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Literature summary for 3.2.1.176 extracted from

  • Stahlberg, J.; Divne, C.; Koivula, A.; Piens, K.; Claeyssens, M.; Teeri, T.T.; Jones, T.A.
    Activity studies and crystal structures of catalytically deficient mutants of cellobiohydrolase I from Trichoderma reesei (1996), J. Mol. Biol., 264, 337-349.
    View publication on PubMed
Search for more literature for 3.2.1.176

Crystallization (Commentary)

Crystallization (Comment) Organism
engineered enzymes Trichoderma reesei

Protein Variants

Protein Variants Comment Organism
D214N impaired catalytic activity Trichoderma reesei
E212Q impaired catalytic activity Trichoderma reesei
E217Q impaired catalytic activity Trichoderma reesei

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.46
-
 2-chloro-4-nitrophenyl-beta-lactoside
-
 Trichoderma reesei
0.57
-
 2-chloro-4-nitrophenyl-beta-lactoside D214N Trichoderma reesei
0.68
-
 2-chloro-4-nitrophenyl-beta-lactoside E212Q Trichoderma reesei
0.78
-
 2-chloro-4-nitrophenyl-beta-lactoside E217Q Trichoderma reesei

Organism

Organism UniProt Comment Textmining
Trichoderma reesei
-
 CBH I
-
Trichoderma reesei CBH I
-
 CBH I
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-chloro-4-nitrophenyl-beta-lactoside
-
 Trichoderma reesei ?
-
 ?
2-chloro-4-nitrophenyl-beta-lactoside
-
 Trichoderma reesei CBH I ?
-
 ?