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Literature summary extracted from

  • Zhong, W.; Kuntz, D.A.; Ember, B.; Singh, H.; Moremen, K.W.; Rose, D.R.; Boons, G.J.
    Probing the substrate specificity of Golgi alpha-mannosidase II by use of synthetic oligosaccharides and a catalytic nucleophile mutant (2008), J. Am. Chem. Soc., 130, 8975-8983.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.2.1.114
-
 Drosophila melanogaster
3.2.1.114 mutants D204A and D341N in complex with 2,4-dinitrophenyl-alpha-D-mannopyranoside and in complex with oligosaccharides containing an alpha-(1,6)-or alpha-(1,3)-linked 1-thio-alpha-mannoside Drosophila melanogaster

Protein Variants

EC Number Protein Variants Comment Organism
3.2.1.114 D204A almost complete loss of activity. Residue D204 is involved in the conformational change of the bound mannoside to a high-energy B2,5 conformation. In the mutant, mannose adopts the low-energy 4C1 conformation Drosophila melanogaster
3.2.1.114 D204A mutant of Drosophila melanogaster, residual mannosidase activity Drosophila melanogaster
3.2.1.114 D341N acid-base mutant, residual mannosidase activity Drosophila melanogaster
3.2.1.114 D341N almost complete loss of activity. Substrate mannose is found in a distorted high energy B2,5 conformation, which is necessary for it to fit in the confined space of the binding pocket Drosophila melanogaster

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.2.1.114 mannostatin
-
 Drosophila melanogaster
3.2.1.114 swainsonine
-
 Drosophila melanogaster

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.2.1.114 Golgi apparatus
-
 Drosophila melanogaster 5794
-

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.114 Drosophila melanogaster
-
-
-
3.2.1.114 Drosophila melanogaster Q24451 isoform GMII
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.114
-
 Drosophila melanogaster

Reaction

EC Number Reaction Comment Organism Reaction ID
3.2.1.114 Man5GlcNAc3-[protein] + 2 H2O = Man3GlcNAc3-[protein] + 2 alpha-D-mannopyranose the conformational change of the bound mannoside to a high-energy B2,5 conformation is facilitated by steric hindrance from, and the formation of strong hydrogen bonds to, resiude D204 Drosophila melanogaster
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.114 2,4-dinitrophenyl alpha-D-mannopyranoside + H2O
-
 Drosophila melanogaster ?
-
 ?
3.2.1.114 2,4-dinitrophenyl-alpha-D-mannopyranoside + H2O
-
 Drosophila melanogaster 2,4-dinitrophenol + D-mannose
-
 ?
3.2.1.114 4-methylumbelliferyl alpha-D-mannoside + H2O
-
 Drosophila melanogaster 4-methylumbelliferone + alpha-D-mannose
-
 ?
3.2.1.114 additional information about 80-fold preference of isoform GMII for the cleavage of substrates containing a nonreducing beta-(1,2)-linked GlcNAc group Drosophila melanogaster ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.2.1.114 GmII
-
 Drosophila melanogaster
3.2.1.114 Golgi alpha-mannosidase II
-
 Drosophila melanogaster