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Literature summary for 3.2.1.52 extracted from

  • Vanek, O.; Brynda, J.; Hofbauerova, K.; Kukacka, Z.; Pachl, P.; Bezouska, K.; Rezacova, P.
    Crystallization and diffraction analysis of beta-N-acetylhexosaminidase from Aspergillus oryzae (2011), Acta Crystallogr. Sect. F, 67, 498-503.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging-drop vapour-diffusion method, crystals of primitive monoclinic and primitive tetragonal crystal forms, to resolutions of 3.2 and 2.4 A, respectively Aspergillus oryzae

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
8000
-
x * 63000, plus x * 8000, glycosylated enzyme catalytic subunit and noncovalently associated propeptide, SDS-PAGE Aspergillus oryzae
63000
-
x * 63000, plus x * 8000, glycosylated enzyme catalytic subunit and noncovalently associated propeptide, SDS-PAGE Aspergillus oryzae

Organism

Organism UniProt Comment Textmining
Aspergillus oryzae Q8J2T0
-
-
Aspergillus oryzae CCF 1066 Q8J2T0
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Aspergillus oryzae

Source Tissue

Source Tissue Comment Organism Textmining
culture fluid
-
Aspergillus oryzae
-

Subunits

Subunits Comment Organism
? x * 63000, plus x * 8000, glycosylated enzyme catalytic subunit and noncovalently associated propeptide, SDS-PAGE Aspergillus oryzae

Synonyms

Synonyms Comment Organism
NagA
-
Aspergillus oryzae