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Literature summary 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

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

Cloned(Commentary)

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

Protein Variants

EC Number Protein Variants Comment Organism
4.2.1.22 A114V naturally occuring mutant involved in CBS deficiency, three-dimensional CBS structure compared to the wild-type enzyme Homo sapiens
4.2.1.22 D444N naturally occuring mutant involved in CBS deficiency, three-dimensional CBS structure compared to the wild-type enzyme Homo sapiens
4.2.1.22 E144K naturally occuring mutant involved in CBS deficiency, three-dimensional CBS structure compared to the wild-type enzyme Homo sapiens
4.2.1.22 G307S naturally occuring mutant involved in CBS deficiency, three-dimensional CBS structure compared to the wild-type enzyme Homo sapiens
4.2.1.22 I278T naturally occuring mutant involved in CBS deficiency, three-dimensional CBS structure compared to the wild-type enzyme Homo sapiens
4.2.1.22 R125Q naturally occuring mutant involved in CBS deficiency, three-dimensional CBS structure compared to the wild-type enzyme Homo sapiens
4.2.1.22 R266K naturally occuring mutant involved in CBS deficiency, three-dimensional CBS structure compared to the wild-type enzyme Homo sapiens
4.2.1.22 T191M naturally occuring mutant involved in CBS deficiency, three-dimensional CBS structure compared to the wild-type enzyme Homo sapiens
4.2.1.22 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)

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

Organism

EC Number Organism UniProt Comment Textmining
4.2.1.22 Homo sapiens P35520
-
-

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 L-cystathionine + H2O
-
 ?

Subunits

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

Synonyms

EC Number Synonyms Comment Organism
4.2.1.22 CBS
-
 Homo sapiens

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
4.2.1.22 37
-
 assay at Homo sapiens

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.2.1.22 8.6
-
 assay at Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
4.2.1.22 pyridoxal 5'-phosphate
-
 Homo sapiens

General Information

EC Number General Information Comment Organism
4.2.1.22 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