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Literature summary for 1.14.15.37 extracted from

  • Zocher, G.; Richter, M.; Mueller, U.; Hertweck, C.
    Structural fine-tuning of a multifunctional cytochrome P450 monooxygenase (2011), J. Am. Chem. Soc., 133, 2292-2302.
    View publication on PubMed
Search for more literature for 1.14.15.37

Crystallization (Commentary)

Crystallization (Comment) Organism
four crystal structures of AurH variants in different conformational states and in complex with the P450 inhibitor ancymidol, X-ray diffraction structure determination and analysis at 1.54 A resolution Streptomyces thioluteus

Protein Variants

Protein Variants Comment Organism
additional information modification of the chemo- and regioselectivity of AurH by site-directed mutagenesis, yielding mutants that catalyze the regioselective six-electron transfer of a nonactivated methyl group to a carboxylic acid via hydroxyl and aldehyde intermediates, overview Streptomyces thioluteus

Inhibitors

Inhibitors Comment Organism Structure
Ancymidol a P450 inhibitor, that induces conformational changes at the active site. It is primarily bound through the interaction of the pyrimidine ring system to the heme iron and to the conserved residue T247. Other interactions to the inhibitor are mediated by loose and hydrophobic contacts, mainly to residues F89, A243, L175, L290, T295 Streptomyces thioluteus

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ heme protein Streptomyces thioluteus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Streptomyces thioluteus AurH is a unique cytochrome P450 monooxygenase catalyzing the stepwise formation of a homochiral oxygen heterocycle, a key structural and pharmacophoric component of the antibiotic aureothin. The enzymatic reaction involves a tandem oxygenation process including a regio- and stereospecific hydroxylation, followed by heterocyclization, overview ?
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Organism

Organism UniProt Comment Textmining
Streptomyces thioluteus Q70KH6
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information AurH is a unique cytochrome P450 monooxygenase catalyzing the stepwise formation of a homochiral oxygen heterocycle, a key structural and pharmacophoric component of the antibiotic aureothin. The enzymatic reaction involves a tandem oxygenation process including a regio- and stereospecific hydroxylation, followed by heterocyclization, overview Streptomyces thioluteus ?
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additional information AurH catalyzes an unprecedented tandem oxygenation process. First, AurH catalyzes an asymmetric hydroxylation of deoxyaureothin, yielding (7R)-7-hydroxydeoxyaureothin as an intermediate, thus setting the absolute configuration of the final product. Second, AurH mediates another C-O bond formation that leads to O-heterocyclization. Structure-function relationship analysis by computational docking, site-directed mutagenesis, and chemical analyses, overview Streptomyces thioluteus ?
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Subunits

Subunits Comment Organism
More overall three-dimensional architecture of AurH and structure comparison, structure-function relationship analysis by computational docking, site-directed mutagenesis, and chemical analyses, overview Streptomyces thioluteus

Synonyms

Synonyms Comment Organism
AurH
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 Streptomyces thioluteus
More the enzyme belongs to the CYP151A group Streptomyces thioluteus
multifunctional cytochrome P450 monooxygenase
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 Streptomyces thioluteus

Cofactor

Cofactor Comment Organism Structure
heme
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 Streptomyces thioluteus

General Information

General Information Comment Organism
physiological function AurH is a unique cytochrome P450 monooxygenase catalyzing the stepwise formation of a homochiral oxygen heterocycle, a key structural and pharmacophoric component of the antibiotic aureothin Streptomyces thioluteus