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Proline dehydrogenase from Escherichia coli K12. Reconstitution of a functional membrane association. by S B Graham; J T Stephenson; J M Wood is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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Soluble and membrane associated proline dehydrogenase differ in catalytic properties. The soluble enzyme transfers electrons from L-proline to exogenous electron acceptors. It has a high Km for L-proline (105 mM) and is insensitive to the respiratory chain inhibitors 5-ethyl-5-isopentyl-barbituric acid and cyanide. The membrane-associated enzyme transfers electrons from L-proline to O2 via the respiratory chain, with coupled transmembrane proton translocation. It has a low Km for L-proline (3 mM) and is inhibited by 5-ethyl-5-isopentyl-barbituric acid and cyanide. Proline:O2 oxidoreductase activity identical to that of native membranes can be reconstituted using enzyme purified in the absence of detergent and enzyme deficient membranes from a putA mutant strain. Reassociation of the enzyme with the membrane is an autocatalytic process that requires the simultaneous presence of L-proline, MgCl2, enzyme, and membranes. It can be monitored by observing the chromogenic reaction of delta 1-pyrroline carboxylic acid with o-aminobenzaldehyde. Reduction of membrane components or generation of a protonmotive force is apparently required to promote enzyme-membrane association or to activate

Who reads Proline dehydrogenase from Escherichia coli K12. Reconstitution of a functional membrane association.?

Author

S B Graham; J T Stephenson; J M Wood

Publisher

Elsevier BV

Published

1984

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)