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Literature summary for 4.2.1.22 extracted from

  • Kozich, V.; Sokolova, J.; Klatovska, V.; Krijt, J.; Janosik, M.; Jelinek, K.; Kraus, J.P.
    Cystathionine beta-synthase mutations: effect of mutation topology on folding and activity (2010), Hum. Mutat., 31, 809-819.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
S-adenosyl-L-methionine
-
Homo sapiens

Cloned(Commentary)

Cloned (Comment) Organism
genotyping of wild-type and mutant CBSs, determination of mutations in patients with homocystinuria due to CBS deficiency, overview Homo sapiens

Protein Variants

Protein Variants Comment Organism
A114V naturally occuring mutant involved in CBS deficiency, three-dimensional CBS structure compared to the wild-type enzyme Homo sapiens
D444N naturally occuring mutant involved in CBS deficiency, three-dimensional CBS structure compared to the wild-type enzyme Homo sapiens
E144K naturally occuring mutant involved in CBS deficiency, three-dimensional CBS structure compared to the wild-type enzyme Homo sapiens
G307S naturally occuring mutant involved in CBS deficiency, three-dimensional CBS structure compared to the wild-type enzyme Homo sapiens
I278T naturally occuring mutant involved in CBS deficiency, three-dimensional CBS structure compared to the wild-type enzyme Homo sapiens
R125Q naturally occuring mutant involved in CBS deficiency, three-dimensional CBS structure compared to the wild-type enzyme Homo sapiens
R266K naturally occuring mutant involved in CBS deficiency, three-dimensional CBS structure compared to the wild-type enzyme Homo sapiens
T191M naturally occuring mutant involved in CBS deficiency, three-dimensional CBS structure compared to the wild-type enzyme Homo sapiens
W409_G453del naturally occuring mutant involved in CBS deficiency, three-dimensional CBS structure compared to the wild-type enzyme Homo sapiens

Natural Substrates/ Products (Substrates)

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

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 L-cystathionine + H2O
-
?

Subunits

Subunits Comment Organism
More three-dimensional CBS structure and molecular dynamics simulation of folding process in CBS wild-type and mutants, overview Homo sapiens

Synonyms

Synonyms Comment Organism
CBS
-
Homo sapiens

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Homo sapiens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.6
-
assay at Homo sapiens

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate
-
Homo sapiens

General Information

General Information Comment Organism
malfunction misfolding of mutant enzymes may play an important role in the pathogenesis of cystathionine beta-synthase deficiency, identification of mutant variants in patients with homocystinuria due to CBS deficiency and phenotypes, the topology of mutations predicts in part the behavior of mutant CBS, pathogenic mechanism in CBS deficiency, molecular dynamics simulations, overview Homo sapiens