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Journal of Bacteriology, January 2002, p. 302-306, Vol. 184, No. 1
0021-9193/01/$04.00+0     DOI: 10.1128/JB.184.1.302-306.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Utilization of L-Ascorbate by Escherichia coli K-12: Assignments of Functions to Products of the yjf-sga and yia-sgb Operons

Wen Shan Yew and John A. Gerlt*

Departments of Biochemistry and Chemistry, University of Illinois, Urbana, Illinois 61801

Received 4 April 2001/ Accepted 2 October 2001

Escherichia coli K-12 can ferment L-ascorbate. The operon encoding catabolic enzymes in the utilization of L-ascorbate (ula) has been identified; this operon of previously unknown function had been designated the yif-sga operon. Three enzymes in the pathway that produce D-xylulose 5-phosphate have been functionally characterized: 3-keto-L-gulonate 6-phosphate decarboxylase (UlaD), L-xylulose 5-phosphate 3-epimerase (UlaE), and L-ribulose 5-phosphate 4-epimerase (UlaF). Several products of the yia-sgb operon were also functionally characterized, although the substrate and physiological function of the operon remain unknown: 2,3-diketo-L-gulonate reductase (YiaK), 3-keto-L-gulonate kinase (LyxK), 3-keto-L-gulonate 6-phosphate decarboxylase (SgbH), and L-ribulose 5-phosphate 4-epimerase (SgbE).

* Corresponding author. Mailing address: Departments of Biochemistry and Chemistry, University of Illinois, 600 South Mathews Avenue, Urbana, IL 61801. Phone: (217) 333-3945. Fax: (217) 265-0385. E-mail: j-gerlt{at}uiuc.edu.

Journal of Bacteriology, January 2002, p. 302-306, Vol. 184, No. 1
0021-9193/01/$04.00+0     DOI: 10.1128/JB.184.1.302-306.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



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