Literature summary for 3.2.1.114 extracted from

Kuntz, D.A.; Liu, H.; Bols, M.; Rose, D.R.
The role of the active site Zn in the catalytic mechanism of the GH38 Golgi alpha -mannosidase II: implications from noeuromycin inhibition (2006), Biocatal. Biotransform., 24, 55-61.

No PubMed abstract available

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Application

Application	Comment	Organism
drug development	development of specific inhibitors of GMII that can lead to novel anti-metastatic or anti-inflammatory compounds	Drosophila melanogaster

Inhibitors

Inhibitors	Comment	Organism	Structure
noeuromycin	-	Drosophila melanogaster

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Zn2+	GMII contains a Zn atom which forms contacts with substrate analogues, stabilizes catalytic intermediates, and other inhibitors observed in the active site	Drosophila melanogaster

Organism

Organism	UniProt	Comment	Textmining
Drosophila melanogaster	-	-	-

Synonyms

Synonyms	Comment	Organism
GH38 Golgi alpha-mannosidase II	-	Drosophila melanogaster
GmII	-	Drosophila melanogaster
Golgi alpha-mannosidase II	-	Drosophila melanogaster

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Release 2023.1 (January 2023)