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Literature summary for 4.2.1.22 extracted from

  • Majtan, T.; Freeman, K.M.; Smith, A.T.; Burstyn, J.N.; Kraus, J.P.
    Purification and characterization of cystathionine beta-synthase bearing a cobalt protoporphyrin (2011), Arch. Biochem. Biophys., 508, 25-30.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 4.2.1.22

Activating Compound

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

Cloned(Commentary)

Cloned (Comment) Organism
expression of wild-type and Co-subsituted CBS as GST-tagged enzymes in Escherichia coli strain Rosetta 2 (DE3) Homo sapiens

Protein Variants

Protein Variants Comment Organism
additional information construction of a cobalt CBS, CoCBS, by metalloporphyrin replacement, which results in a high yield of fully active, high purity enzyme, in which heme is substituted by Co-protoporphyrin IX, CoPPIX. The enzyme contains 92% cobalt and 8% iron. CoCBS is indistinguishable from wild-type FeCBS in its activity, tetrameric oligomerization, PLP saturation and responsiveness to the allosteric activator, S-adenosyl-L-methionine Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ 97.1% Fe2+ and 2.9% Co2+ in wild-type FeCBS enzyme, 8% Fe2+ and 92% Co2+ in the CoCBS enzyme variant Homo sapiens
Fe2+ heme enzyme, 97.1% Fe2+ and 2.9% Co2+ in wild-type FeCBS enzyme, 8% Fe2+ and 92% Co2+ in the CoCBS enzyme variant Homo sapiens
additional information construction of a cobalt CBS, CoCBS, by metalloporphyrin replacement, which results in a high yield of fully active, high purity enzyme, in which heme is substituted by Co-protoporphyrin IX, CoPPIX. the enzyme contains 92% cobalt and 8% iron. CoCBS is indistinguishable from wild-type FeCBS in its activity, tetrameric oligomerization, PLP saturation and responsiveness to the allosteric activator, S-adenosyl-L-methionine Homo sapiens

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
63000
-
 4 * 63000 Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant GST-tagged wild-type and Co-subsituted CBS from Escherichia coli strain Rosetta 2 (DE3) by glutathione affinity and anion exchange chromatography Homo sapiens

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
 cystathionine synthesis activity of FeCBS and CoCBS Homo sapiens
105.2
-
 purified recombinant CoCBS, pH 8.6, 37°C Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the enzyme performs L-cysteine sythesis from L-serine Homo sapiens ?
-
 ?

Subunits

Subunits Comment Organism
homotetramer 4 * 63000 Homo sapiens
More each subunit has a modular structure consisting of three domains: an N-terminal heme binding domain, a highly conserved pyridoxal 5'-phosphate-binding catalytic core, and a S-adenosyl-L-methionine-binding C-terminal regulatory domain 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
heme
-
 Homo sapiens
pyridoxal 5'-phosphate i.e. PLP, serves in the catalytic chemistry of CBS via a well-established mechanism Homo sapiens

General Information

General Information Comment Organism
metabolism cystathionine beta-synthase is a pivotal enzyme in the metabolism of homocysteine, and is a pyridoxal 5'-phosphate-dependent enzyme that also contains heme as a second cofactor Homo sapiens