PHOSPHOENOLPYRUVATE - CARBOHYDRATE PHOSPHOTRANSFERASE SYSTEMS OF BACTERIA

DC FieldValueLanguage
dc.contributor.authorPOSTMA, PW
dc.contributor.authorLENGELER, JW
dc.contributor.authorJACOBSON, GR
dc.date.accessioned2021-12-23T16:16:28Z-
dc.date.available2021-12-23T16:16:28Z-
dc.date.issued1993
dc.identifier.issn01460749
dc.identifier.urihttps://osnascholar.ub.uni-osnabrueck.de/handle/unios/11889-
dc.description.abstractNumerous gram-negative and gram-positive bacteria take up carbohydrates through the phosphoenolpyruvate (PEP):carbohydrate phosphotransferase system (PTS). This system transports and phosphorylates carbohydrates at the expense of PEP and is the subject of this review. The PTS consists of two general proteins, enzyme I and HPr, and a number of carbohydrate-specific enzymes, the enzymes II. PTS proteins are phosphoproteins in which the phospho group is attached to either a histidine residue or, in a number of cases, a cysteine residue. After phosphorylation of enzyme I by PEP, the phospho group is transferred to HPr. The enzymes II are required for the transport of the carbohydrates across the membrane and the transfer of the phospho group from phospho-HPr to the carbohydrates. Biochemical, structural, and molecular genetic studies have shown that the various enzymes II have the same basic structure. Each enzyme II consists of domains for specific-functions, e.g., binding of the carbohydrate or phosphorylation. Each enzyme II complex can consist of one to four different polypeptides. The enzymes II can be placed into at least four classes on the basis of sequence similarity. The genetics of the PTS is complex, and the expression of PTS proteins is intricately regulated because of the central roles of these proteins in nutrient acquisition. In addition to classical induction-repression mechanisms involving repressor and activator proteins, other types of regulation, such as antitermination, have been observed in some PTSs. Apart from their role in carbohydrate transport, PTS proteins are involved in chemotaxis toward PTS carbohydrates. Furthermore, the ILA(Glc) protein, part of the glucose-specific PTS, is a central regulatory protein which in its nonphosphorylated form can bind to and inhibit several non-PTS uptake systems and thus prevent entry of inducers. In its phosphorylated form, P-IIA(Glc) is involved in the activation of adenylate cyclase and thus in the regulation of gene expression. By sensing the presence of PTS carbohydrates in the medium and adjusting the phosphorylation state of IIA(Glc), cells can adapt quickly to changing conditions in the environment. In gram-positive bacteria, it has been demonstrated that HPr can be phosphorylated by ATP on a serine residue and this modification may perform a regulatory function.
dc.description.sponsorshipNATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCESUnited States Department of Health & Human ServicesNational Institutes of Health (NIH) - USANIH National Institute of General Medical Sciences (NIGMS) [R01GM028226] Funding Source: NIH RePORTER; NIGMS NIH HHSUnited States Department of Health & Human ServicesNational Institutes of Health (NIH) - USANIH National Institute of General Medical Sciences (NIGMS) [GM28226] Funding Source: Medline
dc.language.isoen
dc.publisherAMER SOC MICROBIOLOGY
dc.relation.ispartofMICROBIOLOGICAL REVIEWS
dc.subject3-DIMENSIONAL NMR-SPECTROSCOPY
dc.subjectADENYLATE-CYCLASE ACTIVITY
dc.subjectAMINO-ACID-SEQUENCE
dc.subjectESCHERICHIA-COLI K-12
dc.subjectGRAM-POSITIVE BACTERIA
dc.subjectHISTIDINE-CONTAINING PROTEIN
dc.subjectMicrobiology
dc.subjectNUCLEAR-MAGNETIC-RESONANCE
dc.subjectPHOSPHOCARRIER PROTEIN-HPR
dc.subjectSIGNAL-TRANSDUCING PROTEIN
dc.subjectSITE-SPECIFIC MUTAGENESIS
dc.titlePHOSPHOENOLPYRUVATE - CARBOHYDRATE PHOSPHOTRANSFERASE SYSTEMS OF BACTERIA
dc.typereview
dc.identifier.doi10.1128/MMBR.57.3.543-594.1993
dc.identifier.isiISI:A1993LW44100003
dc.description.volume57
dc.description.issue3
dc.description.startpage543
dc.description.endpage594
dc.publisher.place1752 N ST NW, WASHINGTON, DC 20036-2904 USA
dcterms.isPartOf.abbreviationMicrobiol. Rev.
dcterms.oaStatusgold
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