Organization and Expression of the Helicobacter pylori Urease Gene Cluster

Richard L Ferrero, Agnes Labigne

Research output: Chapter in Book/Report/Conference proceedingChapter (Book)Researchpeer-review

Abstract

H. pylori produces a urease (urea amidohydrolase; E,C. 3.5.1.5) that is interesting both from a biochemical as well as a functional standpoint.//, pylori urease is a multimeric complex composed of two repeating subunits that differs from most bacterial ureases, which have three subunits.1"4 Estimates for the molecular weight of the native enzyme have varied from between 380,000 to 680,000 Da.1'2-4"6 Purified H. pylori urease subunits have the capacity to form macromolecular aggregates that stack into either pairs or fours, and this may explain the variation in molecular weight determinations,7 Evidence suggest that H. pylori urease is predominantly associated with the periplasmic or outermembrane regions of the bacterial cell and that cellular components possessing urease activity can be easily extracted from cells.1"3-7 Hence it appears that H, pylori urease differs from most bacterial ureases which have been found to be cytoplasmically located.
Original languageEnglish
Title of host publicationHelicobacter pylori Biology and Clinical Practice
EditorsC. Stewart Goodwin
Place of PublicationBoca Raton USA
PublisherCRC Press
Chapter10
Pages171-190
Number of pages20
Edition1st
ISBN (Print)9781351081610
Publication statusPublished - 1993
Externally publishedYes

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