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EC Number
BRENDA No.
Title
Journal
Volume
Pages
Year
Organism
PubMed ID
3.2.1.130
750913
Contribution of shape and charge to the inhibition of a family GH99 endo-alpha-1,2-mannanase
J. Am. Chem. Soc.
139
1089-1097
2017
Bacteroides xylanisolvens
27992199
3.2.1.130
750913
Contribution of shape and charge to the inhibition of a family GH99 endo-alpha-1,2-mannanase
J. Am. Chem. Soc.
139
1089-1097
2017
Bacteroides xylanisolvens XB1A
27992199
3.2.1.130
750236
Direct assay for endo-alpha-mannosidase substrate preference on correctly folded and misfolded model glycoproteins
Carbohydr. Res.
434
94-98
2016
Homo sapiens
27623439
3.2.1.130
750314
Endo-alpha-mannosidase-catalyzed transglycosylation
ChemBioChem
18
1376-1378
2017
Homo sapiens
28444927
3.2.1.130
750327
Exploration of strategies for mechanism-based inhibitor design for family GH99 endo-alpha-1,2-mannanases
Chemistry
24
7464-7473
2018
Bacteroides xylanisolvens
29508463
3.2.1.130
750327
Exploration of strategies for mechanism-based inhibitor design for family GH99 endo-alpha-1,2-mannanases
Chemistry
24
7464-7473
2018
Bacteroides xylanisolvens XB1A
29508463
3.2.1.130
679134
A single tryptophan residue of endomannosidase is crucial for Golgi localization and in vivo activity
Cell. Mol. Life Sci.
64
1881-1889
2007
Cricetulus griseus
17593322
3.2.1.130
679134
A single tryptophan residue of endomannosidase is crucial for Golgi localization and in vivo activity
Cell. Mol. Life Sci.
64
1881-1889
2007
Rattus norvegicus
17593322
3.2.1.130
646725
Asparagine-linked glycoprotein biosynthesis in rat brain: identification of glucosidase I, glucosidase II, and and endomannosidase (glucosyl mannosidase)
Arch. Biochem. Biophys.
277
114-121
1990
Rattus norvegicus
2407194
3.2.1.130
646725
Asparagine-linked glycoprotein biosynthesis in rat brain: identification of glucosidase I, glucosidase II, and and endomannosidase (glucosyl mannosidase)
Arch. Biochem. Biophys.
277
114-121
1990
Rattus norvegicus Wistar
2407194
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