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Literature summary for 4.2.1.22 extracted from

  • Majtan, T.; Pey, A.L.; Fernandez, R.; Fernandez, J.A.; Martinez-Cruz, L.A.; Kraus, J.P.
    Domain organization, catalysis and regulation of eukaryotic cystathionine beta-synthases (2014), PLoS ONE, 9, e105290 .
    View publication on PubMedView publication on EuropePMC
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Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Drosophila melanogaster
expression in Escherichia coli Homo sapiens
expression in Escherichia coli Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Drosophila melanogaster
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Homo sapiens
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Saccharomyces cerevisiae
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-

General Information

General Information Comment Organism
physiological function comparison of human, fruit fly and yeast enzymes. The fruit fly CBS and yeast CBS are not regulated by the allosteric activator of human CBS, S-adenosyl-L-methionine. The heme-containing Drosophila melanogaster CBS and human CBS show increased thermal stability and retention of the enzyme's catalytic activity Drosophila melanogaster
physiological function comparison of human, fruit fly and yeast enzymes. Truncation of human CBS and yeast CBS, i.e. deletion of the regulatory domains, results in enzyme activation and formation of dimers compared to native tetramers The fruit fly CBS and yeast CBS are not regulated by the allosteric activator of human CBS, S-adenosyl-L-methionine. compared to the yeast CBS, the heme-containing Drosophila melanogaster CBS and human CBS show increased thermal stability and retention of the enzyme's catalytic activity Saccharomyces cerevisiae
physiological function comparison of human, fruit fly and yeast enzymes. Truncation of human CBS and yeast CBS, i.e. deletion of the regulatory domains, results in enzyme activation and formation of dimers compared to native tetramers. Only the human enzyme is regulated by S-adenosylmethionine. The heme-containing Drosophila melanogaster CBS and human CBS show increased thermal stability and retention of the enzyme's catalytic activity Homo sapiens