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Structural and mutational analysis of amino acid residues involved in ATP specificity of Escherichia coli acetate kinase

Paper ID Volume ID Publish Year Pages File Format Full-Text
20381 43172 2014 6 PDF Available
Title
Structural and mutational analysis of amino acid residues involved in ATP specificity of Escherichia coli acetate kinase
Abstract

Acetate kinase (AK) generally utilizes ATP as a phosphoryl donor, but AK from Entamoeba histolytica (PPi-ehiAK) uses pyrophosphate (PPi), not ATP, and is PPi-specific. The determinants of the phosphoryl donor specificity are unknown. Here, we inferred 5 candidate amino acid residues associated with this specificity, based on structural information. Each candidate residue in Escherichia coli ATP-specific AK (ATP-ecoAK), which is unable to use PPi, was substituted with the respective PPi-ehiAK amino acid residue. Each variant ATP-ecoAK had an increased Km for ATP, indicating that the 5 residues are the determinants for the specificity to ATP in ATP-ecoAK. Moreover, Asn-337 of ATP-ecoAK was shown to be particularly significant for the specificity to ATP. The 5 residues are highly conserved in 2625 PPi-ehiAK homologs, implying that almost all organisms have ATP-dependent, rather than PPi-dependent, AK.

Keywords
Pyrophosphate; ATP; Acetate kinase; Entamoeba histolytica; Methanosarcina thermophila
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Structural and mutational analysis of amino acid residues involved in ATP specificity of Escherichia coli acetate kinase
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Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Bioscience and Bioengineering - Volume 118, Issue 5, November 2014, Pages 502–507
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
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Price after discount Only $4.95
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Full-text PDF Download
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