Stereochemical course of the reactions catalyzed by the bacterial phosphoenolpyruvate: Mannitol phosphotransferase system

Journal Article · Tue Jul 24 00:00:00 EDT 1990 · Biochemistry; (USA)

DOI:https://doi.org/10.1021/bi00481a019· OSTI ID:6000902

Mueller, E G; Knowles, J R ^[1]; Khandekar, S S; Jacobson, G R ^[2]

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1. Harvard Univ., Cambridge, MA (USA)
2. Boston Univ., MA (USA)

The authors have determined the overall stereochemical course of the reactions leading to the phosphorylation of D-mannitol by mannitol-specific enzyme II (EII{sup Mtl}) of the Escherichia coli phosphoenolpyruvate- (PEP) dependent phosphotransferase system (PTS). In the presence of enzyme I and HPr of the PTS, and of membranes containing EII{sup Mtl}, the phospho group from ((R)-{sup 16}O, {sup 17}O, {sup 18}O)PEP was transferred to D-mannitol to form mannitol 1-phosphate with overall inversion of the configuration at phosphorus with respect to that of PEP. Since in the course of these reactions enzyme I and HPr are each covalently phosphorylated at a single site and inversion of the chiral phospho group from PEP indicates an odd number of transfer steps overall, transfer from phospho-HPr to mannitol via EII{sup Mtl} must also occur in an odd number of steps. Taken together with the fact that catalytically important phospho-EII{sup Mtl} intermediates have been demonstrated biochemically, the results imply that EII{sup Mtl} is sequentially phosphorylated at two different sites during phospho transfer from phospho-HPr to mannitol. This conclusion is consistent with the available evidence on phospho-EII{sup Mtl} intermediates and in particular with the recent report that two different phospho peptides can be isolated from the fully phosphorylated protein.

• OSTI ID: 6000902
• Journal Information: Biochemistry; (USA), Journal Name: Biochemistry; (USA) Vol. 29:29; ISSN 0006-2960; ISSN BICHA
• Country of Publication: United States
• Language: English

Related Subjects

550201* -- Biochemistry-- Tracer Techniques
59 BASIC BIOLOGICAL SCIENCES
ALDEHYDES
BACTERIA
BIOCHEMICAL REACTION KINETICS
CARBOHYDRATES
CHEMICAL REACTIONS
ENZYMES
ESCHERICHIA COLI
EVEN-EVEN NUCLEI
EVEN-ODD NUCLEI
GLUCOSE
HEXOSES
ISOTOPE APPLICATIONS
ISOTOPES
KINETICS
LIGHT NUCLEI
MANNOSE
MICROORGANISMS
MONOSACCHARIDES
NMR SPECTRA
NUCLEI
ODD-EVEN NUCLEI
ORGANIC COMPOUNDS
OXYGEN 16
OXYGEN 17
OXYGEN 18
OXYGEN ISOTOPES
PHOSPHOENOLPYRUVATE
PHOSPHORUS 31
PHOSPHORUS ISOTOPES
PHOSPHORUS-GROUP TRANSFERASES
PHOSPHORYLATION
PHOSPHOTRANSFERASES
PROTEIN STRUCTURE
REACTION INTERMEDIATES
REACTION KINETICS
SACCHARIDES
SALMONELLA
SALMONELLA TYPHIMURIUM
SPECTRA
STABLE ISOTOPES
STEREOCHEMISTRY
TRACER TECHNIQUES
TRANSFERASES