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Literature summary for 4.2.1.22 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)

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

Protein Variants

Protein Variants Comment Organism
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
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
G247A undetectable beta-replacement activity Saccharomyces cerevisiae
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
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
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
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
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

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
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Substrates and Products (Substrate)

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

Synonyms

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

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate
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Saccharomyces cerevisiae