α-<scp>D</scp>-Glucopyranosyl-<scp>D</scp>-fructoses: distribution of furanoid and pyranoid tautomers in water, dimethyl sulphoxide, and pyridine. Studies on ketoses. Part 4

Lichtenthaler, Frieder W.; Rönninger, Stephan

doi:10.1039/p29900001489

Cited by 73 publications

(28 citation statements)

References 28 publications

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“…Complementation studies conducted by Tangney et al (6) established the PEP-PTS-catalyzed phosphorylation of maltose (4-O-␣-D-glucopyranosyl-D-glucopyranose) by cells of C. acetobutylicum grown previously on this disaccharide. Experiments in our laboratory also confirmed phospho-␣-glucosidase activity, not only in maltose-grown cells of C. acetobutylicum, but also in organisms grown previously on a variety of ␣-D-glucosides, including maltitol, methyl-␣-D-glucoside, and the five ␣-D-glucosyl-D-fructose isomers of sucrose (28,29) trivially designated: trehalulose ␣(131), turanose ␣(133), maltulose ␣(134), leucrose ␣(135), and palatinose ␣(136).…”

supporting

confidence: 55%

Genes malh and pagl of Clostridium acetobutylicum ATCC 824 Encode NAD+- and Mn2+-dependent Phospho-α-glucosidase(s)

Thompson

Hess

Pikis

2004

Journal of Biological Chemistry

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The genome of Clostridium acetobutylicum 824 contains two genes encoding NAD ؉ , Mn 2؉ , and dithiothreitol-dependent phospho-␣-glucosidases that can be assigned to family 4 of the glycosylhydrolase superfamily. The two genes, designated malh (maltose 6-phosphate hydrolase) and pagl (phospho-␣-glucosidase), respectively, reside in separate operons that also encode proteins of the phosphoenolpyruvate-dependent:sugar phosphotransferase system. C. acetobutylicum grows on a variety of ␣-linked glucosides, including maltose, methyl-␣-D-glucoside, and the five isomers of sucrose. In the presence of the requisite cofactors, extracts of these cells readily hydrolyzed the chromogenic substrate p-nitrophenyl-␣-D-glucopyranoside 6-phosphate, but whether hydrolysis reflected expression of enzymes encoded by the malh or pagl genes was not discernible by spectrophotometric analysis or polyacrylamide gel electrophoresis. Resolution of this question required the cloning of the malh and pagl genes, and subsequent high expression, purification, and characterization of maltose-6 -phosphate hydrolase (MalH) and phospho-␣-glucosidase (PagL), respectively. MalH and PagL exhibit 50% residue identity, and in solution are tetramers comprising similar sized (ϳ50 kDa) subunits. The two proteins cross-react with polyclonal rabbit antibody against phospho-␣-glucosidase from Fusobacterium mortiferum. Purified MalH and PagL cleaved p-nitrophenyl-␣-D-glucopyranoside 6-phosphate with comparable efficiency, but only MalH catalyzed the hydrolysis of disaccharide 6 -phosphates formed via the phosphoenolpyruvate-dependent:sugar phosphotransferase system. Importantly, analysis of the proteome of C. acetobutylicum 824 by electrospray ionization-mass spectrometry confirmed expression of MalH during growth on many ␣-glucosides tested. Site-directed changes C169S and D170N yielded full-length, but catalytically inactive MalH. Of the two putative operons, our findings suggest that only proteins encoded by the mal operon participate in the dissimilation of maltose and related O-␣-linked glucosides by C. acetobutylicum 824.

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supporting

confidence: 55%

Genes malh and pagl of Clostridium acetobutylicum ATCC 824 Encode NAD+- and Mn2+-dependent Phospho-α-glucosidase(s)

Thompson

Hess

Pikis

2004

Journal of Biological Chemistry

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“…Lichtenthaler and Rönninger report on a NMR method to distinguish and determine the four possible fructose tautomers (␣-pyranod, ␤-pyranoid, ␣-furanoid and ␤-furanoid, open chain is neglected) in water, pyridine and dimethyl sulphoxide [10]. This method was applied to acetone, acetone/water mixtures, methanol and acetic acid.…”

Section: Introductionmentioning

confidence: 99%

Dehydration of d-fructose to hydroxymethylfurfural in sub- and supercritical fluids

Bicker

Kaiser

Ott

et al. 2005

The Journal of Supercritical Fluids

218

169

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“…-glucose and -fructose, can be modified to yield five isomeric compounds ( Fig. 1) that trivially are designated trehalulose, turanose, maltulose, leucrose and palatinose (Lichtenthaler & Ro$ nninger, 1990 ;Lichtenthaler et al, 1991 ;Immel & Lichtenthaler, 1995). Until recently (Thompson et al, 2001a), there were no reports of the bacterial utilization of the five sucrose isomers.…”

Section: Introductionmentioning

confidence: 99%

Metabolism of sucrose and its five isomers by Fusobacterium mortiferum

et al. 2002

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Fusobacterium mortiferum utilizes sucrose [glucose-fructose in α(1 2) linkage] and its five isomeric α-D-glucosyl-D-fructoses as energy sources for growth.Sucrose-grown cells are induced for both sucrose-6-phosphate hydrolase (S6PH) and fructokinase (FK), but the two enzymes are not expressed above constitutive levels during growth on the isomeric compounds. Extracts of cells grown previously on the sucrose isomers trehalulose α(1 1), turanose α(1 3), maltulose α(1 4), leucrose α(1 5) and palatinose α(1 6) contained high levels of an NAD M plus metal-dependent phospho-α-glucosidase (MalH). The latter enzyme was not induced during growth on sucrose. MalH catalysed the hydrolysis of the 6'-phosphorylated derivatives of the five isomers to yield glucose 6-phosphate and fructose, but sucrose 6-phosphate itself was not a substrate. Unexpectedly, MalH hydrolysed both α-and β-linked stereomers of the chromogenic analogue p-nitrophenyl glucoside 6-phosphate. The gene malH is adjacent to malB and malR, which encode an EII(CB) component of the phosphoenolpyruvate-dependent sugar :phosphotransferase system and a putative regulatory protein, respectively. The authors suggest that for F. mortiferum, the products of malB and malH catalyse the phosphorylative translocation and intracellular hydrolysis of the five isomers of sucrose and of related α-linked glucosides. Genes homologous to malB and malH are present in both Klebsiella pneumoniae and the enterohaemorrhagic strain Escherichia coli O157 :H7. Both these organisms grew well on sucrose, but only K. pneumoniae exhibited growth on the isomeric compounds.

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α-D-Glucopyranosyl-D-fructoses: distribution of furanoid and pyranoid tautomers in water, dimethyl sulphoxide, and pyridine. Studies on ketoses. Part 4

Cited by 73 publications

References 28 publications

Genes malh and pagl of Clostridium acetobutylicum ATCC 824 Encode NAD+- and Mn2+-dependent Phospho-α-glucosidase(s)

Genes malh and pagl of Clostridium acetobutylicum ATCC 824 Encode NAD+- and Mn2+-dependent Phospho-α-glucosidase(s)

Dehydration of d-fructose to hydroxymethylfurfural in sub- and supercritical fluids

Metabolism of sucrose and its five isomers by Fusobacterium mortiferum

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