R. Sagar et al., L-ALANINE-4,5-DIOXOVALERATE TRANSAMINASE IN LEISHMANIA-DONOVANI THAT DIFFERS FROM MAMMALIAN ENZYME, Microbiological research, 150(4), 1995, pp. 419-423
Leishmania protozoans are the causative agents of leishmaniasis, a maj
or parasitic disease in humans. The parasites manifest a nutritional r
equirement for heme compounds since they are deficient in heme biosynt
hesis. In this study we have demonstrated for the first time the prese
nce of the enzyme L-alanine: 4,5-dioxovalerate transaminase in Leishma
nia donovani. This enzyme catalyzes the synthesis of 5-aminolevulinic
acid (ALA), the first committed step in heme synthesis. Thus the defec
t in heme biosynthesis pathway in Leishmania must lie at some enzymati
c level subsequent to synthesis of ALA. The enzyme was found to be pre
sent in both virulent and avirulent strains of L. donovani. The virule
nt promastigotes showed a 41% higher specific activity as compared to
the avirulent strain. The enzyme activity was found to be inhibited in
the presence of heme and methylglyoxal. Immunoblot analysis revealed
that L-alanine: 4,5-dioxovalerate transaminase in L. donovani was immu
nologically different from that in mammals.