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J. Biol. Chem., Vol. 279, Issue 13, 12479-12483, March 26, 2004

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Histidine 167 Is the Phosphate Acceptor in Glucose-6-phosphatase- Forming a Phosphohistidine Enzyme Intermediate during Catalysis^*

Abhijit Ghosh, Jeng-Jer Shieh, Chi-Jiunn Pan, and Janice Yang Chou

From the Section on Cellular Differentiation, Heritable Disorders Branch, NICHD, National Institutes of Health, Bethesda, Maryland 20892

The glucose-6-phosphatase (Glc-6-Pase) family comprises two active endoplasmic reticulum (ER)-associated isozymes: the liver/kidney/intestine Glc-6-Pase- and the ubiquitous Glc-6-Pase-. Both share similar kinetic properties. Sequence alignments predict the two proteins are structurally similar. During glucose 6-phosphate (Glc-6-P) hydrolysis, Glc-6-Pase-, a nine-transmembrane domain protein, forms a covalently bound phosphoryl enzyme intermediate through His¹⁷⁶, which lies on the lumenal side of the ER membrane. We showed that Glc-6-Pase- is also a nine-transmembrane domain protein that forms a covalently bound phosphoryl enzyme intermediate during Glc-6-P hydrolysis. However, the intermediate was not detectable in Glc-6-Pase- active site mutants R79A, H114A, and H167A. Using [³²P]Glc-6-P coupled with cyanogen bromide mapping, we demonstrated that the phosphate acceptor in Glc-6-Pase- is His¹⁶⁷ and that it lies inside the ER lumen with the active site residues, Arg⁷⁹ and His¹¹⁴. Therefore Glc-6-Pase- and Glc-6-Pase- share a similar active site structure, topology, and mechanism of action.

Received for publication, December 4, 2003 , and in revised form, January 12, 2004.

^* The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

These two authors contributed equally to this work.

To whom correspondence should be addressed: Bldg. 10, Rm. 9S241, National Institutes of Health, Bethesda, MD 20892-1830. Tel.: 301-496-1094; Fax: 301-402-6035; E-mail: chouja{at}mail.nih.gov.

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