This view shows enzymes only for those organisms listed below, in the list of taxa known to possess the pathway. If an enzyme name is shown in bold, there is experimental evidence for this enzymatic activity.
Synonyms: transsulfuration pathway
|Superclasses:||Activation/Inactivation/Interconversion → Interconversions|
|Biosynthesis → Amino Acids Biosynthesis → Proteinogenic Amino Acids Biosynthesis → L-cysteine Biosynthesis|
Some taxa known to possess this pathway include : Saccharomyces cerevisiae
Transsulfuration pathways allow the interconversion of L-homocysteine and L-cysteine via L-cystathionine. In contrast to enteric bacteria and mammals, Saccharomyces cerevisiae has two transsulfuration pathways employing two separate sets of enzymes [Thomas97].
Variants: L-cysteine biosynthesis I , L-cysteine biosynthesis II (tRNA-dependent) , L-cysteine biosynthesis III (from L-homocysteine) , L-cysteine biosynthesis V , superpathway of L-cysteine biosynthesis (mammalian)
Barton93: Barton AB, Kaback DB, Clark MW, Keng T, Ouellette BF, Storms RK, Zeng B, Zhong W, Fortin N, Delaney S (1993). "Physical localization of yeast CYS3, a gene whose product resembles the rat gamma-cystathionase and Escherichia coli cystathionine gamma-synthase enzymes." Yeast 9(4);363-9. PMID: 8511966
Belfaiza86: Belfaiza J, Parsot C, Martel A, de la Tour CB, Margarita D, Cohen GN, Saint-Girons I (1986). "Evolution in biosynthetic pathways: two enzymes catalyzing consecutive steps in methionine biosynthesis originate from a common ancestor and possess a similar regulatory region." Proc Natl Acad Sci U S A 83(4);867-71. PMID: 3513164
Cherest92: Cherest H, Surdin-Kerjan Y (1992). "Genetic analysis of a new mutation conferring cysteine auxotrophy in Saccharomyces cerevisiae: updating of the sulfur metabolism pathway." Genetics 130(1);51-8. PMID: 1732168
Cherest93: Cherest H, Thomas D, Surdin-Kerjan Y (1993). "Cysteine biosynthesis in Saccharomyces cerevisiae occurs through the transsulfuration pathway which has been built up by enzyme recruitment." J Bacteriol 1993;175(17);5366-74. PMID: 8366024
Clausen96: Clausen T, Huber R, Laber B, Pohlenz HD, Messerschmidt A (1996). "Crystal structure of the pyridoxal-5'-phosphate dependent cystathionine beta-lyase from Escherichia coli at 1.83 A." J Mol Biol 262(2);202-24. PMID: 8831789
Hansen00: Hansen J, Johannesen PF (2000). "Cysteine is essential for transcriptional regulation of the sulfur assimilation genes in Saccharomyces cerevisiae." Mol Gen Genet 263(3);535-42. PMID: 10821189
Jhee00: Jhee KH, McPhie P, Miles EW (2000). "Yeast cystathionine beta-synthase is a pyridoxal phosphate enzyme but, unlike the human enzyme, is not a heme protein." J Biol Chem 275(16);11541-4. PMID: 10766767
Kraus78: Kraus J, Packman S, Fowler B, Rosenberg LE (1978). "Purification and properties of cystathionine beta-synthase from human liver. Evidence for identical subunits." J Biol Chem 253(18);6523-8. PMID: 681363
Kruger94: Kruger WD, Cox DR (1994). "A yeast system for expression of human cystathionine beta-synthase: structural and functional conservation of the human and yeast genes." Proc Natl Acad Sci U S A 91(14);6614-8. PMID: 8022826
Lambrecht12: Lambrecht JA, Flynn JM, Downs DM (2012). "Conserved YjgF protein family deaminates reactive enamine/imine intermediates of pyridoxal 5'-phosphate (PLP)-dependent enzyme reactions." J Biol Chem 287(5);3454-61. PMID: 22094463
Lodha10: Lodha PH, Jaworski AF, Aitken SM (2010). "Characterization of site-directed mutants of residues R58, R59, D116, W340 and R372 in the active site of E. coli cystathionine beta-lyase." Protein Sci 19(3);383-91. PMID: 20014435
Maclean00: Maclean KN, Janosik M, Oliveriusova J, Kery V, Kraus JP (2000). "Transsulfuration in Saccharomyces cerevisiae is not dependent on heme: purification and characterization of recombinant yeast cystathionine beta-synthase." J Inorg Biochem 81(3);161-71. PMID: 11051561
Matsuo58: Matsuo, Y, Greenberg, DM (1958). "A crystalline enzyme that cleaves homoserine and cystathionine. I. Isolation procedure and some physicochemical properties." J Biol Chem 230(2);545-60. PMID: 13525371
Matsuo59: Matsuo, Y., Greenberg, D.M. (1959). "A crystalline enzyme that cleaves homoserine and cystathionine. IV. Mechanism of action, reversibility, and substrate specificity." J Biol Chem 234(3):516-9. PMID: 13641251
Matsuo59a: Matsuo, Y, Greenberg, DM (1959). "A crystalline enzyme that cleaves homoserine and cystathionine. III. Coenzyme resolution, activators, and inhibitors." J Biol Chem 234(3);507-15. PMID: 13641250
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