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References from COFACTOR SPECIFICITY ENGINEERING OF STREPTOCOCCUS MUTANS NADH OXIDASE 2 FOR NAD(P) + REGENERATION IN BIOCATALYTIC OXIDATIONS. Local targets link to admitted publications; unresolved targets remain external evidence.
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10.1007/s00253-012-4142-9 · External reference
Efficient regeneration of NADPH using an engineered phosphite dehydrogenase
10.1002/bit.21168 · 2007 · External reference
Relaxing the nicotinamide cofactor specificity of phosphite dehydrogenase by rational design
10.1021/bi035018b · 2003 · External reference
Enzymatic vs. fermentative synthesis: Thermostable glucose dehydrogenase catalyzed regeneration of NAD(P)H for use in enzymatic synthesis
10.1021/ja00299a044 · 1985 · External reference
Guidelines for the application of NAD(P)H regenerating glucose dehydrogenase in synthetic processes
10.1002/adsc.201200959 · 2013 · External reference
Cofactor regeneration at the lab scale
2005 · External reference
Recent advances in cofactor regeneration systems applied to biocatalyzed oxidative processes
10.2174/138527212804004643 · 2012 · External reference
10.1021/jo802350f
10.1021/jo802350f · External reference
Enzymatic preparation of 12-ketochenodeoxycholic acid with NADP regeneration
10.1002/bit.260260526 · 1984 · External reference
Preparation of optically active 1,2-diols and α-hydroxy ketones using glycerol dehydrogenase as catalyst: Limits to enzyme-catalyzed synthesis due to noncompetitive and mixed inhibition by product
10.1021/jo00351a005 · 1986 · External reference
A single-point mutation enables lactate dehydrogenase from Bacillus subtilis to utilize NAD+ and NADP+ as cofactor
10.1002/elsc.201000151 · 2011 · External reference
10.1021/ol800549f
10.1021/ol800549f · External reference
In vitro double oxidation of n-heptane with direct cofactor regeneration
10.1002/adsc.201300143 · 2013 · External reference
10.1002/anie.201204683
10.1002/anie.201204683 · External reference
Novel chemo-enzymatic mimic of hydrogen peroxide-forming NAD(P)H oxidase for efficient regeneration of NAD+ and NADP+
10.1002/adsc.200800357 · 2008 · External reference
A new regeneration system for oxidized nicotinamide cofactors
10.1002/adsc.200900033 · 2009 · External reference
Exploitation of a laccase/meldola's blue system for NAD+ regeneration in preparative scale hydroxysteroid dehydrogenase-catalyzed oxidations
10.1002/adsc.201200429 · 2012 · External reference
Expanding the scope of laccase-mediator systems
2013 · External reference
10.1016/j.molcatb.2013.07.006
10.1016/j.molcatb.2013.07.006 · External reference
Electroenzymatic synthesis
10.1016/j.molcatb.2007.10.001 · 2008 · External reference
Biocatalytic redox reactions for organic synthesis: Nonconventional regeneration methods
2010 · External reference
Non-enzymatic regeneration of nicotinamide and flavin cofactors for monooxygenase catalysis
10.1016/j.tibtech.2006.02.003 · 2006 · External reference
The streptococcal flavoprotein NADH oxidase. I. Evidence linking NADH oxidase and NADH peroxidase cysteinyl redox centers
1989 · External reference
The streptococcal flavoprotein NADH oxidase. II. Interactions of pyridine nucleotides with reduced and oxidized enzyme forms
1989 · External reference
Molecular cloning and sequence analysis of the gene encoding the H2O-forming NADH oxidase from Streptococcus mutans
10.1271/bbb.60.39 · 1996 · External reference
The reduced diphosphopyridine nucleotide oxidase of Streptococcus faecalis: purification and properties
10.1016/s0021-9258(19)73802-2 · 1962 · External reference
Characterization of H2O-forming NADH oxidase from Streptococcus pyogenes and its application in l-rare sugar production
10.1016/j.bmcl.2012.01.049 · 2012 · External reference
10.1099/00221287-147-2-431
10.1099/00221287-147-2-431 · External reference
Isolation and biochemical characterization of a new NADH oxidase from Lactobacillus brevis
10.1023/a:1021730131633 · 2003 · External reference
Purification and characterisation of the water forming NADH-oxidase from Lactococcus lactis
10.1016/s0958-6946(01)00031-0 · 2001 · External reference
NAD(P)H oxidase v from Lactobacillus plantarum (NoxV) displays enhanced operational stability even in absence of reducing agents
10.1016/j.molcatb.2011.04.013 · 2011 · External reference
10.1002/1615-4169(200212)344:10<1156::aid-adsc1156>3.0.co;2-#
10.1002/1615-4169(200212)344:10<1156::aid-adsc1156>3.0.co;2-# · External reference
Purification and characterization of an H2O-forming NADH oxidase from Clostridium aminovalericum: Existence of an oxygen-detoxifying enzyme in an obligate anaerobic bacteria
10.1007/s00203-004-0659-3 · 2004 · External reference
10.1006/anae.1999.0196
10.1006/anae.1999.0196 · External reference
Comparison of H2O-forming NADH oxidase from Leuconostoc mesenteroides subsp. mesenteroides NRIC 1541(T) and H2O2-forming NADH oxidase from Sporolactobacillus inulinus NRIC 1133(T)
10.1016/s0922-338x(97)81247-0 · 1996 · External reference
Comparison of alkyl hydroperoxide reductase and two water-forming NADH oxidases from Bacillus cereus ATCC 14579
10.1007/s00253-012-3919-1 · 2012 · External reference
The NADH oxidase from Pyrococcus furiosus: Implications for the protection of anaerobic hyperthermophiles against oxidative stress
10.1046/j.0014-2956.2001.02526.x · 2001 · External reference
TK1299, a highly thermostable NAD(P)H oxidase from Thermococcus kodakaraensis exhibiting higher enzymatic activity with NADPH
10.1016/j.jbiosc.2013.01.020 · 2013 · External reference
Evolution of function in the “two dinucleotide binding domains” flavoproteins
10.1371/journal.pcbi.0030121 · 2007 · External reference
An enzymatic process to α-ketoglutarate from L-glutamate: The coupled system L-glutamate dehydrogenase/NADH oxidase
10.1016/j.tetasy.2004.07.055 · 2004 · External reference
Cloning and characterization of a thermostable H2O-forming NADH oxidase from Lactobacillus rhamnosus
10.1016/j.enzmictec.2012.01.009 · 2012 · External reference
Hexameric ring structure of a thermophilic archaeon NADH oxidase that produces predominantly H2O
10.1111/j.1742-4658.2008.06665.x · 2008 · External reference
Application of a novel thermostable NAD(P)H oxidase from hyperthermophilic archaeon for the regeneration of both NAD+ and NADP+
10.1002/bit.23294 · 2012 · External reference
Identification of two distinct NADH oxidases corresponding to H2O2-forming oxidase and H2O-forming oxidase induced in Streptococcus mutans
10.1099/00221287-139-10-2343 · 1993 · External reference
10.1093/bioinformatics/bti770
10.1093/bioinformatics/bti770 · External reference
KorB protein of promiscuous plasmid RP4 recognizes inverted sequence repetitions in regions essential for conjugative plasmid transfer
10.1093/nar/20.8.1851 · 1992 · External reference
Nature of materials in serum that interfere in the glucose oxidase peroxidase o-dianisidine method for glucose, and their mode of action
10.1093/clinchem/21.1.119 · 1975 · External reference
A simple and efficient expression and purification system using two newly constructed vectors
10.1016/j.pep.2008.09.008 · 2009 · External reference
Sequence saturation mutagenesis (SeSaM): a novel method for directed evolution
10.1093/nar/gnh028 · 2004 · External reference
10.1038/250194a0
10.1038/250194a0 · External reference
Redesign of the coenzyme specificity of a dehydrogenase by protein engineering
10.1038/343038a0 · 1990 · External reference
Pyridine nucleotide complexes with Bacillus anthracis coenzyme A-disulfide reductase: A structural analysis of dual NAD(P)H specificity
10.1021/bi8002204 · 2008 · External reference
The crystal structure of NAD(P)H oxidase from Lactobacillus sanfranciscensis: Insights into the conversion of O2 into two water molecules by the flavoenzyme
10.1021/bi060692p · 2006 · External reference
10.1002/pro.5560030916
10.1002/pro.5560030916 · External reference
Creation of an NADP-dependent pyruvate dehydrogenase multienzyme complex by protein engineering
10.1021/bi00062a001 · 1993 · External reference
Role of aspartic acid 38 in the cofactor specificity of Drosophila alcohol dehydrogenase
10.1111/j.1432-1033.1991.tb16371.x · 1991 · External reference
10.1016/j.str.2005.11.016
10.1016/j.str.2005.11.016 · External reference
Structure-guided alteration of coenzyme specificity of formate dehydrogenase by saturation mutagenesis to enable efficient utilization of NADP+
10.1111/j.1742-4658.2008.06533.x · 2008 · External reference
10.1074/jbc.m111.274571
10.1074/jbc.m111.274571 · External reference
Enantioselective oxidation of aldehydes catalyzed by alcohol dehydrogenase
10.1002/anie.201203219 · 2012 · External reference
Cofactor regeneration of both NAD+ from NADH and NADP+ from NADPH: NADH oxidase from Lactobacillus sanfranciscensis
10.1002/adsc.200303039 · 2003 · External reference
Coenzyme regeneration catalyzed by NADH oxidase from Lactobacillus brevis in the reaction of l-amino acid oxidation
10.1016/j.bej.2007.10.003 · 2008 · External reference
An efficient and selective enzymatic oxidation system for the synthesis of enantiomerically pure D-tert-Leucine
10.1021/ol035314g · 2003 · External reference
