ThegndGene Encoding a Novel 6-Phosphogluconate Dehydrogenase and Its Adjacent Region ofActinobacillus actinomycetemcomitansChromosomal DNA

Yamaguchi, Yasuo; Nakano, Yoshio; Yamashita, Yoshihisa; Kinoshita, Toshihiko

doi:10.1006/bbrc.1996.5917

Cited by 8 publications

(5 citation statements)

References 24 publications

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“…ESTs homologous to the protein encoded by the devB gene of Actinobacillus actinomycetemcomitans (D88189, [8]) were searched with the tblastn function of the BLAST 2.0 program [9,10]. Multiple sequence alignments were made using the PILEUP program of the GCG package (Wisconsin Package version 10.0, Genetics Computer Group, Madison, WI, USA).…”

Section: Methodsmentioning

confidence: 99%

Identification of the cDNA encoding human 6‐phosphogluconolactonase, the enzyme catalyzing the second step of the pentose phosphate pathway

et al. 1999

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We report the sequence of a human cDNA encoding a protein homologous to devB (a bacterial gene often found in proximity to the gene encoding glucose-6-phosphate dehydrogenase in bacterial genomes) and to the C-terminal part of human hexose-6-phosphate dehydrogenase. The protein was expressed in Escherichia coli, purified and shown to be 6-phosphogluconolactonase, the enzyme catalyzing the second step of the pentose phosphate pathway. Sequence analysis indicates that bacterial devB proteins, the C-terminal part of hexose-6-phosphate dehydrogenase and yeast Sol1^4 proteins are most likely also 6-phosphogluconolactonases and that these proteins are related to glucosamine-6-phosphate isomerases.z 1999 Federation of European Biochemical Societies.

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Section: Methodsmentioning

confidence: 99%

Identification of the cDNA encoding human 6‐phosphogluconolactonase, the enzyme catalyzing the second step of the pentose phosphate pathway

et al. 1999

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“…phaseoli [8]. The PssB of R. leguminosarum showed also a moderate homology (41.2% identity) to the CysQ (AmtA) protein from E. coli [25], CysQ (30.5% identity) from Actinobacillus actinomycetemcomitans [26], SuhB (26.2% identity) from E. coli [27] and 25% identity to a family of plant [28] and mammalian inositol monophosphatases (IMP) [29]. IMP hydrolyses the ester bond of myo-inositol 1 (or 4)-phosphate to release myo-inositol and P i and it plays a key role in the biosynthesis of inositol phosphates and inositolphospholipids that are involved in signal transduction in mammalian and plant cells [30].…”

Section: Resultsmentioning

confidence: 96%

The pssB gene product of Rhizobium leguminosarum bv. trifolii is homologous to a family of inositol monophosphatases

Janczarek

1999

FEMS Microbiology Letters

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The Rhizobium leguminosarum bv. trifolii region encoding pssA and pssB genes was cloned. The pssB gene located upstream of the pssA encoded a 28.36-kDa protein which displayed 97.5% identity with the PssB of R. leguminosarum bv. viciae. Inactivation of the pssB gene by insertion of the lacZ-Gm r cassette resulted in the significant increased production of exopolysaccharide in comparison to the wild-type level. A mutant strain was also defective in nitrogen fixation suggesting a regulatory role of pssB in symbiosis with clover. z

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“…phaseoli [8]. The PssB of R. leguminosarum showed also a moderate homology (41.2% identity) to the CysQ (AmtA) protein from E. coli [25], CysQ (30.5% identity) from Actinobacillus actinomycetemcomitans [26], SuhB (26.2% identity) from E. coli [27] and 25% identity to a family of plant [28] and mammalian inositol monophosphatases (IMP) [29]. IMP hydrolyses the ester bond of myo‐inositol 1 (or 4)‐phosphate to release myo‐inositol and P i and it plays a key role in the biosynthesis of inositol phosphates and inositolphospholipids that are involved in signal transduction in mammalian and plant cells [30].…”

Section: Resultsmentioning

confidence: 96%

ThepssBgene product ofRhizobium leguminosarumbv.trifoliiis homologous to a family of inositol monophosphatases

Janczarek

Król

Skorupska

1999

FEMS Microbiology Letters

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The Rhizobium leguminosarum bv. trifolii region encoding pssA and pssB genes was cloned. The pssB gene located upstream of the pssA encoded a 28.36-kDa protein which displayed 97.5% identity with the PssB of R. leguminosarum bv. viciae. Inactivation of the pssB gene by insertion of the lacZ-Gmr cassette resulted in the significant increased production of exopolysaccharide in comparison to the wild-type level. A mutant strain was also defective in nitrogen fixation suggesting a regulatory role of pssB in symbiosis with clover.

show abstract

ThegndGene Encoding a Novel 6-Phosphogluconate Dehydrogenase and Its Adjacent Region ofActinobacillus actinomycetemcomitansChromosomal DNA

Cited by 8 publications

References 24 publications

Identification of the cDNA encoding human 6‐phosphogluconolactonase, the enzyme catalyzing the second step of the pentose phosphate pathway

Identification of the cDNA encoding human 6‐phosphogluconolactonase, the enzyme catalyzing the second step of the pentose phosphate pathway

The pssB gene product of Rhizobium leguminosarum bv. trifolii is homologous to a family of inositol monophosphatases

ThepssBgene product ofRhizobium leguminosarumbv.trifoliiis homologous to a family of inositol monophosphatases

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