Enzymatic properties, renaturation and metabolic role of mannitol-1-phosphate dehydrogenase from Escherichia coli

Teschner, Wolfgang; Serre, Marie-Claude; Garel, Jean‐Renaud

doi:10.1016/0300-9084(90)90170-l

Cited by 21 publications

(22 citation statements)

References 24 publications

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“…The M1PDH from Escherichia coli is also a monomer in solution and like the fungal enzymes, it has a higher affinity for NADH than for NAD + at neutral pH. 13 It prefers NAD + more than 100-fold over NADP + , and its activity appeared to be independent of a metal cofactor. 14 Results are based on processing 2 g moist bacterial biomass.…”

Section: Purification and Molecular And Kinetic Characterization Of mentioning

confidence: 99%

Characterization of recombinant Aspergillus fumigatus mannitol-1-phosphate 5-dehydrogenase and its application for the stereoselective synthesis of protio and deuterio forms of d-mannitol 1-phosphate

Krahulec

Armao

Weber

et al. 2008

Carbohydrate Research

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Section: Purification and Molecular And Kinetic Characterization Of mentioning

confidence: 99%

Characterization of recombinant Aspergillus fumigatus mannitol-1-phosphate 5-dehydrogenase and its application for the stereoselective synthesis of protio and deuterio forms of d-mannitol 1-phosphate

Krahulec

Armao

Weber

et al. 2008

Carbohydrate Research

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“…m Brown and Bowles (1977). n Teschner et al (1990). o One catalytic protein and two 35-kD 14-3-3 proteins.…”

Section: Purification Of M1pdhmentioning

confidence: 99%

“…However, M1PDH in bacteria usually functions for degradation and not for accumulation in vivo, and mannitol absorbed from the medium is catabolized to F6P via M1P for use as a carbon and energy source by a specific phosphotransferase system. Thus, bacterial M1PDH and the mannitol-catabolizing process are thought not to be affected by a salinity change (Teschner et al, 1990). Although the regulation of mannitol accumulation in plants is well documented (Stoop et al, 1996;Loescher and Everard, 2000), the regulation of mannitol metabolism in algae is less defined.…”

mentioning

confidence: 99%

Characterization of Salt-Regulated Mannitol-1-Phosphate Dehydrogenase in the Red Alga Caloglossa continua

2003

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Mannitol-1-phosphate (M1P) dehydrogenase (M1PDH; EC 1.1.1.17), an enzyme catalyzing the reduction of Fru-6-phosphate (F6P) to M1P in algal mannitol biosynthesis, was purified to homogeneity from a cell homogenate of the eulittoral red alga Caloglossa continua (Okamura) King et Puttock. The enzyme was a monomer with an apparent molecular mass of 53 kD, as determined by gel filtration and SDS-PAGE, and exhibited an pI of approximately 5.5. The substrate specificity was very high toward F6P and M1P for respective reductive and oxidative reactions. The enzyme was found to be a sulfhydryl-type, because its activity was inhibited by N-ethylmaleimide and p-hydroxymercuribenzoate, and the inhibition by p-hydroxymercuribenzoate was rescued by 2-mercaptoethanol. Some unknown factors in the extract may also have inhibited the activity, because the total activity was greatly increased through the purification procedure. The optimum pH for F6P reduction was changed from 6.0 or lower to 7.2 by the addition of 200 mm NaCl. The reduction of F6P showed strong substrate inhibition above 0.5 mm. However, K m (F6P) of M1PDH was increased eight times by the addition of 200 mm NaCl, whereas V max was in a similar range with the avoidance of substrate inhibition by F6P. These results indicate that the enzyme was finely and directly regulated by the salt concentration without the requirement for gene expression. M1PDH can therefore be a key enzyme for regulating mannitol biosynthesis when the alga is stressed by a salinity change.

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“…The M6PR functions primarily in a synthetic manner, with only very low rates of mannitol-1-P oxidation observed . M6PR is distinctly different from mannitol-metabolizing enzymes in lower organisms, a11 of which can be characterized as 2-oxidoreductases, catalyzing the interconversion of Fru or Fru-6-P to mannitol or mannitol-1-P (Martinez et al, 1963;Ueng et al, 1976;Niehaus and Dilts, 1982;Morton et al, 1985;Teschner et al, 1990). Many of the mannitol dehydrogenases in lower organisms can function in both directions, e.g.…”

mentioning

confidence: 99%

Effect of Different Carbon Sources on Relative Growth Rate, Internal Carbohydrates, and Mannitol 1-Oxidoreductase Activity in Celery Suspension Cultures

Stoop

Pharr

1993

Plant Physiol.

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Enzymatic properties, renaturation and metabolic role of mannitol-1-phosphate dehydrogenase from Escherichia coli

Cited by 21 publications

References 24 publications

Characterization of recombinant Aspergillus fumigatus mannitol-1-phosphate 5-dehydrogenase and its application for the stereoselective synthesis of protio and deuterio forms of d-mannitol 1-phosphate

Characterization of recombinant Aspergillus fumigatus mannitol-1-phosphate 5-dehydrogenase and its application for the stereoselective synthesis of protio and deuterio forms of d-mannitol 1-phosphate

Characterization of Salt-Regulated Mannitol-1-Phosphate Dehydrogenase in the Red Alga Caloglossa continua

Effect of Different Carbon Sources on Relative Growth Rate, Internal Carbohydrates, and Mannitol 1-Oxidoreductase Activity in Celery Suspension Cultures

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