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

BRENDA support

Literature summary extracted from

  • Sen, S.; Banerjee, R.
    A pathogenic linked mutation in the catalytic core of human cystathionine beta-synthase disrupts allosteric regulation and allows kinetic characterization of a full-length dimer (2007), Biochemistry, 46, 4110-4116.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.2.1.22 mutant enzymes K102N, P78R and P78R/K102N are expressed in Escherichia coli and purified as glutathione S-transferase fusion proteins using recombinant expression Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
4.2.1.22 K102N KM for L-serine is about 2fold higher than wild-type value. KM for L-homocysteine is 2fold higher than wild-type value Homo sapiens
4.2.1.22 P78R KM for L-serine is about 4fold higher than wild-type value. KM for L-homocysteine is comparable to wild-type value Homo sapiens
4.2.1.22 P78R/K102N KM for L-serine is about 2fold higher than wild-type value. Mutant enzyme is insensitive to allosteric regulation and unresponsive to S-adenosyl-L-methionine Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
4.2.1.22 Homo sapiens
-
-
-

Substrates and Products (Substrate)

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

Subunits

EC Number Subunits Comment Organism
4.2.1.22 More mutant enzymes K102N and P78R/K102N behaves like wild-type enzyme by native gel chromatography and exist as a mixture of higher-order quaternary states Homo sapiens