Revealing substrate promiscuity of 1-deoxy-D-xylulose 5-phosphate synthase

Leighanne A. Brammer; Caren Freel Meyers

doi:10.1021/ol901961q

Revealing substrate promiscuity of 1-deoxy-D-xylulose 5-phosphate synthase

Leighanne A. Brammer, Caren Freel Meyers

School of Medicine

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

31 Scopus citations

Abstract

A study of DXP synthase has revealed flexibility In the acceptor substrate binding pocket for nonpolar substrates and has uncovered new details of the catalytic mechanism to show that pyruvate can act as both donor and acceptor substrate.

Original language	English (US)
Pages (from-to)	4748-4751
Number of pages	4
Journal	Organic Letters
Volume	11
Issue number	20
DOIs	https://doi.org/10.1021/ol901961q
State	Published - Oct 15 2009

ASJC Scopus subject areas

Biochemistry
Physical and Theoretical Chemistry
Organic Chemistry

Access to Document

10.1021/ol901961q

Cite this

@article{033435b20ea64c12815daac40e584816,

title = "Revealing substrate promiscuity of 1-deoxy-D-xylulose 5-phosphate synthase",

abstract = "A study of DXP synthase has revealed flexibility In the acceptor substrate binding pocket for nonpolar substrates and has uncovered new details of the catalytic mechanism to show that pyruvate can act as both donor and acceptor substrate.",

author = "Brammer, {Leighanne A.} and Meyers, {Caren Freel}",

year = "2009",

month = oct,

day = "15",

doi = "10.1021/ol901961q",

language = "English (US)",

volume = "11",

pages = "4748--4751",

journal = "Organic Letters",

issn = "1523-7060",

publisher = "American Chemical Society",

number = "20",

}

TY - JOUR

T1 - Revealing substrate promiscuity of 1-deoxy-D-xylulose 5-phosphate synthase

AU - Brammer, Leighanne A.

AU - Meyers, Caren Freel

PY - 2009/10/15

Y1 - 2009/10/15

N2 - A study of DXP synthase has revealed flexibility In the acceptor substrate binding pocket for nonpolar substrates and has uncovered new details of the catalytic mechanism to show that pyruvate can act as both donor and acceptor substrate.

AB - A study of DXP synthase has revealed flexibility In the acceptor substrate binding pocket for nonpolar substrates and has uncovered new details of the catalytic mechanism to show that pyruvate can act as both donor and acceptor substrate.

UR - http://www.scopus.com/inward/record.url?scp=70349906430&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=70349906430&partnerID=8YFLogxK

U2 - 10.1021/ol901961q

DO - 10.1021/ol901961q

M3 - Article

C2 - 19778006

AN - SCOPUS:70349906430

SN - 1523-7060

VL - 11

SP - 4748

EP - 4751

JO - Organic Letters

JF - Organic Letters

IS - 20

ER -

Revealing substrate promiscuity of 1-deoxy-D-xylulose 5-phosphate synthase

Abstract

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this