174908-78-2Relevant articles and documents
Evidence for an insertion-homolysis mechanism for carbon-sulphur bond formation in penicillin biosynthesis; 1. Synthesis of tripeptide probes
Baldwin, Jack E.,Adlington, Robert M.,Marquess, Daniel G.,Pitt, Andrew R.,Porter, Michael J.,Russell, Andrew T.
, p. 2515 - 2536 (1996)
Synthesis of four LLD-ACV analogues, in which the valine residue has been replaced by an amino acid containing a stereospecifically deuterated cyclopropane ring, is described.
Stereochemical course of the conversion of α-ketoisocaproate to β-hydroxyisovalerate by soluble, recombinant mammalian 4-hydroxyphenylpyruvate dioxygenase
Crouch, Nicholas P.,Adlington, Robert M.,Baldwin, Jack E.,Lee, Meng-Huee,MacKinnon, Colin H.,Paul, Diana R.
, p. 10827 - 10840 (2007/10/03)
The stereochemical course of the conversion of α-ketoisocaproate to β-hydroxyisovalerate catalysed by the enzyme 4-hydroxyphenylpyruvate dioxygenase is described.
Stereochemistry of hydroxylation during the conversion of α-ketoisocaproate to β-hydroxyisovalerate by 4-hydroxyphenylpyruvate dioxygenase
Adlington, Robert M.,Baldwin, Jack E.,Crouch, Nicholas P.,Lee, Meng-Huee,MacKinnon, Colin H.,Paul, Diana R.
, p. 2721 - 2724 (2007/10/03)
4-Hydroxyphenylpyruvate dioxygenase catalyzes the oxidative decarboxylation and hydroxylation of α-ketoisocaproate 1 to β-hydroxyisovalerate 2 with retention of configuration during the hydroxylation step.