Reductase gene sequences and protein structures: p-cymene methyl hydroxylase.

作者: Tapan K. Dutta , Irwin C. Gunsalus

DOI: 10.1006/BBRC.1997.6493

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摘要: Abstract Oxygenases are critical to cycling carbon in the biosphere and dependent on reductase action, principally from flavoprotein enzymes. Oxygenase diversity among organisms strains carries a common theme of protein sequence folding. p -Cymene ( para -isopropyl toluene) was chosen as point convergence terpene-aromatic mineralization characterize methyl hydroxylase electron transport system with aerobe Pseudomonas aureofaciens. The cymA gene isolated sequenced primary structure deduced. Optimized amino acid alignments reductases revealed major similarities over length, binding domains for NAD(P)H, flavine centers pro- eukaryote systems.

参考文章(45)
Susan J. Assinder, Peter A. Williams, The TOL Plasmids: Determinants of the Catabolism of Toluene and the Xylenes Advances in Microbial Physiology. ,vol. 31, pp. 1- 69 ,(1990) , 10.1016/S0065-2911(08)60119-8
David Botstein, Ronald W. Davis, John R. Roth, Advanced bacterial genetics Cold Spring Harbor Laboratory. ,(1980)
E. Margoliash, O.F. Walasek, [61] Cytochrome c from vertebrate and invertebrate sources Methods in Enzymology. ,vol. 10, pp. 339- 348 ,(1967) , 10.1016/0076-6879(67)10064-5
C E Cerniglia, K J Lambert, D W Miller, J P Freeman, Transformation of 1- and 2-methylnaphthalene by Cunninghamella elegans Applied and Environmental Microbiology. ,vol. 47, pp. 111- 118 ,(1984) , 10.1128/AEM.47.1.111-118.1984
G Baggi, P Barbieri, E Galli, S Tollari, Isolation of a Pseudomonas stutzeri strain that degrades o-xylene. Applied and Environmental Microbiology. ,vol. 53, pp. 2129- 2132 ,(1987) , 10.1128/AEM.53.9.2129-2132.1987