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Literature summary for 3.2.1.74 extracted from

  • Gilkes, N.R.; Warren, A.J.; Miller Jr., R.C.; Kilburn, D.G.
    Precise excision of the cellulose binding domains from two Cellulomonas fimi cellulases by a homologous protease an the effect on catalysis (1988), J. Biol. Chem., 263, 10401-10407.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
Escherichia coli Cellulomonas fimi

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.7
-
p-nitrophenyl-beta-D-cellobioside
-
Cellulomonas fimi

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
47300
-
x * 47300, nonglycosylated form, SDS-PAGE Cellulomonas fimi
49300
-
x * 49300, glycosylated form, SDS-PAGE Cellulomonas fimi

Organism

Organism UniProt Comment Textmining
Cellulomonas fimi
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Cellulomonas fimi

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
p-nitrophenyl-beta-D-cellobioside + H2O
-
Cellulomonas fimi D-glucose + p-nitrophenyl-beta-D-glucoside
-
?

Subunits

Subunits Comment Organism
? x * 47300, nonglycosylated form, SDS-PAGE Cellulomonas fimi
? x * 49300, glycosylated form, SDS-PAGE Cellulomonas fimi