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Literature summary extracted from

  • Lodha, P.H.; Shadnia, H.; Woodhouse, C.M.; Wright, J.S.; Aitken, S.M.
    Investigation of residues Lys112, Glu136, His138, Gly247, Tyr248, and Asp249 in the active site of yeast cystathionine beta-synthase (2009), Biochem. Cell Biol., 87, 531-540.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.2.1.22 a truncated form of CBS comprising the catalytic core is used for mutational analysis Saccharomyces cerevisiae

Protein Variants

EC Number Protein Variants Comment Organism
4.2.1.22 D249A a series of 8 site-directed mutants is constructed, and their order of impact on the ability of ytCBS to catalyze the beta-replacement reaction is G247S asymptotically equal to K112Q bigger than K112L asymptotically equal to K112R bigger than Y248F bigger D249A asymptotically equal to H138F bigger than E136A Saccharomyces cerevisiae
4.2.1.22 E136A a series of 8 site-directed mutants is constructed, and their order of impact on the ability of ytCBS to catalyze the beta-replacement reaction is G247S asymptotically equal to K112Q bigger than K112L asymptotically equal to K112R bigger than Y248F bigger D249A asymptotically equal to H138F bigger than E136A Saccharomyces cerevisiae
4.2.1.22 G247A undetectable beta-replacement activity Saccharomyces cerevisiae
4.2.1.22 H138F a series of 8 site-directed mutants is constructed, and their order of impact on the ability of ytCBS to catalyze the beta-replacement reaction is G247S asymptotically equal to K112Q bigger than K112L asymptotically equal to K112R bigger than Y248F bigger D249A asymptotically equal to H138F bigger than E136A. Km (L-homocysteine) increased by 8fold Saccharomyces cerevisiae
4.2.1.22 K112L a series of 8 site-directed mutants is constructed, and their order of impact on the ability of ytCBS to catalyze the beta-replacement reaction is G247S asymptotically equal to K112Q bigger than K112L asymptotically equal to K112R bigger than Y248F bigger D249A asymptotically equal to H138F bigger than E136A. Km (L-Ser) increased by 50fold, Km (L-homocysteine) increased by 2fold Saccharomyces cerevisiae
4.2.1.22 K112Q a series of 8 site-directed mutants is constructed, and their order of impact on the ability of ytCBS to catalyze the beta-replacement reaction is G247S asymptotically equal to K112Q bigger than K112L asymptotically equal to K112R bigger than Y248F bigger D249A asymptotically equal to H138F bigger than E136A Saccharomyces cerevisiae
4.2.1.22 K112R a series of 8 site-directed mutants is constructed, and their order of impact on the ability of ytCBS to catalyze the beta-replacement reaction is G247S asymptotically equal to K112Q bigger than K112L asymptotically equal to K112R bigger than Y248F bigger D249A asymptotically equal to H138F bigger than E136A. Km (L-Ser) increased by 90fold, Km (L-homocysteine) increased by 4fold Saccharomyces cerevisiae
4.2.1.22 Y248F a series of 8 site-directed mutants is constructed, and their order of impact on the ability of ytCBS to catalyze the beta-replacement reaction is G247S asymptotically equal to K112Q bigger than K112L asymptotically equal to K112R bigger than Y248F bigger D249A asymptotically equal to H138F bigger than E136A. Km (L-homocysteine) increased by 18fold Saccharomyces cerevisiae

Organism

EC Number Organism UniProt Comment Textmining
4.2.1.22 Saccharomyces cerevisiae
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-
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.2.1.22 L-serine + L-homocysteine
-
Saccharomyces cerevisiae L-cystathionine + H2O
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?

Synonyms

EC Number Synonyms Comment Organism
4.2.1.22 cystathionine beta-synthase
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Saccharomyces cerevisiae
4.2.1.22 ytCBS a truncated form of CBS comprising the catalytic core is used for mutational analysis Saccharomyces cerevisiae

Cofactor

EC Number Cofactor Comment Organism Structure
4.2.1.22 pyridoxal 5'-phosphate
-
Saccharomyces cerevisiae