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
-
2.5.1.48
-
homocystinuria
-
transsulfuration
-
beta-lyase
-
gamma-lyase
-
sulfhydrylase
-
o-acetylhomoserine
-
gamma-replacement
-
l-cystathionine
-
cystathionase
-
o-phosphohomoserine
-
paucicostata
-
gamma-elimination
-
homocystine
-
s-methylmethionine
-
remethylation
-
synthesis
- 2.5.1.48
- homocystinuria
-
transsulfuration
-
beta-lyase
-
gamma-lyase
-
sulfhydrylase
- o-acetylhomoserine
-
gamma-replacement
- l-cystathionine
- cystathionase
- o-phosphohomoserine
- paucicostata
-
gamma-elimination
- homocystine
- s-methylmethionine
-
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
Advanced search results
Cofactor
Cofactor on EC 2.5.1.48 - cystathionine gamma-synthase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
-
-
pyridoxal 5'-phosphate
-
Km: 0.00004 mM
pyridoxal 5'-phosphate
-
4 mol tightly bound per mol of enzyme
pyridoxal 5'-phosphate
-
one molecule is attached to one subunit of the protein, apoenzyme is completely inactive. Unfolding by guanidinium/HCl inactivates the enzyme due to loss of ketoenamine tautomer. Though pyridoxal 5'-phosphate induces difference in secondary structure content, it is unable to provide stabilizing effect during the overall secondary structure unfolding process. It induces tertiary structure stability of the protein thereby counteracting the deleterious effect of denaturant
pyridoxal 5'-phosphate
the pyridoxal phosphate cofactor is covalently bound to Lys204 via a Schiff base linkage in the deep cavity