Design and synthesis of chromogenic thiopeptolide substrates as MetAPs active site probes

Yong Mei Cui, Jing Ya Li, Ling Ling Chen, Jia Li, Qizhuang Ye, Fa Jun Nan

Research output: Contribution to journalArticle

6 Citations (Scopus)

Abstract

Twenty one chromogenic thiopeptolide substrates were designed and synthesized as the active site probes and analyzed with each S1 site of mutant residues and enzymes of wild-type MetAP1s. The preliminary enzymatic experiments indicate that cysteine 70 or 202, at either Escherichia coli or human MetAP1, played a crucial role in the methionine hydrolysis.

Original languageEnglish (US)
Pages (from-to)2853-2861
Number of pages9
JournalBioorganic and Medicinal Chemistry
Volume12
Issue number11
DOIs
StatePublished - Jun 1 2004
Externally publishedYes

Fingerprint

Chromogenic Compounds
Methionine
Escherichia coli
Cysteine
Hydrolysis
Catalytic Domain
Enzymes
Experiments

Keywords

  • Chromogenic thiopeptolide substrates
  • Methionine aminopeptidases

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Organic Chemistry
  • Drug Discovery
  • Pharmaceutical Science

Cite this

Design and synthesis of chromogenic thiopeptolide substrates as MetAPs active site probes. / Cui, Yong Mei; Li, Jing Ya; Chen, Ling Ling; Li, Jia; Ye, Qizhuang; Nan, Fa Jun.

In: Bioorganic and Medicinal Chemistry, Vol. 12, No. 11, 01.06.2004, p. 2853-2861.

Research output: Contribution to journalArticle

Cui, Yong Mei ; Li, Jing Ya ; Chen, Ling Ling ; Li, Jia ; Ye, Qizhuang ; Nan, Fa Jun. / Design and synthesis of chromogenic thiopeptolide substrates as MetAPs active site probes. In: Bioorganic and Medicinal Chemistry. 2004 ; Vol. 12, No. 11. pp. 2853-2861.
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