Advances in Enzymology and Related Areas of Molecular by Alton Meister
By Alton Meister
Maintains the authoritative sequence that studies study into enzymology and similar components of molecular biology. provides six papers by way of top specialists.
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Additional resources for Advances in Enzymology and Related Areas of Molecular Biology, Volume 56
Serine sulfhydrase isolated from chicken liver (41) was assayed by measuring initial @replacement rates in the assay system with L-cysteine 2-mercaptoethanol (26,64). The experimental results clearly demonstrate the close functional homology of serine sulfhydrase from chicken liver (2) or yeast (2a) with cystathionine P-synthase (3)from rat (63) and human (52) hepatic tissue as species-specific allelozymes (2), as indicated by us in 1971 (26). E). B. There are also substantial differences in M , values and isoelectric points.
Competitive inhibitor constants, lyjapp),(in regard to normal PLP-enzyme) of E. coli tryptophanase (15), tryptophan synthase (107,112), y-cystathionase (91), serine sulfhydrase, and cystathionine P-synthase (36,92). The latter two enzymes are P-replacement-specific, the others are catalytically multifunctional. Considerable differences were observed in the coenzyme analog patterns of the individual lyases, but no characteristic contrast was revealed between those of replacement-specific type and the others, with the exception of the more stringent structural requirements of serine sulfhydrase, 2, and cystathionine P-synthase 3, for catalytically active analogs.
Extract from mitochondrial acetone powder 124 (72) 3. 5 4. 8 elution 5. 8 6. 34 7. 15 gel Fractionation steps Activity' Blue lupine" TABLE V1 Purification of P-Cyanoalanine Synthases from Lupine Seedlings 30 ALEXANDER E. BRAUNSTEIN AND ELIZABETH V. ) 0 0 " From references 65 and 66. rnin-'/l mg enzyme). Concentration is not exact because of the high volatility of the compound. 0 mM). , detoxication of cyanide and the first step in L-asparagine biosynthesis). The synthase unexpectedly proved capable of utilizing 3-thiocyano-L-alanine (= S-cyano-L-cysteine)as a primary substrate (28,66), we observed that lyase 4 effects a slow reaction of cystine with KCN (but with none of the thiol cosubstrates), producing hydrogen sulfide thiocyanate ion and substantially more than one equivalent of cyanoalanine.