Enzymic conversion of deuterated analogues of δ-l-α-aminoadipoyl-l-cysteinyl-d-allylglycine, an unnatural substrate for isopenicilin n synthase: A unified theory of second ring closure.

Jack E. Baldwin; Mar K. Bradley; Nicholas J. Turner; Robert M. Adlington; Andrew R. Pitt; Andrew E. Derome

doi:10.1016/S0040-4020(01)91016-6

Enzymic conversion of deuterated analogues of δ-l-α-aminoadipoyl-l-cysteinyl-d-allylglycine, an unnatural substrate for isopenicilin n synthase: A unified theory of second ring closure.

Jack E. Baldwin^*, Mar K. Bradley, Nicholas J. Turner, Robert M. Adlington, Andrew R. Pitt, Andrew E. Derome

^*Corresponding author for this work

Oxford University

Research output: Contribution to journal › Article › peer-review

Abstract

The enzyme Isopenicillin N Synthase catalyses the conversion of the modified substrate δ-L-α-aminoadipoyl-L-cysteinyl-D-all to six β-lactam containing metabotites. Eight tripeptides deuterated in the allylglycine moiety have been prepared and the stereochemical course of their cyclization to the β-lactam containing metabolites has been investigated.

Original language	English
Pages (from-to)	8223-8242
Number of pages	20
Journal	Tetrahedron
Volume	47
Issue number	38
DOIs	https://doi.org/10.1016/S0040-4020(01)91016-6
Publication status	Published - 16 Sept 1991

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10.1016/S0040-4020(01)91016-6

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@article{f3e216a50076411496d5b7c12288662d,

title = "Enzymic conversion of deuterated analogues of δ-l-α-aminoadipoyl-l-cysteinyl-d-allylglycine, an unnatural substrate for isopenicilin n synthase: A unified theory of second ring closure.",

abstract = "The enzyme Isopenicillin N Synthase catalyses the conversion of the modified substrate δ-L-α-aminoadipoyl-L-cysteinyl-D-all to six β-lactam containing metabotites. Eight tripeptides deuterated in the allylglycine moiety have been prepared and the stereochemical course of their cyclization to the β-lactam containing metabolites has been investigated.",

author = "Baldwin, \{Jack E.\} and Bradley, \{Mar K.\} and Turner, \{Nicholas J.\} and Adlington, \{Robert M.\} and Pitt, \{Andrew R.\} and Derome, \{Andrew E.\}",

year = "1991",

month = sep,

day = "16",

doi = "10.1016/S0040-4020(01)91016-6",

language = "English",

volume = "47",

pages = "8223--8242",

journal = "Tetrahedron",

issn = "0040-4020",

publisher = "Elsevier BV",

number = "38",

}

Enzymic conversion of deuterated analogues of δ-l-α-aminoadipoyl-l-cysteinyl-d-allylglycine, an unnatural substrate for isopenicilin n synthase: A unified theory of second ring closure. / Baldwin, Jack E.; Bradley, Mar K.; Turner, Nicholas J. et al.
In: Tetrahedron, Vol. 47, No. 38, 16.09.1991, p. 8223-8242.

Research output: Contribution to journal › Article › peer-review

TY - JOUR

T1 - Enzymic conversion of deuterated analogues of δ-l-α-aminoadipoyl-l-cysteinyl-d-allylglycine, an unnatural substrate for isopenicilin n synthase

T2 - A unified theory of second ring closure.

AU - Baldwin, Jack E.

AU - Bradley, Mar K.

AU - Turner, Nicholas J.

AU - Adlington, Robert M.

AU - Pitt, Andrew R.

AU - Derome, Andrew E.

PY - 1991/9/16

Y1 - 1991/9/16

N2 - The enzyme Isopenicillin N Synthase catalyses the conversion of the modified substrate δ-L-α-aminoadipoyl-L-cysteinyl-D-all to six β-lactam containing metabotites. Eight tripeptides deuterated in the allylglycine moiety have been prepared and the stereochemical course of their cyclization to the β-lactam containing metabolites has been investigated.

AB - The enzyme Isopenicillin N Synthase catalyses the conversion of the modified substrate δ-L-α-aminoadipoyl-L-cysteinyl-D-all to six β-lactam containing metabotites. Eight tripeptides deuterated in the allylglycine moiety have been prepared and the stereochemical course of their cyclization to the β-lactam containing metabolites has been investigated.

UR - https://www.scopus.com/pages/publications/0025994422

U2 - 10.1016/S0040-4020(01)91016-6

DO - 10.1016/S0040-4020(01)91016-6

M3 - Article

AN - SCOPUS:0025994422

SN - 0040-4020

VL - 47

SP - 8223

EP - 8242

JO - Tetrahedron

JF - Tetrahedron

IS - 38

ER -

Enzymic conversion of deuterated analogues of δ-l-α-aminoadipoyl-l-cysteinyl-d-allylglycine, an unnatural substrate for isopenicilin n synthase: A unified theory of second ring closure.

Abstract

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