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Information on EC 3.2.1.209 - endoplasmic reticulum Man9GlcNAc2 1,2-alpha-mannosidase and Organism(s) Homo sapiens and UniProt Accession Q9UKM7

for references in articles please use BRENDA:EC3.2.1.209
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IUBMB Comments
The enzyme, located in the endoplasmic reticulum, primarily trims a single alpha-1,2-linked mannose residue from Man9GlcNAc2 to produce Man8GlcNAc2 isomer 8A1,2,3B1,3 (the names of the isomers listed here are based on a nomenclature system proposed by Prien et al ). The removal of the single mannosyl residue occurs in all eukaryotes as part of the processing of N-glycosylated proteins, and is absolutely essential for further elongation of the outer chain of properly-folded N-glycosylated proteins in yeast. In addition, the enzyme is involved in glycoprotein quality control at the ER quality control compartment (ERQC), helping to target misfolded glycoproteins for degradation. When present at very high concentrations in the ERQC, the enzyme can trim the carbohydrate chain further to Man(5-6)GlcNAc2.
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Homo sapiens
UNIPROT: Q9UKM7
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The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Synonyms
edem1, ermani, edem3, er mannosidase i, alpha1,2-mannosidases, alpha1,2-mannosidase e-i, er mani, er alpha1,2-mannosidase i, class i alpha1,2-mannosidase, endoplasmic reticulum alpha1,2-mannosidase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
alpha-mannosidase
Class 1 mannosidases, CAZy GH family 47
endoplasmic reticulum alpha-(1-->2)-mannosidase I
-
alpha-(1,2)-mannosidase I
-
-
class I alpha1,2-mannosidase
-
-
EDEM1
-
-
endoplasmic reticulum mannosidase I
-
-
ER alpha1,2-mannosidase I
-
-
ER degradation enhancing alpha-mannosidase-like protein 1
-
-
ER ManI
-
-
ER mannosidase I
-
-
ERManI
Golgi alpha1,2-mannosidase IC
-
-
MAN1B1
-
-
-
-
mannosyl oligosaccharide, alpha 1,2-mannosidase
-
-
MNS1
-
-
-
-
MNS3
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of O-glycosyl bond
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -
SYSTEMATIC NAME
IUBMB Comments
Man9GlcNAc2-[protein]2-alpha-mannohydrolase (configuration-inverting)
The enzyme, located in the endoplasmic reticulum, primarily trims a single alpha-1,2-linked mannose residue from Man9GlcNAc2 to produce Man8GlcNAc2 isomer 8A1,2,3B1,3 (the names of the isomers listed here are based on a nomenclature system proposed by Prien et al [7]). The removal of the single mannosyl residue occurs in all eukaryotes as part of the processing of N-glycosylated proteins, and is absolutely essential for further elongation of the outer chain of properly-folded N-glycosylated proteins in yeast. In addition, the enzyme is involved in glycoprotein quality control at the ER quality control compartment (ERQC), helping to target misfolded glycoproteins for degradation. When present at very high concentrations in the ERQC, the enzyme can trim the carbohydrate chain further to Man(5-6)GlcNAc2.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-O-alpha-D-mannopyranosyl-alpha-D-mannopyranose + H2O
2 alpha-D-mannose
show the reaction diagram
-
-
-
?
alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-alpha-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-2-pyridylamine + H2O
alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-alpha-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-2-pyridylamine + D-mannopyranose
show the reaction diagram
alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,6)]-alpha-D-mannopyranosyl-(1,6)]-beta-D-mannopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranose + H2O
alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,6)]-alpha-D-mannopyranosyl-(1,6)]-beta-D-mannopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranose + D-mannose
show the reaction diagram
-
-
-
?
alpha1-antitrypsin NHK + H2O
? + D-mannose
show the reaction diagram
substrate is a variant of alpha1-antitrypsin and substrate for ER-associated degradation of misfolded proteins
-
-
?
human alpha1-antitrypsin genetic variant null + H2O
? + D-mannose
show the reaction diagram
substrate misfolds following biosynthesis
-
-
?
Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)[Manalpha(1-2)Manalpha(1-6)[Manalpha(1-2)Manalpha(1-3)]Manalpha(1-6)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + H2O
Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)[Manalpha(1-6)[Manalpha(1-2)Manalpha(1-3)]Manalpha(1-6)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + alpha-D-mannose
show the reaction diagram
-
-
-
?
Manalpha(1-2)Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manalpha(1-6)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAc + 4 H2O
(Man)5GlcNAc + 4 D-mannose
show the reaction diagram
-
product is Man8GlcNAc
?
alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,6)]-alpha-D-mannopyranosyl-(1,6)]-beta-D-mannopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranose + H2O
alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,6)]-alpha-D-mannopyranosyl-(1,6)]-beta-D-mannopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranose + D-mannose
show the reaction diagram
-
-
-
-
?
alpha1-antitrypsin null (Hong Kong) + H2O
? + D-mannose
show the reaction diagram
-
-
-
-
?
alpha1-antitrypsin null + H2O
? + D-mannose
show the reaction diagram
-
-
-
-
?
alpha1-antitrypsin null + H2O
alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,6)]-alpha-D-mannopyranosyl-(1,6)]-beta-D-mannopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranose + D-mannose
show the reaction diagram
-
-
-
-
?
alpha1-antitrypsin null + H2O
alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,6)]-alpha-D-mannopyranosyl-(1,6)]-beta-D-mannopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranose + D-mannose
show the reaction diagram
-
-
-
-
?
alpha1-antitrypsin null + H2O
alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,6)]-alpha-D-mannopyranosyl-(1,6)]-beta-D-mannopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranose + D-mannose
show the reaction diagram
-
-
-
-
?
alpha1-antitrypsin null + H2O
alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,6)]-alpha-D-mannopyranosyl-(1,6)]-beta-D-mannopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranose + D-mannose
show the reaction diagram
-
-
-
-
?
alpha1-antitrypsin null + H2O
alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,6)]-alpha-D-mannopyranosyl-(1,6)]-beta-D-mannopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranose + D-mannose
show the reaction diagram
-
overexpression of each Golgi alpha1,2-mannosidase enhances alpha1-antitrypsin null degradation and trimming of its N-glycans to alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,6)]-alpha-D-mannopyranosyl-(1,6)]-beta-D-mannopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranose
-
-
?
Glcalpha(1-3)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)[Manalpha(1-2)Manalpha(1-3)[Manalpha(1-2)Manalpha(1-6)]Manalpha(1-6)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + H2O
Glcalpha(1-3)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)[Manalpha(1-2)Manalpha(1-3)[Manalpha(1-6)]Manalpha(1-6)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + D-mannose
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-alpha-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-2-pyridylamine + H2O
alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-alpha-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-2-pyridylamine + D-mannopyranose
show the reaction diagram
-
-
-
?
alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,6)]-alpha-D-mannopyranosyl-(1,6)]-beta-D-mannopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranose + H2O
alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,6)]-alpha-D-mannopyranosyl-(1,6)]-beta-D-mannopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranose + D-mannose
show the reaction diagram
-
-
-
-
?
alpha1-antitrypsin null + H2O
? + D-mannose
show the reaction diagram
-
-
-
-
?
additional information
?
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-deoxymannojirimycin
EDTA
Ca2+ restores
EGTA
complete loss of acvtivity at 0.1 mM, Ca2+ restores
kifunensine
1-deoxymannojirimycin
-
found in crystal structures of the active site
brefeldin A
-
known inhibitor of vesicle transport, ablated intracellular turnover of the radiolabeled molecules. Plus digestion with potato acid phosphatase implies that phosphorylation of ER mannosidase I is responsible for the altered electrophoretic mobility
Chloroquine
-
lysosomotrophic amine capable of raising the pH of acidic intracellular compartments, added to the medium with weak inhibition
kifunensine
lactacystin
-
irreversible inhibitor of multicatalytic proteasomes, only a minor effect on the disappearance of radiolabeled human ER mannosidase I
leupeptin
-
lysosomal protease inhibitor, intracellular turnover of pulse-radiolabeled recombinant human ER mannosidase I is substantially inhibited
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.015 - 0.51
alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-alpha-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-2-pyridylamine
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000026 - 3.7
alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-alpha-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-2-pyridylamine
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.3
mutant enzyme E330Q
6.5
mutant enzyme T688A, R461A and R461L
6.6
mutant enzyme E330Q/E599Q and D463N/E599Q
6.7
mutant enzyme E599Q
6.9
mutant enzyme H524A
7.1
wild-type enzyme
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
malfunction
-
endoplasmic reticulum mannosidase I knockdown does not affect binding of an endoplasmic reticulum-associated degradation substrate glycoprotein to EDEM1
physiological function
-
endoplasmic reticulum mannosidase I activity is not required for association of H2a with EDEM1
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
MA1B1_HUMAN
699
1
79580
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
79000
-
Western blotting of cell lysates, transiently expressed recombinant human ER mannosidase I is absent from mock transfected cells but detected as a single immunoreactive 79 kDa band following transient expression
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 82000, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
co-complex with an uncleaved thiodisaccharide substrate analog, hanging drop vapor diffusion method
docking studies
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D463N
D463N/E599Q
pH-optimum is 6.6 compared to 7.1 for wild-type enzyme, kcat/Km is 8.3fold lower than wild-type value
E330Q
E330Q/E599Q
pH-optimum is 6.6 compared to 7.1 for wild-type enzyme, kcat/Km is 340000fold lower than wild-type value
E599Q
F659A
H524A
pH-optimum is 6.9 compared to 7.1 for wild-type enzyme, kcat/Km is 28.3fold lower than wild-type value
R334A
mutant enzyme is not detected in the culture medium, kcat/Km is 28.3fold lower than wild-type value
R461A
R461L
R597A
T688A
E220Q
-
the mutant contains a conserved acidic amino acid mutation that abolishes alpha1,2-mannosidase enzyme activity
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Pichia pastoris
overexpressed in HEK-293 cells
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
homozygosity for the minor A allele rs4567(A), but not rs4567(G), suppresses ERManI translation under endoplasmic reticulum stress conditions
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Gonzalez, D.S.; Karaveg, K.; Vandersall-Nairn, A.S.; Lal, A.; Moremen, K.W.
Identification, expression, and characterization of a cDNA encoding human endoplasmic reticulum mannosidase I, the enzyme that catalyzes the first mannose trimming step in mammalian Asn-linked oligosaccharide biosynthesis
J. Biol. Chem.
274
21375-21386
1999
Homo sapiens (Q9UKM7), Homo sapiens
Manually annotated by BRENDA team
Lobsanov, Y.D.; Vallee, F.; Imberty, A.; Yoshida, T.; Yip, P.; Herscovics, A.; Howell, P.L.
Structure of Penicillium citrinum alpha-1,2-mannosidase reveals the basis for differences in specificity of the endoplasmic reticulum and golgi class I enzymes
J. Biol. Chem.
277
5620-5630
2002
Homo sapiens (Q9UKM7), Homo sapiens, Saccharomyces cerevisiae (P32906), Saccharomyces cerevisiae
Manually annotated by BRENDA team
Karaveg, K.; Siriwardena, A.; Tempel, W.; Liu, Z.; Glushka, J.; Wang, B.; Moremen, K.W.
Mechanism of class 1 (glycosylhydrolase family 47) alpha-mannosidases involved in N-glycan processing and endoplasmic reticulum quality control
J. Biol. Chem.
280
16197-16207
2005
Homo sapiens (Q9UKM7)
Manually annotated by BRENDA team
Karaveg, K.; Moremen, K.W.
Energetics of substrate binding and catalysis by class 1 (glycosylhydrolase family 47) alpha-mannosidases involved in N-glycan processing and endoplasmic reticulum quality control
J. Biol. Chem.
280
29837-29848
2005
Homo sapiens (Q9UKM7)
Manually annotated by BRENDA team
Hosokawa, N.; You, Z.; Tremblay, L.O.; Nagata, K.; Herscovics, A.
Stimulation of ERAD of misfolded null Hong Kong alpha1-antitrypsin by Golgi alpha1,2-mannosidases
Biochem. Biophys. Res. Commun.
362
626-632
2007
Homo sapiens, Mus musculus (P39098), Mus musculus (P45700)
Manually annotated by BRENDA team
Mulakala, C.; Nerinckx, W.; Reilly, P.J.
The fate of beta-D-mannopyranose after its formation by endoplasmic reticulum alpha-(1-->2)-mannosidase I catalysis
Carbohydr. Res.
342
163-169
2007
Homo sapiens, Saccharomyces cerevisiae (P32906), Saccharomyces cerevisiae
Manually annotated by BRENDA team
Wu, Y.; Termine, D.J.; Swulius, M.T.; Moremen, K.W.; Sifers, R.N.
Human endoplasmic reticulum mannosidase I is subject to regulated proteolysis
J. Biol. Chem.
282
4841-4849
2007
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Mast, S.W.; Moremen, K.W.
Family 47 alpha-mannosidases in N-glycan processing
Methods Enzymol.
415
31-46
2006
Saccharomyces cerevisiae (P32906), Homo sapiens (Q9UKM7)
Manually annotated by BRENDA team
Cantu, D.; Nerinckx, W.; Reilly, P.J.
Theory and computation show that Asp463 is the catalytic proton donor in human endoplasmic reticulum alpha-(1-->2)-mannosidase I
Carbohydr. Res.
343
2235-2242
2008
Homo sapiens (Q9UKM7), Homo sapiens
Manually annotated by BRENDA team
Hosokawa, N.; Tremblay, L.O.; Sleno, B.; Kamiya, Y.; Wada, I.; Nagata, K.; Kato, K.; Herscovics, A.
EDEM1 accelerates the trimming of alpha1,2-linked mannose on the C branch of N-glycans
Glycobiology
20
567-575
2010
Homo sapiens
Manually annotated by BRENDA team
Pan, S.; Huang, L.; McPherson, J.; Muzny, D.; Rouhani, F.; Brantly, M.; Gibbs, R.; Sifers, R.N.
Single nucleotide polymorphism-mediated translational suppression of endoplasmic reticulum mannosidase I modifies the onset of end-stage liver disease in alpha1-antitrypsin deficiency
Hepatology
50
275-281
2009
Homo sapiens
Manually annotated by BRENDA team
Rafiq, M.; Kuss, A.; Puettmann, L.; Noor, A.; Ramiah, A.; Ali, G.; Hu, H.; Kerio, N.; Xiang, Y.; Garshasbi, M.; et al
Mutations in the alpha 1,2-mannosidase gene, MAN1B1, cause autosomal-recessive intellectual disability
Am. J. Hum. Genet.
89
176-182
2011
Homo sapiens
Manually annotated by BRENDA team
Groisman, B.; Shenkman, M.; Ron, E.; Lederkremer, G.Z.
Mannose trimming is required for delivery of a glycoprotein from EDEM1 to XTP3-B and to late endoplasmic reticulum-associated degradation steps
J. Biol. Chem.
286
1292-1300
2011
Homo sapiens
Manually annotated by BRENDA team
Hosokawa, N.; Kamiya, Y.; Kamiya, D.; Kato, K.; Nagata, K.
Human OS-9, a lectin required for glycoprotein ERAD, recognizes mannose-trimmed N-glycans
J. Biol. Chem.
284
17061-17068
2009
Mus musculus (Q2HXL6), Homo sapiens (Q9UKM7), Homo sapiens
Manually annotated by BRENDA team
Termine, D.J.; Moremen, K.W.; Sifers, R.N.
The mammalian UPR boosts glycoprotein ERAD by suppressing the proteolytic downregulation of ER mannosidase I
J. Cell Sci.
122
976-984
2009
Homo sapiens (Q9UKM7)
Manually annotated by BRENDA team