Specific biotinylation of IMP dehydrogenase

B. Christopher Hoefler; Deviprasad R Gollapalli; Lizbeth Hedstrom

doi:10.1016/j.bmcl.2011.01.042

Back

Specific biotinylation of IMP dehydrogenase

Journal article

Open access

Peer reviewed

Specific biotinylation of IMP dehydrogenase

B. Christopher Hoefler, Deviprasad R Gollapalli and Lizbeth Hedstrom

Bioorganic & Medicinal Chemistry Letters, Vol.21(5), pp.1363-1365

03/01/2011

DOI: https://doi.org/10.1016/j.bmcl.2011.01.042

PMCID: PMC3044611

PMID: 21295473

Abstract

IMPDH

Biotin probe

Enzyme inhibitors

6-Cl-purine ribotide

Nucleotide biosynthesis

Mechanism-based probe

Biochemistry

IMP dehydrogenase (IMPDH) catalyzes a critical step in guanine nucleotide biosynthesis. IMPDH also has biological roles that are distinct from its enzymatic function. We report a biotin-linked reagent that selectively labels IMPDH and is released by dithiothreitol. This reagent will be invaluable in elucidating the moonlighting functions of IMPDH.

Files and links (1)

url

Specific biotinylation of IMP dehydrogenaseView

Published (Version of record) Open

Metrics

28 Record Views

Details

Title: Specific biotinylation of IMP dehydrogenase
Creators: B. Christopher Hoefler (Author) - Graduate Program in Biochemistry, Brandeis University, MS 009, 415 South St., Waltham, MA 02454, USA
Deviprasad R Gollapalli (Author) - Department of Biology, Brandeis University, MS 009, 415 South St., Waltham, MA 02454, USA
Lizbeth Hedstrom (Author) - Department of Biology, Brandeis University, MS 009, 415 South St., Waltham, MA 02454, USA
Publication Details: Bioorganic & Medicinal Chemistry Letters, Vol.21(5), pp.1363-1365
Publisher: Elsevier Ltd
Identifiers: 9923957836201921
Academic Unit: Department of Chemistry; Department of Biology
Language: English
Resource Type: Journal article

Specific biotinylation of IMP dehydrogenase

Abstract

Files and links (1)

Metrics

Details

Brandeis University Social media