Evidence that the pyrromethane cofactor of hydroxymethylbilane synthase (porphobilinogen deaminase) is bound to the protein through the sulphur atom of cysteine-242-Reference-Cited by-同舟云学术

Evidence that the pyrromethane cofactor of hydroxymethylbilane synthase (porphobilinogen deaminase) is bound to the protein through the sulphur atom of cysteine-242

Published:1988-09-15 Issue:3 Volume:254 Page:915-918
ISSN:0264-6021
Container-title:Biochemical Journal
language:en
Short-container-title:

Author:

Miller A D¹,Hart G J¹,Packman L C²,Battersby A R¹

Affiliation:

1. University of Cambridge Chemical Laboratory, Lensfield Road, Cambridge CB2 1EW, U.K.

2. Department of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge CB2 IQW, U.K.

Abstract

The pyrromethane cofactor of hydroxymethylbilane synthase (porphobilinogen deaminase) from Escherichia coli is bound to the protein through the sulphur atom of a cysteine residue [Hart, Miller & Battersby (1988) Biochem. J. 252, 909-912; Beifuss, Hart, Miller & Battersby (1988) Tetrahedron Lett. 29, 2591-2594]. We show that the pyrromethane-binding residue is cysteine-242.

Publisher

Portland Press Ltd.

Subject

Cell Biology,Molecular Biology,Biochemistry

Link

https://portlandpress.com/biochemj/article-pdf/254/3/915/594486/bj2540915.pdf

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