KEGG   ENZYME: 3.2.1.210
Entry
EC 3.2.1.210                Enzyme                                 

Name
endoplasmic reticulum Man8GlcNAc2 1,2-alpha-mannosidase;
MNL1 (gene name)
Class
Hydrolases;
Glycosylases;
Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds
Sysname
Man8GlcNAc2-[protein] 2-alpha-mannohydrolase (configuration-inverting)
Reaction(IUBMB)
Man8GlcNAc2-[protein] (isomer 8A1,2,3B1,3) + H2O = Man7GlcNAc2-[protein] (isomer 7A1,2,3B3) + D-mannopyranose
Substrate
Man8GlcNAc2-[protein] (isomer 8A1,2,3B1,3);
H2O [CPD:C00001]
Product
Man7GlcNAc2-[protein] (isomer 7A1,2,3B3);
D-mannopyranose [CPD:C00159]
Comment
In yeast this activity is catalysed by a dedicated enzyme that processes unfolded protein-bound Man8GlcNAc2 N-glycans within the endoplasmic reticulum to Man7GlcNAc2. The exposed alpha-1,6-linked mannose residue in the product enables the recognition by the YOS9 lectin, targeting the proteins for degradation. In mammalian cells this activity is part of the regular processing of N-glycosylated proteins, and is not associated with protein degradation. It is carried out by EC 3.2.1.113, Golgi mannosyl-oligosaccharide 1,2-alpha-mannosidase. The names of the isomers listed here are based on a nomenclature system proposed by Prien et al [5].
History
EC 3.2.1.210 created 2019
Orthology
K23979  endoplasmic reticulum Man8GlcNAc2 1,2-alpha-mannosidase
Genes
SCE: YHR204W(MNL1)
AGO: AGOS_ADL390W
KLA: KLLA0_B03608g
KMX: KLMA_40481(MNL1)
LTH: KLTH0D17226g
VPO: Kpol_1000p15
ZRO: ZYRO0G00528g
CGR: CAGL0F09053g
NCS: NCAS_0A06430(NCAS0A06430)
NDI: NDAI_0D03410(NDAI0D03410)
TPF: TPHA_0B00250(TPHA0B00250)
TBL: TBLA_0E04960(TBLA0E04960)
TDL: TDEL_0D00340(TDEL0D00340)
KAF: KAFR_0B06970(KAFR0B06970)
PIC: PICST_35546(MLN1)
CAL: CAALFM_C203910CA(CaO19.834)
SLB: AWJ20_4678(MNL1)
 » show all
Reference
1  [PMID:11254655]
  Authors
Nakatsukasa K, Nishikawa S, Hosokawa N, Nagata K, Endo T
  Title
Mnl1p, an alpha -mannosidase-like protein in yeast Saccharomyces cerevisiae, is required for endoplasmic reticulum-associated degradation of glycoproteins.
  Journal
J Biol Chem 276:8635-8 (2001)
DOI:10.1074/jbc.C100023200
  Sequence
[sce:YHR204W]
Reference
2  [PMID:11375935]
  Authors
Jakob CA, Bodmer D, Spirig U, Battig P, Marcil A, Dignard D, Bergeron JJ, Thomas DY, Aebi M
  Title
Htm1p, a mannosidase-like protein, is involved in glycoprotein degradation in yeast.
  Journal
EMBO Rep 2:423-30 (2001)
DOI:10.1093/embo-reports/kve089
  Sequence
[sce:YHR204W]
Reference
3  [PMID:19111666]
  Authors
Quan EM, Kamiya Y, Kamiya D, Denic V, Weibezahn J, Kato K, Weissman JS
  Title
Defining the glycan destruction signal for endoplasmic reticulum-associated degradation.
  Journal
Mol Cell 32:870-7 (2008)
DOI:10.1016/j.molcel.2008.11.017
Reference
4  [PMID:19124653]
  Authors
Clerc S, Hirsch C, Oggier DM, Deprez P, Jakob C, Sommer T, Aebi M
  Title
Htm1 protein generates the N-glycan signal for glycoprotein degradation in the endoplasmic reticulum.
  Journal
J Cell Biol 184:159-72 (2009)
DOI:10.1083/jcb.200809198
  Sequence
[sce:YHR204W]
Reference
5  [PMID:19181540]
  Authors
Prien JM, Ashline DJ, Lapadula AJ, Zhang H, Reinhold VN
  Title
The high mannose glycans from bovine ribonuclease B isomer characterization by ion trap MS.
  Journal
J Am Soc Mass Spectrom 20:539-56 (2009)
DOI:10.1016/j.jasms.2008.11.012
Reference
6  [PMID:21979948]
  Authors
Chantret I, Kodali VP, Lahmouich C, Harvey DJ, Moore SE
  Title
Endoplasmic reticulum-associated degradation (ERAD) and free oligosaccharide generation in Saccharomyces cerevisiae.
  Journal
J Biol Chem 286:41786-800 (2011)
DOI:10.1074/jbc.M111.251371
Other DBs
ExplorEnz - The Enzyme Database: 3.2.1.210
IUBMB Enzyme Nomenclature: 3.2.1.210
ExPASy - ENZYME nomenclature database: 3.2.1.210
BRENDA, the Enzyme Database: 3.2.1.210
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