Methylophilus

Medium recycle (item 5) means that organic materials released from Methylophilus... 

This by-passes the energy-consuming GS step of the GS/GOGAT pathway used by Methylophilus methylotrophus and is thus more effident. 

It was dedded to use genetic engineering to put the more-effident GDH system from E. coli into Methylophilus methylotrophus AS1. The strategy was as follows ... 

Membrane module, 369-373 Methylophilus methylotrophus, 338 Michaelis-Menten equation, 109, 137 Microfiltration, 357... 

A protein, designated cyctochrome c", isolated from the methylotrophic bacterium Methylophilus methylotrophus, has been studied extensively because of its unusual properties and was found to have an average molecular mass of 14293.0 Da and to contain 124 amino acid residues. The A-terminal sequence to residue 62 had been determined and the heme binding site had been located at Cys-49 and Cys-52 [12]. Further studies were concerned with determining the remainder of the sequence. 

Table 5.9 Peptides detected during the LC-electrospray-MS (LC-ESMS) analysis of the endoproteinase Lys-C digest from native cytochrome c". Reprinted from Biochim. Biophys. Acta, 1412, Klarskov, K., Leys, D., Backers, K., Costa, H. S., Santos, H., Gnisez, Y. and Van Beenmen, J. J., Cytochrome c" from the obligate methylotroph Methylophilus methylotrophus, an unexpected homolog of sphaeroides heme protein from the phototroph Rhodobacter sphaeroides", 47-55, Copyright (1999), with permission from Elsevier Science...

WYBORN, N.R., SCHERR, D.J., JONES, C.W., Purification, properties and heterologous expression of formamidase from Methylophilus methylotrophus, Microbiology, 1994,140,191-195. 

Methylophilus methylotrophus, 11 3 Methylotrophic yeasts, 72 479 Methylparaben, antimicrobial used in cosmetics, 7 831t Methyl Parathion... 

Methylamine dehydrogenase of Methylophilus methylotro-phus, proton transfer from the methylamine adduct of tryptophan tryptophylquinone (TTQ) CHs-amine vs. CDs-amine, transient kinetics studies of H-transfer step, H/D IE 5-40 °C, Ah/Ad = 16.8 0.5, AH 42.2 1.1 (H), 43.2 1.8 (D) kJ/mol, rate constant unchanged. 

Evidence for a hydride transfer mechanism (Scheme 29) for the PQQ-dependent enzyme methanol dehydrogenase (MDH) was obtained by a theoretical analysis combined with an improved refinement of a 1.9 A resolution crystal structure of MDH from Methylophilus methylotrophus in the presence of CH3OH <2001PNA432>. The alternative mechanism proceeding via a hemiketal intermediate was discounted when the observed tetrahedral configuration of the C-5 atom of PQQ in that crystal structure was shown to be the C-5-reduced form of the cofactor 198, a precursor to the more common reduced form of PQQ 199. 

Trimethylamine dehydrogenase is an iron-sulfur flavoprotein found in the methylotrophic bacterium Methylophilus methylotrophus W3A1. It catalyzes the oxidative N-demethylation of trimethylamine by water with formation of dimethylamine and formaldehyde (Steenkamp and Mallinson, 1976). The protein is a symmetrical dimer consisting of 166kDa subunits (Kasprzak et al., 1983 Lim et al., 1982). Each subunit contains one 4Fe-4S center and one FMN cofactor. The latter is bound covalently through the 6... 

FIGURE 13. Amino acid sequence of the two subunits of methanol dehydrogenase. AMI indicates the sequence for MDH from Methylobac-terium ( xtorqiietis AMI (Anderson ei a/.. 1990 Nunn el a ., 1989 Anthony, 1992b) W3A1 indicates the sequence for Methylophilus W3A1 (Xia el al.. 1996). 

Cox, J. M., Day, D. J., and Anthony, C., 1992, The interaction of methanol dehydrogenase and its electron acceptor, cytochrome Cl, in the facultative methylotroph Methylobacterium extorquens AMI and in the obligate methylotroph Methylophilus methylotrophus. Biochim. Biophys. Acta. 1119 97nl06. 

Long, A. R., and Anthony, C., 1991, The periplasmic modifier protein for methanol dehydrogenase in the methylotrophs Methylophilus methylotrophus and Paracoccus denitrificans. Journal of General Microbiology 137 235392360. 

Page, M. D., and Anthony, C., 1986, Regulation of formaldehyde oxidation by the methanol dehydrogenase modifier proteins of Methylophilus methylotrophus and Pseudomonas AMI. Journal of General Microbiology 132 155391563. 

Mathews, F. S., Trickey, P., Barton, J. D., and Chen, Z.-W., 1996, Crystal structures of recombinant wild-type and a C30A mutant trimethylamine dehydrogenase from Methylophilus WjAi, in Flavins and Flavoproteins (K. Stevenson, V. Massey, and C. H. Williams, eds.). University of Calgary Press, Calgary, pp. 873-876. 

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