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J Bacteriol. 1988 April; 170(4): 1926-1933

research-article

Phosphoglycerate kinase gene from Zymomonas mobilis: cloning, sequencing, and localization within the gap operon.

T Conway and L O Ingram

Department of Microbiology and Cell Science, University of Florida, Gainesville 32611.

ABSTRACT

The Zymomonas mobilis gene encoding phosphoglycerate kinase (EC 2.7.3.2), pgk, has been cloned into Escherichia coli and sequenced. It consists of 336 amino acids, including the N-terminal methionine, with a molecular weight of 41,384. This promoterless gene is located 225 base pairs downstream from the gap gene and is part of the gap operon. Previous studies have shown that the specific activities of glyceraldehyde-3-phosphate dehydrogenase and phosphoglycerate kinase do not change coordinately in Z. mobilis, although the two enzymes appear to be under the control of a common promoter. The translated amino acid sequence for the Z. mobilis phosphoglycerate kinase is less conserved than those of eucaryotic genes. A comparison of known sequences for phosphoglycerate kinase revealed a high degree of conservation of structure with 102 amino acid positions being retained by all. In general, the amino acid positions at the boundaries of beta-sheet and alpha-helical regions and those connecting these regions were more highly conserved than the amino acid positions within regions of secondary structure.

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J Bacteriol. 1988 April; 170(4): 1926-1933

This article has been cited by other articles:

• Charpentier, B., Bardey, V., Robas, N., Branlant, C. (1998). The EIIGlc Protein Is Involved in Glucose-Mediated Activation of Escherichia coli gapA and gapB-pgk Transcription. J. Bacteriol. 180: 6476-6483 [Abstract] [Full Text]  
• Walla, O., de Groot, E., Schweiger, M (1994). On the molecular mechanism of the circadian clock. The 41,000 M(r) clock protein of Chlorella was identified as 3-phosphoglycerate kinase. J. Cell Sci. 107: 719-726 [Abstract]