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Literature summary for 4.2.1.28 extracted from

  • Tobimatsu, T.; Kawata, M.; Toraya, T.
    The N-terminal regions of beta and gamma subunits lower the solubility of adenosylcobalamin-dependent diol dehydratase (2005), Biosci. Biotechnol. Biochem., 69, 455-462.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
N-terminal truncations (20 or 16 amino acid residues) of either or both of the beta and gamma subunits are expressed on a high level in Escherichia coli. All the mutant enzymes obtained are expressed in a soluble, active form. The mutant enzyme with the N-terminal truncations of both beta and gamma subunits are indistinguishable in catalytic properties from recombinant wild-type enzyme of the enzyme purified from Klebsiella oxytoca in a soluble form Klebsiella oxytoca

General Stability

General Stability Organism
limited proteolysis of the enzyme with trypsin converts the enzyme into a highly soluble form without loss of activity Klebsiella oxytoca

Organism

Organism UniProt Comment Textmining
Klebsiella oxytoca
-
-
-

Subunits

Subunits Comment Organism
hexamer
-
Klebsiella oxytoca