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Literature summary for 2.1.1.381 extracted from

  • He, H.; Henderson, A.; Du, Y.; Ryan, K.
    Two-enzyme pathway links L-arginine to nitric oxide in N-nitroso biosynthesis (2019), J. Am. Chem. Soc., 141, 4026-4033 .
    View publication on PubMed
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KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.4
-
 L-arginine pH not specified in the publication, temperature not specified in the publication Streptomyces achromogenes subsp. streptozoticus

Organism

Organism UniProt Comment Textmining
Streptomyces achromogenes subsp. streptozoticus A0A411MRB2
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information no substrate: L-citrulline Streptomyces achromogenes subsp. streptozoticus ?
-
-
S-adenosyl-L-methionine + L-arginine
-
 Streptomyces achromogenes subsp. streptozoticus S-adenosyl-L-homocysteine + Nomega-methyl-L-arginine
-
 ?

Synonyms

Synonyms Comment Organism
stzE
-
 Streptomyces achromogenes subsp. streptozoticus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.098
-
 L-arginine pH not specified in the publication, temperature not specified in the publication Streptomyces achromogenes subsp. streptozoticus

General Information

General Information Comment Organism
physiological function free L-arginine is N-methylated by StzE to give Nomega-monomethyl-L-arginine. This product is then oxidized by StzF, a nonheme iron-dependent enzyme, generating an urea compound and NO. StzE is required for biosynthesis of streptozocin Streptomyces achromogenes subsp. streptozoticus