KEGG ENZYME: 3.2.1.210

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)

SEUB:

DI49_2609

SPAO:

SPAR_H02460

AGO:	AGOS_ADL390W

KLA:	KLLA0_B03608g

KMX:	KLMA_40481(MNL1)

LTH:	KLTH0D17226g

VPO:	Kpol_1000p15

ZRO:	ZYRO0G00528g

CGR:	2887848(GVI51_F08591)

NCS:	NCAS_0A06430(NCAS0A06430)

NDI:	NDAI_0D03410(NDAI0D03410)

TPF:	TPHA_0B00250(TPHA0B00250)

TBL:	TBLA_0E04960(TBLA0E04960)

TGB:	HG536_0C06460

TDL:	TDEL_0D00340(TDEL0D00340)

KAF:	KAFR_0B06970(KAFR0B06970)

KNG:	KNAG_0M00200(KNAG0M00200)

ZMK:	HG535_0H04240

DHA:	DEHA2D06930g

PIC:	PICST_35546(MLN1)

PGU:	PGUG_02459

SPAA:

SPAPADRAFT_135794

LEL:	PVL30_001239

LBG:	92209795(LODBEIA_P45990)

CAL:	CAALFM_C203910CA(CaO19.834)

CTP:	CTRG_01440

COT:	CORT_0A10670

CDU:	CD36_18550

CTEN:

18249520(PSN45_000605)

CLU:	CLUG_00447

CLUS:

A9F13_08g02552

CAUR:

CJI96_0005007

PPA:	PAS_chr3_0891

PKZ:	C5L36_0B03840

BNN:	FOA43_000922

BBRX:

BRETT_004958

OPA:	HPODL_03333

YLI:	2911267(YALI2_D00262g)

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

All links

Gene (41)   
   KEGG ORTHOLOGY (1)   
   KEGG GENES (40)   
All databases (41)   

Download RDF

DBGET integrated database retrieval system