1.20.1.1: phosphonate dehydrogenase
This is an abbreviated version!
For detailed information about phosphonate dehydrogenase, go to the full flat file.
Word Map on EC 1.20.1.1
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1.20.1.1
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phosphorus
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stutzeri
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hydride
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baeyer-villiger
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biotechnology
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bvmos
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phenylacetone
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d-hydroxy
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synthesis
- 1.20.1.1
- phosphorus
- stutzeri
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hydride
-
baeyer-villiger
- biotechnology
-
bvmos
- phenylacetone
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d-hydroxy
- synthesis
Reaction
Synonyms
NAD-dependent phosphite dehydrogenase, NAD:phosphite oxidoreductase, phosphite dehydrogenase, PTDH, PtxD
ECTree
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Application
Application on EC 1.20.1.1 - phosphonate dehydrogenase
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biotechnology
synthesis
additional information
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application of mutant Q137R/I150F/Q215L/R275Q/L276Q/A319E/V315A/Q132R/V71I/E130K/I313L/A325V/A176R for regeneration of NADPH in xylose reductase-catalyzed xylitol synthesis and alcohol dehydrogenase-catalyzed (R)-phenylethanol synthesis. comparison of enzyme with commercial Pseudomonas sp. formate dehydrogenase. Mutant Q137R/I150F/Q215L/R275Q/L276Q/A319E/V315A/Q132R/V71I/E130K/I313L/A325V/A176R shows higher substrate conversion and higher total turnover numbers for NADP+ than formate dehydrogenase
biotechnology
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evaluation of enzyme mutants for regeneration of reduced cofactors NADH and NADPH in industrial processes and comparison with Candida boidinii formate dehydrogenase
biotechnology
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improvement of enzyme for use in regeneration of NADH and NADPH, application in bioconversion of trimethylpyruvate to L-tert-leucine as model reaction
biotechnology
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use of enzyme mutant E175A/A176R for regeneration of NADH and NADPH. Model system converting xylose into xylitol by NADP-dependent xylose reductase and comparison of regeneration of NADPH by enzyme mutant and by Pseudomonas sp. formate dehydrogenase
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production of deuterium- or tritium-labeled substances, mutant enzymes could be applied as NADPH regeneration systems
synthesis
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production of deuterium- or tritium-labeled substances, mutant enzymes could be applied as NADPH regeneration systems
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additional information
random mutagenesis followed by comprehensive saturation mutagenesis further improves the enzyme thermostability while maintaining its activity. Mutant has improved the half-life of thermal inactivation at 45°C by 23,000fold over the parent enzyme. The engineered phosphite dehydrogenase will be useful in NAD(P)H regeneration