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Literature summary extracted from

  • Meier, M.; Oliveriusova, J.; Kraus, J.P.; Burkhard, P.
    Structural insights into mutations of cystathionine beta-synthase (2003), Biochim. Biophys. Acta, 1647, 206-213.
    View publication on PubMed

Application

EC Number Application Comment Organism
4.2.1.22 medicine inherited deficiency leads to homocystinura, a disease of sulfur metabolism characterized by increased levels of homocysteine and methionine and decreased levels of cysteine Homo sapiens

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.2.1.22
-
 Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
4.2.1.22 A114V mutation in dimer interface of patients with homocystinurea, variable amounts of residual activity Homo sapiens
4.2.1.22 A114V mutation in the heme binding site of patients with homocystinurea Homo sapiens
4.2.1.22 A226T mutation in the connecting loop between the N- and C-terminal domain between beta-strand 7 and alpha-helix 6, patients respond to vitamin B6 treatment Homo sapiens
4.2.1.22 A331V mutation effects can be suppressed in a yeast assay by the deletion of the regulatory domain of the protein Homo sapiens
4.2.1.22 E176K mutation in dimer interface of patients with homocystinurea Homo sapiens
4.2.1.22 E176K mutation in dimer interface of patients with homocystinurea, patients do not respond to vitamin B6 treatment, mutant forms high molecular wight aggregates devoid of heme after expression in Escherichia coli Homo sapiens
4.2.1.22 G116R mutation in dimer interface of patients with homocystinurea Homo sapiens
4.2.1.22 G148R active site mutation in patients with homocystinurea Homo sapiens
4.2.1.22 G259S active site mutation in patients with homocystinurea Homo sapiens
4.2.1.22 G305R active site mutation in patients with homocystinurea Homo sapiens
4.2.1.22 G307S active site mutation in patients with homocystinurea Homo sapiens
4.2.1.22 I278T located in the middle of beta-strand 9 and the beta-sheet of the C-terminal domain, effects of this mutation can be suppressed when expressed in yeast by certain point mutations in the regulatory domain or by complete deletion of the C-terminal region Homo sapiens
4.2.1.22 N228K active site mutation in patients with homocystinurea Homo sapiens
4.2.1.22 N228S active site mutation in patients with homocystinurea Homo sapiens
4.2.1.22 P78R mutation in dimer interface of patients with homocystinurea Homo sapiens
4.2.1.22 P88S mutation in dimer interface of patients with homocystinurea Homo sapiens
4.2.1.22 R224H mutation in the connecting loop between the N- and C-terminal domain between beta-strand 7 and alpha-helix 6, patients respond to vitamin B6 treatment Homo sapiens
4.2.1.22 R336C mutation causes a mild disease type Homo sapiens
4.2.1.22 R336C mutation in dimer interface of patients with homocystinurea Homo sapiens
4.2.1.22 R336H mutation causes a mild disease type Homo sapiens
4.2.1.22 R336H mutation in dimer interface of patients with homocystinurea Homo sapiens
4.2.1.22 R58W mutation in the heme binding site of patients with homocystinurea, reduced ability to bind heme Homo sapiens
4.2.1.22 S352N patients with this mutation are not vitamin B6 responsive Homo sapiens
4.2.1.22 T257M active site mutation in patients with homocystinurea Homo sapiens
4.2.1.22 T353M mutation effects can be suppressed in a yeast assay by the deletion of the regulatory domain of the protein, patients with this mutation are not vitamin B6 responsive Homo sapiens
4.2.1.22 V180A mutation in dimer interface of patients with homocystinurea Homo sapiens
4.2.1.22 V354M patients with this mutation are not vitamin B6 responsive Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
4.2.1.22 Homo sapiens
-
 patients with homocystinuria
-

Substrates and Products (Substrate)

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