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Literature summary for 2.5.1.151 extracted from

  • Koutmos, M.; Gherasim, C.; Smith, J.; Banerjee, R.
    Structural basis of multifunctionality in a vitamin B 12-processing enzyme (2011), J. Biol. Chem., 286, 29780-29787 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.5.1.151

Cloned(Commentary)

Cloned (Comment) Organism
-
 Homo sapiens

Crystallization (Commentary)

Crystallization (Comment) Organism
crystallization of apo- and cobalamin-bound forms, cocrystallization of truncated CblCDELTAC44 with methylcobalamin, vapor diffusion method Homo sapiens

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
28900
-
 His-tagged recombinant truncated human protein (t-CblC), t-CblC is the predominant, if not only, form of CblC Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens Q9Y4U1
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Homo sapiens

Synonyms

Synonyms Comment Organism
cblC
-
 Homo sapiens

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
41.5
-
 full-length protein CblC Homo sapiens
46.6
-
 truncated protein (t-CblC) Homo sapiens

Cofactor

Cofactor Comment Organism Structure
additional information the enzyme also catalyzes the reductive decyanation of cyanocob(III)alamin in the presence of FMN/FAD and NADPH, cf. EC 1.16.1.6, cyanocobalamin reductase (cyanide-eliminating) Homo sapiens

General Information

General Information Comment Organism
evolution in addition to its dealkylase function, the enzyme also catalyses a decyanase reaction with cyanocobalamin, cf. EC 1.16.1.6, cyanocobalamin reductase (cyanide-eliminating). The enzyme represents an example of evolutionary adaptation of a common structural platform to perform diverse chemistries Homo sapiens