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Information on EC 3.2.1.113 - mannosyl-oligosaccharide 1,2-alpha-mannosidase and Organism(s) Homo sapiens and UniProt Accession Q9NR34

for references in articles please use BRENDA:EC3.2.1.113
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IUBMB Comments
This family of mammalian enzymes, located in the Golgi system, participates in the maturation process of N-glycans that leads to formation of hybrid and complex structures. The enzymes catalyse the hydrolysis of the four (1->2)-linked alpha-D-mannose residues from the Man9GlcNAc2 oligosaccharide attached to target proteins as described in reaction (1). Alternatively, the enzymes act on the Man8GlcNAc2 isomer formed by EC 3.2.1.209, endoplasmic reticulum Man9GlcNAc2 1,2-alpha-mannosidase, as described in reaction (2). The enzymes are type II membrane proteins, require Ca2+, and use an inverting mechanism. While all three human enzymes can catalyse the reactions listed here, some of the enzymes can additionally catalyse hydrolysis in an alternative order, generating additional isomeric intermediates, although the final product is the same. The names of the isomers listed here are based on a nomenclature system proposed by Prien et al .
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Homo sapiens
UNIPROT: Q9NR34
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
mania, manic, mannosidase i, man1b1, man1a1, man9-mannosidase, man1c1, man1a2, golgi alpha-mannosidase i, mns1p, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Golgi alpha1,2-mannosidase I
-
ManIC
isoform
(alpha1,2)-mannosidase-I
-
-
-
-
1,2-alpha-mannosidase
-
-
-
-
alpha-(1->2)-mannosidase I
-
alpha-1,2-mannosidase
-
-
-
-
alpha-1,2-mannosidase IC
-
-
-
-
alpha1,2-mannosidase
-
-
alpha1,2-mannosidase I
-
alpha1-2-mannosidase I
-
-
endoplasmic reticulum mannosidase I
-
ER alpha-1,2-mannosidase
-
-
-
-
exo-alpha-1,2-mannanase
-
-
-
-
glycoprotein processing mannosidase I
-
-
-
-
Golgi alpha1,2-mannosidase I
Golgi alpha1,2-mannosidase II
-
-
HMIC
-
-
-
-
Man(9)-alpha-mannosidase
-
-
-
-
Man9-mannosidase
-
-
-
-
Man9GlcNAc2-specific processing alpha-mannosidase
-
-
-
-
ManIA2
isoform
mannose-9 processing alpha-mannosidase
-
-
-
-
mannosidase 1A
-
-
-
-
mannosidase 1B
-
-
-
-
mannosidase I
-
-
-
-
mannosidase, exo-1,2-alpha-
-
-
-
-
MIa,b,c
-
-
MIIx
-
-
N-glycan processing class I alpha-1,2-mannosidase
-
-
-
-
processing alpha-1,2-mannosidase IC
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of O-glycosyl bond
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
Man9GlcNAc2-[protein] alpha-2-mannohydrolase (configuration-inverting)
This family of mammalian enzymes, located in the Golgi system, participates in the maturation process of N-glycans that leads to formation of hybrid and complex structures. The enzymes catalyse the hydrolysis of the four (1->2)-linked alpha-D-mannose residues from the Man9GlcNAc2 oligosaccharide attached to target proteins as described in reaction (1). Alternatively, the enzymes act on the Man8GlcNAc2 isomer formed by EC 3.2.1.209, endoplasmic reticulum Man9GlcNAc2 1,2-alpha-mannosidase, as described in reaction (2). The enzymes are type II membrane proteins, require Ca2+, and use an inverting mechanism. While all three human enzymes can catalyse the reactions listed here, some of the enzymes can additionally catalyse hydrolysis in an alternative order, generating additional isomeric intermediates, although the final product is the same. The names of the isomers listed here are based on a nomenclature system proposed by Prien et al [7].
CAS REGISTRY NUMBER
COMMENTARY hide
9068-25-1
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
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)GlcNAcbeta-2-pyridylamine + H2O
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)GlcNAcbeta-2-pyridylamine + D-mannose
show the reaction diagram
-
-
-
?
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)GlcNAcbeta-2-pyridylamine + H2O
Manalpha(1->3)[Manalpha(1->2)Manalpha(1->6)[Manalpha(1->2)Manalpha(1->3)]Manalpha(1->6)]Manbeta(1->4)GlcNAcbeta(1->4)GlcNAcbeta-2-pyridylamine + D-mannose
show the reaction diagram
-
-
-
?
Manalpha(1->3)[Manalpha(1->2)Manalpha(1->6)[Manalpha(1->2)Manalpha(1->3)]Manalpha(1->6)]Manbeta(1->4)GlcNAcbeta(1->4)GlcNAcbeta-2-pyridylamine + H2O
Manalpha(1->3)[Manalpha(1->6)[Manalpha(1->2)Manalpha(1->3)]Manalpha(1->6)]Manbeta(1->4)GlcNAcbeta(1->4)GlcNAcbeta-2-pyridylamine + D-mannose
show the reaction diagram
-
-
-
?
Manalpha(1->3)[Manalpha(1->6)[Manalpha(1->2)Manalpha(1->3)]Manalpha(1->6)]Manbeta(1->4)GlcNAcbeta(1->4)GlcNAcbeta-2-pyridylamine + H2O
Manalpha(1->3)[Manalpha(1->6)[Manalpha(1->3)]Manalpha(1->6)]Manbeta(1->4)GlcNAcbeta(1->4)GlcNAcbeta-2-pyridylamine + 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-N-Asn-[protein] + 4 H2O
alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-alpha-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn-[protein] + 4 beta-D-mannopyranose
show the reaction diagram
-
-
-
-
?
Man9GlcNAc2 + H2O
Man8GlcNAc2 (isomer 8A1,2,3B1,3) + D-mannose
show the reaction diagram
Man9GlcNAc2-Asn + H2O
Man8GlcNAc2-Asn (isomer 8A1,2,3B1,3) + D-mannose
show the reaction diagram
-
-
-
?
Man9GlcNAc2-pyridylamine + H2O
Man8GlcNAc2-pyridylamine (isomer 8A1,2,3B1,3) + 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
-
-
products are Man5-8GlcNAc, with Man6GlcNAc being major product
?
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)GlcNAcbeta(1-4)GlcNAc + H2O
(Man)6(GlcNAc)2 + D-mannose
show the reaction diagram
-
i.e. (Man)9(GlcNAc)2
-
-
?
Manalpha(1-6)(Manalpha(1-3))Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + H2O
(Man)5(GlcNAc)2-Asn + D-mannose
show the reaction diagram
-
i.e. GPIV
major product formed, 3.5 mol mannose/mol GP IV per h, i.e. GPI
?
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)GlcNAcbeta-2-pyridylamine + H2O
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)GlcNAcbeta-2-pyridylamine + D-mannose
show the reaction diagram
-
-
-
?
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)GlcNAcbeta-2-pyridylamine + H2O
Manalpha(1->3)[Manalpha(1->2)Manalpha(1->6)[Manalpha(1->2)Manalpha(1->3)]Manalpha(1->6)]Manbeta(1->4)GlcNAcbeta(1->4)GlcNAcbeta-2-pyridylamine + D-mannose
show the reaction diagram
-
-
-
?
Manalpha(1->3)[Manalpha(1->2)Manalpha(1->6)[Manalpha(1->2)Manalpha(1->3)]Manalpha(1->6)]Manbeta(1->4)GlcNAcbeta(1->4)GlcNAcbeta-2-pyridylamine + H2O
Manalpha(1->3)[Manalpha(1->6)[Manalpha(1->2)Manalpha(1->3)]Manalpha(1->6)]Manbeta(1->4)GlcNAcbeta(1->4)GlcNAcbeta-2-pyridylamine + D-mannose
show the reaction diagram
-
-
-
?
Manalpha(1->3)[Manalpha(1->6)[Manalpha(1->2)Manalpha(1->3)]Manalpha(1->6)]Manbeta(1->4)GlcNAcbeta(1->4)GlcNAcbeta-2-pyridylamine + H2O
Manalpha(1->3)[Manalpha(1->6)[Manalpha(1->3)]Manalpha(1->6)]Manbeta(1->4)GlcNAcbeta(1->4)GlcNAcbeta-2-pyridylamine + 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
Man9GlcNAc2 + H2O
Man8GlcNAc2 (isomer 8A1,2,3B1,3) + D-mannose
show the reaction diagram
Man9GlcNAc2-Asn + H2O
Man8GlcNAc2-Asn (isomer 8A1,2,3B1,3) + D-mannose
show the reaction diagram
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
required for activity. Optimum concentration 1.5 mM or 15 mM. Isoform ManIC is stable in the absence of Ca2+, even though Ca2+ is also effective for activity
Zn2+
the activity of isoform ManIC is 94% in the presence of 15 mM Zn2+ and 50% in the presence of 1.5 mM Zn2+ compared with that of the original solution
additional information
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-deoxymannojirimycin
no activity at 0.01 mM
kifunensine
no activity at 0.01 mM
swainsonine
isoform ManIC shows 86% activity at 0.5 mM swainsonine
1-deoxymannojirimycin
deoxymannojirimycin
-
EDTA
the enzyme inhibition by EDTA can be reversed by the addition of Ca2+ and to a lesser extent by Fe2+ and Mn2+
EGTA
the enzyme inhibition by EGTA can be reversed by the addition of Ca2+ and to a lesser extent by Fe2+ and Mn2+
kifunensine
additional information
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 6.5
isoform ManIC
6.5 - 7
isoform ManIA2
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 8
the enzyme is active between pH 6.0 and 8.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35
isoform ManIC
37
-
assay at
40
isoform ManIA2
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
HepG2, HepG2.2.15, AD38, and N10
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
aberrant regulation of alpha-1,2 mannosidases can result in cancer. MAN1C1 plays a role in tumor suppression in hepatocarcinogenesis. Down-regulation of MAN1C activates unfolded protein response during hepatocarcinogenesis
metabolism
overexpression MAN1C1 shows anti-tumor effect by inducing apoptosis. MAN1C1 overexpression remarkably increases the ratio of Bax/Bcl-2 and inhibits epithelial-mesenchymal transition by increasing the expression of E-CA. In addition, the ratio of Bax/Bcl-2 and E-cadherin is increased in MAN1C1 gene overexpression renal cancer cells compared with the control cells
physiological function
key enzymes in N-glycosylation is required for the formation of mature glycoproteins in eukaryotes. MAN1C1 plays a role in tumor suppression in hepatocarcinogenesis. Down-regulation of MAN1C activates unfolded protein response during hepatocarcinogenesis
malfunction
metabolism
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
MA1C1_HUMAN
630
1
70911
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
58000
x * 58000, SDS-PAGE
58000
x * 58000, SDS-PAGE
71000
-
x * 71000, deduced from gene sequence, type-II transmembrane protein
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 58000, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
-
three potential N-glycosylation sites, one of which is used
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with kifunensine
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
up
hepatitis B virus upregulates host expression of class I alpha-1,2-mannosidases via the PPARalpha pathway. Hepatitis B virus increases the expression of alpha-mannosidases both in vitro and in vivo via activation of the PPARalpha pathway by its envelope protein
D463N
the mutant shows 0.1% of wild type catalytic efficiency
D463N/E599Q
the mutant shows 0.0003% of wild type catalytic efficiency
E330Q
the mutant shows 3.5% of wild type catalytic efficiency
E330Q/E599Q
the mutant shows 0.006% of wild type catalytic efficiency
E599Q
the mutant shows 0.0005% of wild type catalytic efficiency
up
hepatitis B virus upregulates host expression of class I alpha-1,2-mannosidases via the PPARalpha pathway. Hepatitis B virus increases the expression of alpha-mannosidases both in vitro and in vivo via activation of the PPARalpha pathway by its envelope protein
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 6
isoform ManIC is stable (more than 75% activity) in the pH range of 5.5-6.0 at 37°C for 90 min
715684
6.5 - 8
isoform ManIA2 is stable (more than 75% activity) in the pH range of 6.5-8.0 at 37°C for 90 min
715684
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
isoform ManIC shows more than 75% activity at 40°C in the absence and presence of Ca2+
20 - 30
isoform ManIA2 shows more than 75% activity at 30°C in the presence of Ca2+, and more than 75% activity at 20°C in the absence of Ca2+
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Talon Co2+ affinity resin column chromatography
IgG-Sepharose bead chromatography
partial
-
Talon Co2+ affinity resin column chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli JM109 (DE3) cells
MAN1C1 gene over-expression is used to transfect human renal cancer cell lines 786-O and OS-RC-2
enzyme-protein A-fusion protein is expressed in COS cells
expressed in Escherichia coli JM109 (DE3) cells
expressed in HEK-293 cells
-
expression in Escherichia coli
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
increased expression after anti-CD3 stimulation
-
T cell receptor signaling enhances mRNA levels of MIa,b,c
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
diagnostics
MAN1C1 may be a useful prognostic biomarker and potential therapeutic target in clear cell renal cell carcinoma, with the potential to lead to better outcomes for patients with these poor prognosis malignancies
medicine
the class I alpha-mannosidases can be used as drug targets to inhibit the demannosylation of HBV, thereby improving the binding of the virus to DC-SIGN and disrupting the immune tolerance to prevent and treat viral infection
drug development
-
development of anti-cancer therapies
medicine
the class I alpha-mannosidases can be used as drug targets to inhibit the demannosylation of HBV, thereby improving the binding of the virus to DC-SIGN and disrupting the immune tolerance to prevent and treat viral infection
pharmacology
in triple KO (MAN1A1, MAN1A2, and MAN1B1) cells, Man9GlcNAc2 and Man8GlcNAc2 are the major N-glycan structures. The N-glycan structures on recombinant proteins expressed in triple KO cells are simplified and changed from complex types to high-mannose types at the protein level. The triple KO HEK293 cells are suitable for producing recombinant proteins, including lysosomal enzymes with high-mannose-type N-glycans. This approach should accelerate the production of biopharmaceutical proteins with homogenous glycans
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Porwoll, S.; Fuchs, H.; Tauber, R.
Characterization of a soluble class I alpha-mannosidase in human serum
FEBS Lett.
449
175-178
1999
Homo sapiens
Manually annotated by BRENDA team
Chandrasekaran, E.V.; Savila, M.; Nixon, D.; Mendicino, J.
Purification and properties of alpha-D-mannose:beta-1,2-N-acetylglucosaminyl-transferases and alpha-D-mannosidases from human adenocarcinoma
Cancer Res.
44
4059-4068
1984
Homo sapiens
Manually annotated by BRENDA team
Shah, N.; Kuntz, D.A.; Rose, D.R.
Comparison of kifunensine and 1-deoxymannojirimycin binding to class I and II alpha-mannosidases demonstrates different saccharide distortions in inverting and retaining catalytic mechanisms
Biochemistry
42
13812-13816
2003
Homo sapiens
Manually annotated by BRENDA team
Bause E.;Bieberich E.;Rolfs A.;Volker C.;Schmidt B.
Molecular cloning and primary structure of Man9-mannosidase from human kidney
Eur. J. Biochem.
217
535-40
1993
Homo sapiens
Manually annotated by BRENDA team
Lu, Y.; Xu, Y.Y.; Fan, K.Y.; Shen, Z.H.
1-Deoxymannojirimycin, the alpha1,2-mannosidase inhibitor, induced cellular endoplasmic reticulum stress in human hepatocarcinoma cell 7721
Biochem. Biophys. Res. Commun.
344
221-225
2006
Homo sapiens
Manually annotated by BRENDA team
Chen, H.L.; Li, C.F.; Grigorian, A.; Tian, W.; Demetriou, M.
T cell receptor signaling co-regulates multiple Golgi genes to enhance N-glycan branching
J. Biol. Chem.
284
32454-32461
2009
Homo sapiens
Manually annotated by BRENDA team
Isoyama-Tanaka, J.; Dohi, K.; Misaki, R.; Fujiyama, K.
Improved expression and characterization of recombinant human Golgi alpha1,2-mannosidase I isoforms (IA2 and IC) by Escherichia coli
J. Biosci. Bioeng.
112
14-19
2011
Homo sapiens (O60476), Homo sapiens (Q9NR34)
Manually annotated by BRENDA team
Tu, H.C.; Hsiao, Y.C.; Yang, W.Y.; Tsai, S.L.; Lin, H.K.; Liao, C.Y.; Lu, J.W.; Chou, Y.T.; Wang, H.D.; Yuh, C.H.
Up-regulation of Golgi alpha-mannosidase IA and down-regulation of Golgi alpha-mannosidase IC activates unfolded protein response during hepatocarcinogenesis
Hepatol. Commun.
1
230-247
2017
Homo sapiens (P33908), Homo sapiens (Q9NR34)
Manually annotated by BRENDA team
Jin, Z.C.; Kitajima, T.; Dong, W.; Huang, Y.F.; Ren, W.W.; Guan, F.; Chiba, Y.; Gao, X.D.; Fujita, M.
Genetic disruption of multiple alpha1,2-mannosidases generates mammalian cells producing recombinant proteins with high-mannose-type N-glycans
J. Biol. Chem.
293
5572-5584
2018
Homo sapiens (O60476), Homo sapiens (P33908), Homo sapiens (Q9UKM7)
Manually annotated by BRENDA team
Li, H.; Wang, G.; Yu, Y.; Jian, W.; Zhang, D.; Wang, Y.; Wang, T.; Meng, Y.; Yuan, C.; Zhang, C.
alpha-1,2-Mannosidase MAN1C1 inhibits proliferation and invasion of clear cell renal cell carcinoma
J. Cancer
9
4618-4626
2018
Homo sapiens (Q9NR34), Homo sapiens
Manually annotated by BRENDA team
Hu, S.; Jiang, L.B.; Zou, X.J.; Yi, W.; Tian, D.Y.
Hepatitis B virus upregulates host expression of alpha-1,2-mannosidases via the PPARalpha pathway
World J. Gastroenterol.
22
9534-9543
2016
Homo sapiens (O60476), Homo sapiens (P33908), Homo sapiens (Q9NR34), Homo sapiens (Q9UKM7), Homo sapiens
Manually annotated by BRENDA team
Cantu, D.; Nerinckx, W.; Reilly, P.
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)
Manually annotated by BRENDA team
Gonzalez, D.; Karaveg, K.; Vandersall-Nairn, A.; Lal, A.; Moremen, K.
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
Hosokawa, N.; Tremblay, L.; You, Z.; Herscovics, A.; Wada, I.; Nagata, K.
Enhancement of endoplasmic reticulum (ER) degradation of misfolded null Hong Kong alpha1-antitrypsin by human ER mannosidase I
J. Biol. Chem.
278
26287-26294
2003
Homo sapiens
Manually annotated by BRENDA team
Fujiyama, K.; Sakuradani, S.; Moran, D.G.; Yoshida, T.; Seki, T.
Effect of alpha-1,2-mannosidic linkage located in a alpha1,3-branch of Man6GlcNAc2 oligosaccharide on enzyme activity of recombinant human Man9-mannosidase produced in Escherichia coli
J. Biosci. Bioeng.
91
419-421
2001
Homo sapiens
Manually annotated by BRENDA team