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186 PROTEIN METABOLISM<br />

CO 2<br />

Dec-SAM<br />

(11)<br />

SAM<br />

5-methyl thioadenosine<br />

(12)<br />

(10)<br />

2-K-4-M-thiobutyrate<br />

(2)<br />

(14)<br />

(15)<br />

5-methylthioribose<br />

1-phosphate<br />

(16)<br />

1-P-2,3-diK-5-M-thiopentane<br />

5-M-thioribulose-1-P<br />

<br />

Metanethiol NH 4<br />

α-ketobutyrate<br />

‘CH<br />

SAM<br />

3 ’<br />

(1) (2) (3)<br />

METHIONINE<br />

Betaine<br />

mTHF<br />

<br />

α-KG NH 4 SH 2<br />

(9)<br />

(5)<br />

S-adenosyl-homocysteine<br />

Homocysteine<br />

(6)<br />

Cystathionine<br />

(7)<br />

(4)<br />

SERINE<br />

<br />

α-KG NH 4<br />

5-methylthioribose<br />

(13)<br />

SERINE SH 2<br />

(8)<br />

CYSTEINE<br />

FIGURE 8.3 Methionine salvage pathways and catabolism. SAM, S-adenosylmethionine; dec-SAM, decarboxylated<br />

S-adenosylmethionine; -KG, -ketoglurate; ‘CH 3 ’, methyl group <strong>trans</strong>ferred to several substrates; 5-M-thioribulose-<br />

1-P, 5-methylthioribulose-1-phosphate; 1-P-2,3-diK-5-M-thiopentane, 1-phospho-2,3-diketo-5-methylthiopentane;<br />

2-K-4-M-thiobutyrate, 2-keto-4-methylthiobutyrate; mTHF, methyltetrahydrofolate. (1) methionine -lyase;<br />

(2) S-adenosylmethionine synthetase; (3) S-adenosylmethionine-linked methyl <strong>trans</strong>ferases; (4) S-adenosylhomocysteine<br />

hydrolase; (5) methionine synthase; (6) cystathionine -synthetase; (7) -cystathionase; (8) L-serine<br />

desulfhydrase; (9) homocysteine desulfurase; (10) S-adenosylmethionine decarboxylase; (11) spermidine synthase;<br />

(12) 5-methylthioadenosine nucleosidase; (13) 5-methylthioribose kinase; (14) 5-methylthioadenosine phosphorylase;<br />

(15) 5-methylthioribose 1-phosphate isomerase; (16) methionine amino<strong>trans</strong>ferase.<br />

Cysteine can be obtained from methionine,<br />

through the reactions of cystathionine-synthetase<br />

and -cystathionase (Figure 8.3).<br />

Cystathionine--synthetase has been studied<br />

in T. vaginalis and in nematodes; like the<br />

mammalian enzyme, both parasite enzymes<br />

have L-serine sulfhydrase activity which catalyzes<br />

the reversible interconversion of cysteine<br />

and serine, with the exchange of SH 2 .<br />

In contrast to the mammalian enzyme, the<br />

parasite enzymes have ‘activated L-serine<br />

sulfhydrase’ activity catalyzing the reaction of<br />

cysteine with a number of R-SH compounds,<br />

resulting in the formation of a cysteine thioether<br />

and the liberation of SH 2 . Both the nematode<br />

and the T. vaginalis enzymes are inhibited by a<br />

number of compounds, such as dichlorophene<br />

and hexachlorophene, which have both antitrichomonal<br />

and anthelmintic effects.<br />

Threonine and serine<br />

Two pathways of threonine catabolism have<br />

been described in some protozoa (Figure 8.4).<br />

BIOCHEMISTRY AND CELL BIOLOGY: PROTOZOA

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