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

BRENDA support

Literature summary for 3.2.1.21 extracted from

  • Noguchi, J.; Hayashi, Y.; Baba, Y.; Okino, N.; Kimura, M.; Ito, M.; Kakuta, Y.
    Crystal structure of the covalent intermediate of human cytosolic beta-glucosidase (2008), Biochem. Biophys. Res. Commun., 374, 549-552.
    View publication on PubMed
Search for more literature for 3.2.1.21

Crystallization (Commentary)

Crystallization (Comment) Organism
covalent intermediate of mutant E165P, in which glucose is bound to nucleophile E373. Structure confirms a double displacement mechanism Homo sapiens

Protein Variants

Protein Variants Comment Organism
E165P crystallization data of covalent intermediate with substrate, in which glucose is bound to nucleophile E373 Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol
-
 Homo sapiens 5829
-

Organism

Organism UniProt Comment Textmining
Homo sapiens Q9H227
-
-

Reaction

Reaction Comment Organism Reaction ID
celloheptaose + 6 H2O = 7 beta-D-glucose double replacement mechanism, retaining the configuration. A water molecule may be involved in the stabilization of transition states through a sugar 2-hydroxyl oxygen Homo sapiens
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-nitrophenyl beta-D-glucopyranoside + H2O
-
 Homo sapiens 4-nitrophenol + beta-D-glucose
-
 ?

Synonyms

Synonyms Comment Organism
GBA3
-
 Homo sapiens
Klotho-related protein
-
 Homo sapiens
KLrP
-
 Homo sapiens