Structural and mutational analysis of amino acid residues involved in ATP specificity of Escherichia coli acetate kinase.
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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.
収録刊行物
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- Journal of bioscience and bioengineering
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Journal of bioscience and bioengineering 118 (5), 502-507, 2014-05-23
Elsevier B.V.
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キーワード
- Pyrophosphate
- ATP
- Acetate kinase
- Entamoeba histolytica
- Methanosarcina thermophila
- Acetate Kinase/chemistry
- Acetate Kinase/genetics
- Acetate Kinase/isolation & purification
- Acetate Kinase/metabolism
- Adenosine Triphosphate/metabolism
- Amino Acid Sequence
- Amino Acid Substitution/genetics
- Diphosphates/metabolism
- Entamoeba histolytica/enzymology
- Escherichia coli/enzymology
- Escherichia coli/genetics
- Kinetics
- Models, Molecular
- Molecular Sequence Data
- Substrate Specificity
詳細情報 詳細情報について
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- CRID
- 1050001335813458688
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- NII論文ID
- 110009894832
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- NII書誌ID
- AA11307678
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- ISSN
- 13891723
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- HANDLE
- 2433/198558
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- NDL書誌ID
- 025932095
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- 本文言語コード
- en
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- 資料種別
- journal article
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- データソース種別
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- IRDB
- NDL
- Crossref
- CiNii Articles