Unknown

Dataset Information

0

An alpha-formylglycine building block for fmoc-based solid-phase peptide synthesis.


ABSTRACT: [reaction: see text] Nearly all known sulfatases share a common active site modification that is required for their activity: conversion of cysteine to alpha-formylglycine. We report the synthesis of an alpha-formylglycine building block suitable for Fmoc-based solid-phase peptide synthesis. The building block was incorporated into a synthetic peptide derived from the active site of a Mycobacterium tuberculosis sulfatase.

SUBMITTER: Rush J 

PROVIDER: S-EPMC2527029 | biostudies-literature | 2006 Jan

REPOSITORIES: biostudies-literature

altmetric image

Publications

An alpha-formylglycine building block for fmoc-based solid-phase peptide synthesis.

Rush Jason J   Bertozzi Carolyn R CR  

Organic letters 20060101 1


[reaction: see text] Nearly all known sulfatases share a common active site modification that is required for their activity: conversion of cysteine to alpha-formylglycine. We report the synthesis of an alpha-formylglycine building block suitable for Fmoc-based solid-phase peptide synthesis. The building block was incorporated into a synthetic peptide derived from the active site of a Mycobacterium tuberculosis sulfatase. ...[more]

Similar Datasets

| S-EPMC2902660 | biostudies-literature
| S-EPMC2699315 | biostudies-literature
| S-EPMC3971734 | biostudies-literature
| S-EPMC6274427 | biostudies-literature
| S-EPMC7756758 | biostudies-literature
| S-EPMC2598405 | biostudies-literature
| S-EPMC3184774 | biostudies-literature
| S-EPMC2702766 | biostudies-literature
| S-EPMC8399505 | biostudies-literature
| S-EPMC3037452 | biostudies-literature