Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 4.2.1.22 extracted from

  • Yamanishi, M.; Kabil, O.; Sen, S.; Banerjee, R.
    Structural insights into pathogenic mutations in heme-dependent cystathionine-beta-synthase (2006), J. Inorg. Biochem., 100, 1988-1995.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
D444N basal activity of the recombinant D444N mutant is 1.5fold higher than that of wild-type enzyme under similar conditions but 1.3fold lower than wild-type enzyme in the presence of S-adenosyl-L-methionine. D444N mutant retains the ability to bind AdoMet albeit with reduced affinity Homo sapiens
I437T mutation results in loss of S-adenosyl-L-methionine-dependent activation but exhibits basal activity that is comparable to that of wild-type enzyme expressed under the same conditions. Purified recombinant I435T shows a two to 3fold higher basal activity compared to wild-type enzyme but is unresponsive to the allosteric activator S-adenosyl-L-methionine Homo sapiens
additional information structural insights into pathogenic mutations Homo sapiens
S466L mutant exhibits a higher basal activity than wild-type enzyme but cannot be further activated by the allosteric effecto S-adenosyl-L-methionine Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining

Organism

Organism UniProt Comment Textmining
Homo sapiens P35520
-
-

Substrates and Products (Substrate)

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

Cofactor

Cofactor Comment Organism Structure
heme
-
Homo sapiens