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4.2.1.22: cystathionine beta-synthase

This is an abbreviated version!
For detailed information about cystathionine beta-synthase, go to the full flat file.

Word Map on EC 4.2.1.22

Reaction

L-serine
+
L-homocysteine
=
L-cystathionine
 +
H2O

Synonyms

Beta-thionase, CBS, CBS424, CDCP2, CNNM2, Cys4, CysB, cystathionine beta synthase, cystathionine beta-synthase, cystathionine beta-synthase domain-containing protein, cystathionine-beta-synthase, Cysteine synthase, EC 4.2.1.21, hCBS, Hemoprotein H-450, LbrM.17.0230, Methylcysteine synthase, osmoprotectant transporter OpuC, PF1953, PH0267, Serine sulfhydrase, Serine sulfhydrylase, Serine sulphhydrase, TA0289, TM0935, TV1335, yCBS, ytCBS

ECTree

     4 Lyases
         4.2 Carbon-oxygen lyases
             4.2.1 Hydro-lyases
                4.2.1.22 cystathionine beta-synthase

Metals Ions

Metals Ions on EC 4.2.1.22 - cystathionine beta-synthase

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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
contains 0.38 Ca atoms/subunit
Co2+
-
97.1% Fe2+ and 2.9% Co2+ in wild-type FeCBS enzyme, 8% Fe2+ and 92% Co2+ in the CoCBS enzyme variant
Co3+
-
cobalt-substituted variant of hCBS, i.e. Co hCBS, in which CoPPIX replaces FePPIX, i.e. heme. Co(III) hCBS is a unique Co-substituted heme protein: the Co(III) ion is 6-coordinate, low-spin, diamagnetic, and bears a cysteine(thiolate) as one of its axial ligands. Electronic absorption and MCD spectra of the Co-substituted heme protein, overview. Co(III) hCBS is slowly reduced to Co(II) hCBS, which contains a 5-coordinate, low-spin, S = 1/2 Co-porphyrin that does not retain the cysteine(thiolate) ligand. This form of Co(II)hCBS binds NO but not CO. Co(II) hCBS is reoxidized in the air to form a new Co(III) form, which does not contain a cysteine(thiolate) ligand. Maintaining the native heme ligation motif of wild-type Fe hCBS (Cys/His) is essential in maintaining maximal activity in Co hCBS
Zn2+
-
contains 0.35 Zn atoms/subunit
additional information