Isopenicillin N synthase binds δ-(L-α-aminoadipoyl)-L-cysteinyl-D-thia-allo-isoleucine through both sulfur atoms.
Isopenicillin N synthase (IPNS) catalyses the synthesis of isopenicillin N (IPN), the biosynthetic precursor to penicillin and cephalosporin antibiotics. IPNS is a non-heme iron(II) oxidase that mediates the oxidative cyclisation of the tripeptide δ-L-α-aminoadipoyl-L-cysteinyl-D-valine (ACV) to IPN...
Үндсэн зохиолчид: | Clifton, I, Ge, W, Adlington, R, Baldwin, J, Rutledge, P |
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Формат: | Journal article |
Хэл сонгох: | English |
Хэвлэсэн: |
2011
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The crystal structure of isopenicillin N synthase with δ-((L)-α-aminoadipoyl)-(L)-cysteinyl-(D)-methionine reveals thioether coordination to iron.
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Structural studies on the reaction of isopenicillin N synthase with the truncated substrate analogues delta-(L-alpha-aminoadipoyl)-L-cysteinyl-glycine and delta-(L-alpha-aminoadipoyl)-L-cysteinyl-D-alanine.
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Structural studies on the reaction of isopenicillin N synthase with the substrate analogue delta-(l-alpha-aminoadipoyl)-l-cysteinyl-d-alpha-aminobutyrate.
-н: Long, A, зэрэг
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AN EFFICIENT SUBSTITUTE FOR THE ALPHA-AMINOADIPOYL MOIETY OF DELTA-(L-ALPHA-AMINOADIPOYL)-L-CYSTEINYL-D-VALINE IN THE ENZYMATIC-SYNTHESIS OF PENICILLINS
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