Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Tsukada, T.; Igarashi, K.; Fushinobu, S.; Samejima, M.
    Role of subsite +1 residues in pH dependence and catalytic activity of the glycoside hydrolase family 1 beta-glucosidase BGL1A from the basidiomycete Phanerochaete chrysosporium (2008), Biotechnol. Bioeng., 99, 1295-1302.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
3.2.1.21 D229N site-directed mutagenesis, mutation of the isozyme BGL1A residue from subsite +1 to the correspondent residue of isozyme BGL1B, the mutant shows decreased catalytic efficiency compared to the wild-type BGL1A Phanerodontia chrysosporium
3.2.1.21 D229N/K253A site-directed mutagenesis, mutation of the isozyme BGL1A residues from subsite +1 to the correspondent residues of isozyme BGL1B, the double mutant has a hydrolytic activity at neutral pH that is restored to that of the wild-type enzyme Phanerodontia chrysosporium
3.2.1.21 H231D site-directed mutagenesis, mutation of the isozyme BGL1A residue from subsite +1 to the correspondent residue of isozyme BGL1B, the mutant shows decreased catalytic efficiency compared to the wild-type BGL1A Phanerodontia chrysosporium
3.2.1.21 K253A site-directed mutagenesis, mutation of the isozyme BGL1A residue from subsite +1 to the correspondent residue of isozyme BGL1B, the mutant shows decreased catalytic efficiency compared to the wild-type BGL1A Phanerodontia chrysosporium
3.2.1.21 M177L site-directed mutagenesis, mutation of the isozyme BGL1A residue from subsite +1 to the correspondent residue of isozyme BGL1B, the mutant shows catalytic efficiency similar to the wild-type BGL1A Phanerodontia chrysosporium
3.2.1.21 V173C site-directed mutagenesis, mutation of the isozyme BGL1A residue from subsite +1 to the correspondent residue of isozyme BGL1B, the mutant shows catalytic efficiency similar to the wild-type BGL1A Phanerodontia chrysosporium

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2.1.21 6.8
-
cellobiose pH 6.5, wild-type isozyme BGL1A Phanerodontia chrysosporium
3.2.1.21 9.22
-
cellobiose pH 6.5, mutant M177L Phanerodontia chrysosporium
3.2.1.21 13.3
-
cellobiose pH 6.5, mutant V173C Phanerodontia chrysosporium
3.2.1.21 21
-
cellobiose pH 6.5, mutant H231D Phanerodontia chrysosporium
3.2.1.21 46.5
-
cellobiose pH 6.5, mutant K253A Phanerodontia chrysosporium
3.2.1.21 114
-
cellobiose pH 6.5, mutant D229N Phanerodontia chrysosporium

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.2.1.21 cellobiose + H2O Phanerodontia chrysosporium
-
2 beta-D-glucose
-
?

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.21 Phanerodontia chrysosporium Q25BW4 isozyme BGL1B; gene bgl1B, isozyme BGL1B
-
3.2.1.21 Phanerodontia chrysosporium Q25BW5 isozyme BGL1A; gene bgl1A, isozyme BGL1A
-

Reaction

EC Number Reaction Comment Organism Reaction ID
3.2.1.21 celloheptaose + 6 H2O = 7 beta-D-glucose the putative acid/base catalyst is Glu170 Phanerodontia chrysosporium

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.21 cellobiose + H2O
-
Phanerodontia chrysosporium 2 beta-D-glucose
-
?

Subunits

EC Number Subunits Comment Organism
3.2.1.21 More molecular modeling and amino acid sequence analysis of isozyme BGL1A, residues V173, M177, D229, H231, K253 are involved in formation of subsite +1 responsible for substrate recognition, overview Phanerodontia chrysosporium

Synonyms

EC Number Synonyms Comment Organism
3.2.1.21 BGL1A
-
Phanerodontia chrysosporium
3.2.1.21 BGL1B
-
Phanerodontia chrysosporium
3.2.1.21 More the enzyme belongs to the glycoside hydrolase family 1 Phanerodontia chrysosporium

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.2.1.21 2.53
-
cellobiose pH 6.5, mutant M177L Phanerodontia chrysosporium
3.2.1.21 3.23
-
cellobiose pH 6.5, mutant D229N Phanerodontia chrysosporium
3.2.1.21 3.94
-
cellobiose pH 6.5, mutant H231D Phanerodontia chrysosporium
3.2.1.21 4.35
-
cellobiose pH 6.5, mutant V173C Phanerodontia chrysosporium
3.2.1.21 4.47
-
cellobiose pH 6.5, mutant K253A Phanerodontia chrysosporium
3.2.1.21 181
-
cellobiose pH 6.5, wild-type isozyme BGL1A Phanerodontia chrysosporium

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.21 5.5
-
mutant D229N Phanerodontia chrysosporium
3.2.1.21 6
-
mutants V173C and D229N/K253A Phanerodontia chrysosporium
3.2.1.21 6.5
-
wild-type BGL1A, and mutants M177L, H231D, and K253A Phanerodontia chrysosporium

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.2.1.21 4.5 8 pH-profile of wild-type and mutant isozymes BGL1A, overview Phanerodontia chrysosporium
3.2.1.21 4.5 8 pH-profile of wild-type isozyme BGL1B, overview Phanerodontia chrysosporium