Biosynthesis of membrane-derived oligosaccharides: characterization of mdoB mutants defective in phosphoglycerol transferase I activity

Jackson, Brian; Bohin, Jean-Pierre; Kennedy, Eugene P.

doi:10.1128/jb.160.3.976-981.1984

Cited by 61 publications

(27 citation statements)

References 16 publications

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“…2). For two more members of the AlkP superfamily, phosphopentomutase31 and phosphoglycerol transferase,32 homologous Ser or Thr residues could not be unambiguously identified from PSI‐BLAST results, but could be tentatively predicted from secondary structure assignments.…”

Section: Resultsmentioning

confidence: 99%

Conserved core structure and active site residues in alkaline phosphatase superfamily enzymes

Galperin

Jedrzejas²

2001

Proteins

114

124

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Cofactor-independent phosphoglycerate mutase (iPGM) has been previously identified as a member of the alkaline phosphatase (AlkP) superfamily of enzymes, based on the conservation of the predicted metal-binding residues. Structural alignment of iPGM with AlkP and cerebroside sulfatase confirmed that all these enzymes have a common core structure and revealed similarly located conserved Ser (in iPGM and AlkP) or Cys (in sulfatases) residues in their active sites. In AlkP, this Ser residue is phosphorylated during catalysis, whereas in sulfatases the active site Cys residues are modified to formylglycine and sulfatated. Similarly located Thr residue forms a phosphoenzyme intermediate in one more enzyme of the AlkP superfamily, alkaline phosphodiesterase/nucleotide pyrophosphatase PC-1 (autotaxin). Using structure-based sequence alignment, we identified homologous Ser, Thr, or Cys residues in other enzymes of the AlkP superfamily, such as phosphopentomutase, phosphoglycerol transferase, phosphonoacetate hydrolase, and GPI-anchoring enzymes (glycosylphosphatidylinositol phosphoethanolamine transferases) MCD4, GPI7, and GPI13. We predict that catalytical cycles of all the enzymes of AlkP superfamily include phosphoenzyme (or sulfoenzyme) intermediates.

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Section: Resultsmentioning

confidence: 99%

Conserved core structure and active site residues in alkaline phosphatase superfamily enzymes

Galperin

Jedrzejas²

2001

Proteins

114

124

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“…Similar data were reported for the rat liver enzyme (Barsky & Hoffee, 1983). Singh and Setlow (1979a);2, Cameras et al (1982); 3, Hammer-Jespersen and Munch-Petersen (1970); 4, Henthorn et al (1992); 5, Murphy et al (1995); 6, Mansoun and Piepersberg (1991); 7, Oda et al (1993); 8, Jackson and Kennedy (1983);9, Nakashita et al (1997); 10, McGrath et ai. (1995); 11, Dotson et ai.…”

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confidence: 99%

“…MnZ+ was also shown to stim-ulate the activity of three additional members of the AP superfamily ( Fig. I ; Table I), phosphoglycerol transferase (Jackson & Kennedy, 1983), phosphonoacetate hydrolase (McGrath et al, 1995), and phosphonate monoesterase from a glyphosate-degrading bacterium (Dotson et al, 1996). Another unusual member of the AP superfamily is the Ca'+-dependent ATPase that requires two Ca atoms for activity (Desrosiers et al, 1996;Peiffer et al, 1996).…”

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confidence: 99%

A superfamily of metalloenzymes unifies phosphopentomutase and cofactor‐independent phosphoglycerate mutase with alkaline phosphatases and sulfatases

1998

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Sequence analysis of the probable archaeal phosphoglycerate mutase resulted in the identification of a superfamily of metalloenzymes with similar metal-binding sites and predicted conserved structural fold. This superfamily unites alkaline phosphatase, N-acetylgalactosamine-4-sulfatase, and cerebroside sulfatase, enzymes with known three-dimensional structures, with phosphopentomutase, 2,3-bisphosphoglycerate-independent phosphoglycerate mutase, phosphoglycerol transferase, phosphonate monoesterase, streptomycin-6-phosphate phosphatase, alkaline phosphodiesterase/nucleotide pyrophosphatase PC-1, and several closely related sulfatases. In addition to the metal-binding motifs, all these enzymes contain a set of conserved amino acid residues that are likely to be required for the enzymatic activity. Mutational changes in the vicinity of these residues in several sulfatases cause mucopolysaccharidosis (Hunter, Maroteaux-Lamy, Morquio, and Sanfilippo syndromes) and metachromatic leucodystrophy.

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“…The mdoB locus (Jackson et at., 1984;Fiedler and Rotering, 1985) encodes the phosphoglycerol transferase I, an enzyme of the cytoplasmic membrane that catalyses the in vitro transfer of phosphoglycerol residues from phosphatidylglycerol to MDO (Jackson and Kennedy, 1983). In vivo, this reaction occurs on the periplasmic side of the membrane (Bohin and Kennedy, 1984b).…”

mentioning

confidence: 99%

Homology between a genetic locus (mdoA) involved in the osmoregulated biosynthesis of periplasmic glucans in Escherichia coli and a genetic locus (hrpM) controlling pathogenicity of Pseudomonas syringae

Loubens

Debarbieux

Bohin

et al. 1993

Molecular Microbiology

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Membrane-derived oligosaccharides (MDO) of Escherichia coli are representative members of a family of glucans found in the periplasmic space of Gram-negative bacteria. The two genes forming the mdoGH operon are necessary for the synthesis of MDO. The nucleotide sequence (4759 bp) and the transcriptional start of this operon were determined. Both gene products were further characterized by gene fusion analysis. MdoG is a 56 kDa periplasmic protein whose function remains to be determined. MdoH, whose presence was shown to be necessary for normal glucosyl transferase activity, is a 97 kDa protein spanning the cytoplasmic membrane. To our surprise, these proteins are not homologous to the periplasmic glucan biosynthetic enzymes previously characterized in the Rhizobiaceae family. However, a considerable homology (69% identical nucleotides out of 2816) was discovered between mdoGH and the two genes present at the hrpM locus of the phytopathogenic bacterium Pseudomonas syringae pv. syringae. Functions of these genes remain mysterious but they are known to be required for both the expression of disease symptoms on host plants and the development of the hypersensitive reaction on non-host plants (Mills and Mukhopadhyay, 1990). These results confirm the importance of periplasmic glucans for the physiological ecology of Gram-negative bacteria.

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Biosynthesis of membrane-derived oligosaccharides: characterization of mdoB mutants defective in phosphoglycerol transferase I activity

Cited by 61 publications

References 16 publications

Conserved core structure and active site residues in alkaline phosphatase superfamily enzymes

Conserved core structure and active site residues in alkaline phosphatase superfamily enzymes

A superfamily of metalloenzymes unifies phosphopentomutase and cofactor‐independent phosphoglycerate mutase with alkaline phosphatases and sulfatases

Homology between a genetic locus (mdoA) involved in the osmoregulated biosynthesis of periplasmic glucans in Escherichia coli and a genetic locus (hrpM) controlling pathogenicity of Pseudomonas syringae

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