L(+) lactate dehydrogenase activity from the electric organ of Electrophorus electricus (L.).

Abstract:

:Properties of L(+) lactate dehydrogenase (LDH) of Electrophorus electricus (L.) electric organ were studied, comparing the substrates pyruvate and lactate. Electric organ LDH is a soluble enzyme with a pH optimum of 7.4 for pyruvate and 9.0 for lactate. The apparent Km was lower for pyruvate (Km = 2.5 X 10(-4) M) than for lactate (Km = 1.5 X 10(-2) M). With lactate as a substrate at pH 7.4, malonate, oxalate and pyruvate inhibited competitively. For pyruvate as substrate at pH 9.0 malonate inhibited non-competitively and oxalate shiwed uncompetitive inhibition. The different effects of the carboxylic acids on LDH activity suggest different stereospecificities of the two enzyme-coenzyme complexes in the forward and reserve reactions. The reactions of electric organ LDH with substrates and inhibitors are consistent with electrophoretic analysis suggesting that the enzyme is of the M-type.

journal_name

An Acad Bras Cienc

authors

Torres-da Matta J,Nery da Matta A,Hassón-Voloch A

subject

Has Abstract

pub_date

1976-01-01 00:00:00

pages

145-51

issue

1

eissn

0001-3765

issn

1678-2690

journal_volume

48

pub_type

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