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J. Biol. Chem., Vol. 275, Issue 51, 40316-40323, December 22, 2000
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,
,
,
, and
**
From the The ability of Porphyromonas
gingivalis to biosynthesize tetrapyrroles de novo has
been investigated. Extracts of the bacterium do not possess
activity for 5- aminolevulinic-acid dehydratase or porphobilinogen
deaminase, two key enzymes involved in the synthesis of
uroporphyrinogen III. Similarly, it was not possible to detect any
genetic evidence for these early enzymes with the use of degenerate
polymerase chain reaction. However, the bacterium does appear to harbor
some of the enzymes for cobalamin biosynthesis since cobyric acid, a
pathway intermediate, was converted into cobinamide. Furthermore,
degenerate polymerase chain reaction with primers to cbiP,
which encodes cobyric-acid synthase, produced a fragment with a high
degree of identity to Salmonella typhimurium cbiP. Indeed,
the recently released genome sequence data confirmed the presence of
cbiP together with 14 other genes of the cobalamin pathway.
A number of these genes were cloned and functionally characterized.
Although P. gingivalis harbors all the genes necessary to
convert precorrin-2 into cobalamin, it is missing the genes for the
synthesis of precorrin-2. Either the organism has a novel pathway for
the synthesis of precorrin-2, or more likely, it has lost this early
part of the pathway. The remainder of the pathway may be being
maintained to act as a salvage route for corrin synthesis.
School of Biological Sciences, Queen Mary,
University of London, Mile End Road, London E1 4NS, United Kingdom, the
§ Department of Biochemistry, University of Utah School of
Medicine, Salt Lake City, Utah 84132, the ¶ Department of Life
Sciences, University of East London, London E15 4LZ, United Kingdom,
and the
Public Health Laboratory Service, Central Public
Health Laboratory, 61 Colindale Avenue,
London NW9 5HT, United Kingdom
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