Cloning, expression, and characterization of acetate kinase from Lactobacillus sanfranciscensis

Ruth Knorr, Matthias A. Ehrmann, Rudi F. Vogel

Research output: Contribution to journalArticlepeer-review

16 Scopus citations

Abstract

In the metabolism of Lactobacillus sanfranciscensis, the acetate kinase (AK) is a key enzyme and responsible for dephosphorylation of acetyl phosphate with the concomitant production of acetate and ATP. The L. sanfranciscensis ack gene was identified by PCR methods. It encodes a 397 amino acid protein sharing 56% similarity with Bacillus subtilis AK. Whereas cotranscription of ack and pta (phosphotrans acetylase) is reported in previously characterised organisms, the L. sanfranciscensis ack gene is not located in direct neighbourhood to the encoding gene. AK was heterologously expressed in E. coli and characterised by its Vmax and Km values and by the dependence of enzyme activity on temperature and pH. Based on this data the in vivo role of the enzyme is discussed.

Original languageEnglish
Pages (from-to)267-277
Number of pages11
JournalMicrobiological Research
Volume156
Issue number3
DOIs
StatePublished - 2001
Externally publishedYes

Keywords

  • Acetate kinase
  • Lactobacillus sanfranciscensis

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