Malate utilization by a group D Streptococcus: physiological properties and purification of an inducible malic enzyme.

Abstract:

:Growth of Streptococcus faecalis in the presence of l-malate resulted in the induction of a "malic enzyme" [l-malate:nicotinamide adenine dinucleotide (NAD) oxidoreductase (decarboxylating), E.C. 1.1.1.39]. Synthesis of the malic enzyme did not appear to be subject to catabolite repression by intermediate products of glucose or fructose dissimilation. However, malate utilization was inhibited during growth in the presence of glucose or fructose. The purified enzyme was specific for malate as substrate and NAD as cofactor. Mn(+2) or Mg(+2) was required for optimal activity and NH(4)Cl stimulated the reaction rate. Several lines of indirect evidence suggested that the streptococcal malic enzyme was involved primarily with energy production and not biosynthesis.

journal_name

J Bacteriol

journal_title

Journal of bacteriology

authors

London J,Meyer EY

doi

10.1128/JB.98.2.705-711.1969

subject

Has Abstract

pub_date

1969-05-01 00:00:00

pages

705-11

issue

2

eissn

0021-9193

issn

1098-5530

journal_volume

98

pub_type

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