TY - CHAP
T1 - “Designer Membranes”
T2 - Construction of a Cell Containing Multiple Membrane-Bound Cytochromes P450
AU - Estabrook, Ronald W.
AU - Trant, John M.
AU - Mathew, Porunelloor A.
AU - Mason, J. Ian
AU - Waterman, Michael R.
N1 - Funding Information:
ACKNOWLEDGMENTS This article is dedicated to Paul A. Srere, a master enzymologist, on the occasion of his 65th birthday. Supported in part by grants from the National Institutes of Health (GM16488, GM37942, and AG08175) and the Robert A. Welch Foundation (1-624 and 1-959). J.M.T. was supported by a U.S. Public Health Service Training Grant (5-T32HD07190).
PY - 1992/1/1
Y1 - 1992/1/1
N2 - This chapter discusses designer membranes and its construction of a cell containing multiple membrane-bound cytochromes p450. The techniques of molecular biology offer the opportunity to introduce foreign DNA into naive cells to express enzymatically active proteins that can be tested in situ. Indeed, one is able to introduce simultaneously the DNAs for a number of different soluble and membrane-bound proteins, and thereby construct a functional metabolic pathway in a cell not programmed for such activities. Cytochrome P450 is best characterized as the catalyst for many monooxygenase—mixed function oxidase—reactions. For these reactions, a P450 serves as the central agent for the binding of a molecule of substrate, the acceptance of reducing equivalents provided by electrons transferred from reduced pyridine nucleotide via an abbreviated electron transport chain, and the activation of a molecule of molecular oxygen. The use of heterologous expression of enzymes, in particular membrane-bound enzymes, at present offers the possibility to contribute new types of data needed for the better understanding the functioning of enzymes in the environment of a cell.
AB - This chapter discusses designer membranes and its construction of a cell containing multiple membrane-bound cytochromes p450. The techniques of molecular biology offer the opportunity to introduce foreign DNA into naive cells to express enzymatically active proteins that can be tested in situ. Indeed, one is able to introduce simultaneously the DNAs for a number of different soluble and membrane-bound proteins, and thereby construct a functional metabolic pathway in a cell not programmed for such activities. Cytochrome P450 is best characterized as the catalyst for many monooxygenase—mixed function oxidase—reactions. For these reactions, a P450 serves as the central agent for the binding of a molecule of substrate, the acceptance of reducing equivalents provided by electrons transferred from reduced pyridine nucleotide via an abbreviated electron transport chain, and the activation of a molecule of molecular oxygen. The use of heterologous expression of enzymes, in particular membrane-bound enzymes, at present offers the possibility to contribute new types of data needed for the better understanding the functioning of enzymes in the environment of a cell.
UR - http://www.scopus.com/inward/record.url?scp=0026439445&partnerID=8YFLogxK
U2 - 10.1016/B978-0-12-152833-1.50029-0
DO - 10.1016/B978-0-12-152833-1.50029-0
M3 - Chapter
C2 - 1499343
AN - SCOPUS:0026439445
T3 - Current Topics in Cellular Regulation
SP - 419
EP - 431
BT - Current Topics in Cellular Regulation
ER -