By Ryan J. Huxtable
There may be few parts with a biochemistry as coherent as that of sulfur. this significant point is essential to myriad points of metabo lism, catalysis, and constitution. The plurality of features during which sulfur is concerned derives squarely from the varied oxidation states during which it might exist, a few having nice balance, a few being able to prepared redox interconversions, and but others having nice instability. for this reason, the flux of sulfur from the geosphere throughout the a variety of kingdoms of lifestyles leaves few biochemical approaches unaffected. even supposing there are huge gaps within the cloth of our simple wisdom of sulfur biochemistry, it's sufficiently framed to permit a unified and arranged tale, a narrative which some of the best-known names in bio chemistry have helped to jot down. it's been either a job and a privilege to aim and summarize this tale, person who is gigantic, complicated, quickly relocating, nonetheless constructing and, primarily, interesting. i assume that no mo nographer of any such great topic might be happy along with his efforts. it really is regrettably possible that during trying this job i've got made as many blunders as a Stilton cheese has blue streaks, and as many omissions as a Swiss cheese has holes. Perfection isn't to be completed in a monograph. Inasmuch as i've got succeeded, the credits belongs to these whose efforts gave us the information we've got. the place i've got failed, the fault is barely mine.
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Additional resources for Biochemistry of Sulfur
In the first case, formate condenses with THF to form a methine which is reduced to 5,1 0-methylene THF. In the second case, methylene THF is formed directly by the reaction of serine and THF. Reduction of the 5,10-methylene derivative yields 5-methyl THF. It is the 5-methyl group which is transferred to form Met. 5-Methyl THF (and its polyglutamate analogs) serve no known metabolic function apart from their involvement in Met biosynthesis. Mutants of bacteria lacking methylene tetrahydrofolate reductase are Met auxotrophs (Smith, 1971).
Enzyme dependence on methylfolate derivatives has the effect of coordinating formation of Hey and methyl groups for Met synthesis, and preventing the buildup of methylated folates in the absence of Hey. This differs from regulation in enteric bacteria, where y-synthase activity is controlled by synergistic end-product inhibition. Cystathionine y-synthase from Neurospora consists of two proteins. It was at one time thought that one of these proteins had sulfhydrylase activity, but this has been convincingly disproved (Kerr, 1971; Kerr and Flavin, 1970).