2.5.1.48: cystathionine gamma-synthase
This is an abbreviated version!
For detailed information about cystathionine gamma-synthase, go to the full flat file.
Word Map on EC 2.5.1.48
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2.5.1.48
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homocystinuria
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transsulfuration
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beta-lyase
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gamma-lyase
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sulfhydrylase
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o-acetylhomoserine
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gamma-replacement
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l-cystathionine
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cystathionase
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o-phosphohomoserine
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paucicostata
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gamma-elimination
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homocystine
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s-methylmethionine
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remethylation
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synthesis
- 2.5.1.48
- homocystinuria
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transsulfuration
-
beta-lyase
-
gamma-lyase
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sulfhydrylase
- o-acetylhomoserine
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gamma-replacement
- l-cystathionine
- cystathionase
- o-phosphohomoserine
- paucicostata
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gamma-elimination
- homocystine
- s-methylmethionine
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remethylation
- synthesis
Reaction
Synonyms
AtCGS, CGS, CGS1, CS,26, cystathionine gamma-synthase, cystathionine synthase, cystathionine synthetase, cystathionine-gamma-synthase, EC 4.2.99.9, homoserine O-transsuccinylase, homoserine transsuccinylase, HTS, MetB, O-succinyl-L-homoserine succinate-lyase (adding cysteine), O-succinylhomoserine (Thiol)-lyase, O-succinylhomoserine synthase, O-succinylhomoserine synthetase, synthase, cystathionine gamma-
ECTree
2.5.1.48 cystathionine gamma-synthaseAdvanced search results
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results (Engineering
Engineering on EC 2.5.1.48 - cystathionine gamma-synthase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
D45A
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decrease in kcat and increase in Km value of succinyl-L-homoserine substrate
D45F
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reduction in catalytic effciency, without change in reaction specificity
D45F/E325Y
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reduction in catalytic effciency, without change in reaction specificity
D45N
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decrease in kcat and increase in Km value of succinyl-L-homoserine substrate
E325Y
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reduction in catalytic effciency, without change in reaction specificity
R106A
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the Arg residues at positions 48, 106 and 361 tether the distal and alpha-carboxylate moieties, respectively, of the succinyl-L-homoserine substrate
R106K
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the Arg residues at positions 48, 106 and 361 tether the distal and alpha-carboxylate moieties, respectively, of the succinyl-L-homoserine substrate
R361K
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the Arg residues at positions 48, 106 and 361 tether the distal and alpha-carboxylate moieties, respectively, of the succinyl-L-homoserine substrate
R48K
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the Arg residues at positions 48, 106 and 361 tether the distal and alpha-carboxylate moieties, respectively, of the succinyl-L-homoserine substrate
R49K
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3fold increase in Km value for both succinyl-L-homoserine and L-cysteine
S326A
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decrease in kcat and increase in Km value of succinyl-L-homoserine substrate
Y46F
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large decrease in kcat and increase in Km value of succinyl-L-homoserine substrate
F97Y
additional information
F97Y
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the mutant shows reduced activity compared to the wild type enzyme
F97Y
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enzymatic activity at 80°C is similar to wild-type at acidic to neutral pH, and about 50% of wild-type at basic pH
F97Y
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the mutant shows reduced activity compared to the wild type enzyme
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F97Y
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enzymatic activity at 80°C is similar to wild-type at acidic to neutral pH, and about 50% of wild-type at basic pH
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additional information
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overexpression of full-length enzyme and its truncated version that lacks the N-terminal region in transgenic Nicotiana tobacum plants. Transgenic plants expressing both types of enzyme have a significant higher level of Met and S-methyl-Met content in their proteins. Plants expressing full-length enzyme show the same phenotype and developmental pattern as wild-type plants, those expressing the truncated length enzyme show a severely abnormal phenotype
additional information
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overexpression of the enzyme in Brassica juncea, 5 transgenic lines with up to 10fold increased enzyme level, enzyme expression enhances selenium volatilization in the transgenic plants compared to the wild-type plants, transgenic plants show increased tolerance against selenite and reduced selenite levels in shoots and roots, overview
additional information
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co-expression of Arabidopsis thaliana cystathionine gamma-synthase and bacterial feedback-insensitive aspartate kinase in tobacco. Plants co-expressing both enzymes have significantly higher methionine and threonine levels compared with the levels found in wild-type plants, but the methionine level does not increase beyond that found in plants expressing cystathionine gamma-synthase alone. Plants expressing bacterial feedback-insensitive aspartate kinase and one of two mutated forms of cystathionine gamma-synthase in which the domains responsible for the feedback regulation have been deleted, show significantly higher methionine contents and its metabolites levels accumulate in the newly produced plants. The levels of threonine are also significantly higher than in the wild-type plants. The transcript level of the two mutated forms of cystathionine gamma-synthase significantly increases when there is a high content of threonine in the plants, suggesting that threonine modulates, probably indirectly, the transcript level of cystathionine gamma-synthase
