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Literature summary for 3.2.1.176 extracted from

  • Borisova, A.S.; Eneyskaya, E.V.; Bobrov, K.S.; Jana, S.; Logachev, A.; Polev, D.E.; Lapidus, A.L.; Ibatullin, F.M.; Saleem, U.; Sandgren, M.; Payne, C.M.; Kulminskaya, A.A.; Stahlberg, J.
    Sequencing, biochemical characterization, crystal structure and molecular dynamics of cellobiohydrolase Cel7A from Geotrichum candidum 3C (2015), FEBS J., 282, 4515-4537.
    View publication on PubMed
Search for more literature for 3.2.1.176

Crystallization (Commentary)

Crystallization (Comment) Organism
structures, with and without bound thio-oligosaccharides, show conformational diversity of tunnel-enclosing loops, including a form with partial tunnel collapse at subsite -4 Geotrichum candidum

Inhibitors

Inhibitors Comment Organism Structure
cellobiose
-
 Geotrichum candidum

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.84
-
 2-chloro-4-nitrophenyl beta-D-cellobioside catalyticdomain, pH 5.0, 37°C Geotrichum candidum
0.85
-
 4-nitrophenyl beta-D-cellobioside catalyticdomain, pH 5.0, 37°C Geotrichum candidum
1.07
-
 4-nitrophenyl beta-D-lactoside catalyticdomain, pH 5.0, 37°C Geotrichum candidum

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
 Geotrichum candidum
-
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
46000
-
 x * 75000, full-length enzyme, x * 46000, catalytic domain, SDS-PAGE Geotrichum candidum
75000
-
 x * 75000, full-length enzyme, x * 46000, catalytic domain, SDS-PAGE Geotrichum candidum

Organism

Organism UniProt Comment Textmining
Geotrichum candidum A0A088T0J9
-
-
Geotrichum candidum 3C A0A088T0J9
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein the crystal structures show attached N-glycans at two of the predicted N-glycosylation sites (Asn57 and Asn206) and also at Asn432 near the C terminus of the catalytic domain. O-glycosylation at Ser196 is indicated by electron density, on a loop where the glycan probably influences loop contacts across the active site and interactions with the cellulose surface Geotrichum candidum
proteolytic modification the encoded preprotein consists of 535 amino acids, divided into a 17-residue signal peptide followed by a GH7 catalytic module of about 436 residues, a Ser/Thr-rich linker region of about 47 residues, and finally a C-terminal CBM1 of about 35 residues Geotrichum candidum

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1860
-
 substrate carboxymethyl cellulose, pH 5.0, 37°C Geotrichum candidum
1910
-
 substrate lichenan, pH 5.0, 37°C Geotrichum candidum
2150
-
 substrate avicel, pH 5.0, 37°C Geotrichum candidum
40000
-
 substrate bacterial cellulose, pH 5.0, 37°C Geotrichum candidum
275000
-
 substrate phosphoric acid swollen cellulose, pH 5.0, 37°C Geotrichum candidum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-chloro-4-nitrophenyl beta-D-cellobioside + H2O
-
 Geotrichum candidum 2-chloro-4-nitrophenol + D-cellobiose
-
 ?
2-chloro-4-nitrophenyl beta-D-cellobioside + H2O
-
 Geotrichum candidum 3C 2-chloro-4-nitrophenol + D-cellobiose
-
 ?
4-nitrophenyl beta-D-cellobioside
-
 Geotrichum candidum 4-nitrophenol + D-cellobiose
-
 ?
4-nitrophenyl beta-D-cellobioside
-
 Geotrichum candidum 3C 4-nitrophenol + D-cellobiose
-
 ?
4-nitrophenyl beta-D-lactoside
-
 Geotrichum candidum 4-nitrophenol + beta-D-lactose
-
 ?
avicel + H2O
-
 Geotrichum candidum cellobiose + ?
-
 ?
avicel + H2O
-
 Geotrichum candidum 3C cellobiose + ?
-
 ?
bacterial cellulose + H2O
-
 Geotrichum candidum cellobiose + ?
-
 ?
carboxymethyl cellulose + H2O
-
 Geotrichum candidum cellobiose + ?
-
 ?
carboxymethyl cellulose + H2O
-
 Geotrichum candidum 3C cellobiose + ?
-
 ?
lichenan + H2O
-
 Geotrichum candidum cellobiose + ?
-
 ?
microcrystalline cellulose + H2O
-
 Geotrichum candidum cellobiose + ?
-
 ?
additional information no substrate: beechwood xylan Geotrichum candidum ?
-
 ?
additional information no substrate: beechwood xylan Geotrichum candidum 3C ?
-
 ?
phosphoric acid swollen cellulose + H2O
-
 Geotrichum candidum cellobiose + ?
-
 ?

Subunits

Subunits Comment Organism
? x * 75000, full-length enzyme, x * 46000, catalytic domain, SDS-PAGE Geotrichum candidum

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
50
-
-
 Geotrichum candidum

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
60
-
 1 h, 45% residual activity Geotrichum candidum

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.1
-
 4-nitrophenyl beta-D-cellobioside catalyticdomain, pH 5.0, 37°C Geotrichum candidum
0.11
-
 2-chloro-4-nitrophenyl beta-D-cellobioside catalyticdomain, pH 5.0, 37°C Geotrichum candidum
0.19
-
 4-nitrophenyl beta-D-lactoside catalyticdomain, pH 5.0, 37°C Geotrichum candidum

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5
-
-
 Geotrichum candidum

pH Range

pH Minimum pH Maximum Comment Organism
4 6.5 more than 85% of maximum activity Geotrichum candidum

pH Stability

pH Stability pH Stability Maximum Comment Organism
4 7 24 h, 37°C, stable Geotrichum candidum

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.05
-
 cellobiose catalyticdomain, pH 5.0, 37°C Geotrichum candidum

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.118
-
 4-nitrophenyl beta-D-cellobioside catalyticdomain, pH 5.0, 37°C Geotrichum candidum
0.131
-
 2-chloro-4-nitrophenyl beta-D-cellobioside catalyticdomain, pH 5.0, 37°C Geotrichum candidum
0.178
-
 4-nitrophenyl beta-D-lactoside catalyticdomain, pH 5.0, 37°C Geotrichum candidum