organism
structure of the selenomethionine derivative, to 2.08 A resolution shows a dimer with three distinct domains Streptomyces achromogenes subsp. streptozoticus

Protein Variants

Protein Variants Comment Organism
D315A complete loss of activity Streptomyces achromogenes subsp. streptozoticus
E215A complete loss of activity Streptomyces achromogenes subsp. streptozoticus
E281A complete loss of activity Streptomyces achromogenes subsp. streptozoticus
H225A complete loss of activity Streptomyces achromogenes subsp. streptozoticus
H311A complete loss of activity Streptomyces achromogenes subsp. streptozoticus
H318A complete loss of activity Streptomyces achromogenes subsp. streptozoticus
H407A/H409A/H448A variant accumulates intermediate Ndelta,Nomega-dihydroxy-Nomega-methyl-L-arginine but does not generate the final product Streptomyces achromogenes subsp. streptozoticus

Metals/Ions

Metals/Ions Comment Organism Structure
Iron recombinant protein purified aerobically contains around 0.9 Fe per monomer Streptomyces achromogenes subsp. streptozoticus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Streptomyces achromogenes subsp. streptozoticus SznF activity requires FeII, oxygen and external reductants. L-arginine is not accepted as a substrate ?
-
-
Ndelta,Nomega-dihydroxy-Nomega-methyl-L-arginine + O2 Streptomyces achromogenes subsp. streptozoticus
-
 Ndelta-hydroxy-Nomega-methyl-Nomega-nitroso-L-citrulline + H2O
-
 ?
Ndelta-hydroxy-Nomega-methyl-L-arginine + NADH + H+ + O2 Streptomyces achromogenes subsp. streptozoticus
-
 Ndelta,Nomega-dihydroxy-Nomega-methyl-L-arginine + NAD+ + H2O
-
 ?
Nomega-methyl-L-arginine + 2 NADH + 2 H+ + 3 O2 Streptomyces achromogenes subsp. streptozoticus
-
 Ndelta-hydroxy-Nomega-methyl-Nomega-nitroso-L-citrulline + 2 NAD+ + 3 H2O
-
 ?
Nomega-methyl-L-arginine + NADH + H+ + O2 Streptomyces achromogenes subsp. streptozoticus
-
 Ndelta-hydroxy-Nomega-methyl-L-arginine + NAD+ + H2O
-
 ?

Organism

Organism UniProt Comment Textmining
Streptomyces achromogenes subsp. streptozoticus A0A411MR89
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information SznF activity requires FeII, oxygen and external reductants. L-arginine is not accepted as a substrate Streptomyces achromogenes subsp. streptozoticus ?
-
-
Ndelta,Nomega-dihydroxy-Nomega-methyl-L-arginine + O2
-
 Streptomyces achromogenes subsp. streptozoticus Ndelta-hydroxy-Nomega-methyl-Nomega-nitroso-L-citrulline + H2O
-
 ?
Ndelta-hydroxy-Nomega-methyl-L-arginine + NADH + H+ + O2
-
 Streptomyces achromogenes subsp. streptozoticus Ndelta,Nomega-dihydroxy-Nomega-methyl-L-arginine + NAD+ + H2O
-
 ?
Nomega-methyl-L-arginine + 2 NADH + 2 H+ + 3 O2
-
 Streptomyces achromogenes subsp. streptozoticus Ndelta-hydroxy-Nomega-methyl-Nomega-nitroso-L-citrulline + 2 NAD+ + 3 H2O
-
 ?
Nomega-methyl-L-arginine + NADH + H+ + O2
-
 Streptomyces achromogenes subsp. streptozoticus Ndelta-hydroxy-Nomega-methyl-L-arginine + NAD+ + H2O
-
 ?

Synonyms

Synonyms Comment Organism
StzF
-
 Streptomyces achromogenes subsp. streptozoticus
sznF
-
 Streptomyces achromogenes subsp. streptozoticus

General Information

General Information Comment Organism
metabolism SznF catalyzes the oxidative rearrangement of a guanidine group to an N-nitrosourea in a reaction dependent on both non-haem iron and oxygen. The two metallocofactors of SznF are functionally distinct, with the central domain catalyzing two sequential N-hydroxylations of L-N-methylarginine and the cupin domain enabling oxidative rearrangement and N-N bond formation to yield the N-nitrosourea product Streptomyces achromogenes subsp. streptozoticus
physiological function sznF is involved in the biosynthesis of streptozotocin, SznF catalyzes an oxidative rearrangement of the guanidine group of Nomega-methyl-L-arginine to generate an N-nitrosourea product using two separate active sites that promote distinct steps in this transformation using different iron-containing metallocofactors. Knockout of SznF abolishes the production of streptozotocin Streptomyces achromogenes subsp. streptozoticus