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Mutants alcohol dehydrogenase

Ziegelman-Fjeld, K., Musa, M., Phillips, R., Zeikus, J. and Vieille, C., A Thermoanaerobacter ethanolicus secondary alcohol dehydrogenase mutant derivative highly active and stereoselective on phenylacetone and benzylacetone. Protein Eng. Des. Set, 2007, 20, 47-55. [Pg.286]

The Protein Data Bank PDB ID 1A71 Colby T D Bahnson B J Chin J K Klinman J P Goldstein B M Active Site Modifications m a Double Mutant of Liver Alcohol Dehydrogenase Structural Studies of Two Enzyme Ligand Com plexes To be published... [Pg.1298]

Lapierre, C. Pollet, B. MacKay, J. J. Sederoff, R. R. Lignin structure in a mutant pine deficient in cinnamyl alcohol dehydrogenase. J. Agric. Food Chem. 2000, 48, 2326-2331. [Pg.418]

Deltour L, Foglio MH, Deuster G. Metabolic deficiencies in alcohol dehydrogenase Adhl, Adh3, and Adh4 null mutant mice Overlapping roles of Adhl and Adh4 in ethanol clearance and metabolism of retinol to retinoic acid. J Biol Chem 1999 274 16796-16801. [Pg.440]

Horse liver alcohol dehydrogenase and the F93W mutant, hydride transfer from henzyl alcohol to NAD in MeOH/water. [Pg.52]

Horse liver alcohol dehydrogenase, F93W mutant with 1224 also mutated to G,A,V,L. hydride transfer from benzyl alcohol to NAD Heterotetrameric sarcosine oxidase of Arthrobacter sp. 1-IN, proton transfer from adduct of FAD with sarcosine-(CH3) and sarcosine-(CD3)... [Pg.52]

An enzyme reaction mechanism involving A binding before B and followed with the random release of products. In the absence of products and abortive complexes, the steady-state rate expression is identical to the rate expression for the ordered Bi Bi mechanism . A random on-ordered off Bi Bi mechanism has been proposed for a mutant form of alcohol dehydrogenase. ... [Pg.527]

Arnau J, Jorgensen F, Madsen SM, Vrang A, Israelsen H (1998) Cloning of the Lactococcus lactis adhE gene, encoding a multifunctional alcohol dehydrogenase, by complementation of a fermentative mutant of Escherichia coli. J Bacteriol 180 3049-3055... [Pg.159]

Coniferaldehyde (3.76) can undergo several fates, some of which can ultimately lead to the same end product. It can be reduced to coniferyl alcohol (3.79) by the enzyme cinnamyl alcohol dehydrogenase (CAD). Alternatively, the enzyme coniferyl aldehyde/coniferyl alcohol 5-hydroxylase (C5H), also known by its less accurate name ferulic acid 5-hydroxylase (F5H Humphreys et al., 1999) can catalyze the hydroxylation of C5 to result in 5-hydroxyconiferyl aldehyde (3.77). C5H is also able to form 5-hydroxyconiferyl alcohol (3.80) from coniferyl alcohol (3.79). This enzyme was initially identified as F5H, after analysis of the Arabidopsis ferulic acid hydroxylase 1 (fahl) mutant, which was isolated in a mutant screen based on reduced levels of the UV-fluorescent sinapoyl esters (Section 13 Chappie et al., 1992). The FAH1 gene was cloned using a T-DNA tagged mutant allele (Meyer et al., 1996), which revealed that the... [Pg.105]

Sibout, R., Eudes, A., Pollet, B., Goujon, T., Mila, I., Granier, F., Seguin, A., Lapierre, C., and Jouanin, L., 2003, Expression pattern of two paralogs encoding cinnamyl alcohol dehydrogenases in Arabidopsis. Isolation and characterization of the corresponding mutants, Plant Physiol. 132 848-860. [Pg.147]

Jacobs, M., Dolferus, R. Van Den Bossche (1988). Isolation and biochemical analysis of ethyl methane sulfonate induced alcohol dehydrogenase null mutants of Arabidopsis thaliana (L.) Heynth. Biochemical Genetics 26, 105-12. [Pg.244]

Table 10.5 Comparison of the properties of wild-type and mutant (R)-alcohol dehydrogenase from L brevis. Table 10.5 Comparison of the properties of wild-type and mutant (R)-alcohol dehydrogenase from L brevis.
Horse liver alcohol dehydrogenase, F93W mutant with 1224 also mutated to... [Pg.51]

Riva, M. E. and A. S. Robinson. (1986) "Induction of alcohol dehydrogenase null mutants in the Mediterranean fruit fly, Ceratitis capitata." Biochem. Genet. 24 765-774. [Pg.143]

O Donnell, J., L. Gerace, F. Leister and W. Soffer. (1975) "Chemical selection of mutants that affect alcohol dehydrogenase in Drosophila. II Use of 1-pentyn-3-ol." Genetics 79 73-83. [Pg.143]

JJ MacKay, DM O Malley, T Presnell, FL Booker, MM Campbell, RW Whetten, RR Sederoff. Inheritance, Gene Expression and Lignin Characterization in a Mutant Pine Deficient in Cinnamyl Alcohol Dehydrogenase. Proc Natl Acad Sci USA 94 8255, 1997. [Pg.392]

Luo, J., Kahn, K. and Bruice, T.C. (1999). The linear dependence of log(/ccat//e m) for reduction of NAD + by PhCH2OH on the distance between reactants when catalyzed by horse liver alcohol dehydrogenase and 203 single point mutants. Bioorg. Chem. 27, 289-296... [Pg.361]

See other pages where Mutants alcohol dehydrogenase is mentioned: [Pg.61]    [Pg.284]    [Pg.79]    [Pg.5]    [Pg.158]    [Pg.203]    [Pg.321]    [Pg.570]    [Pg.123]    [Pg.152]    [Pg.201]    [Pg.577]    [Pg.60]    [Pg.198]    [Pg.763]    [Pg.736]    [Pg.15]    [Pg.200]    [Pg.596]    [Pg.145]    [Pg.242]    [Pg.381]    [Pg.392]   


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