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Information on EC 3.2.1.106 - mannosyl-oligosaccharide glucosidase and Organism(s) Homo sapiens

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IUBMB Comments
This enzyme catalyses the first step in the processing of the N-glycan tetradecasaccharide precursor Glc3Man9GlcNAc2, which takes place in the endoplasmic reticulum, by removing the distal alpha-1,2-linked glucose residue. This and subsequent processing steps are required before complex N-glycans can be synthesized.
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This record set is specific for:
Homo sapiens
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Synonyms
acid alpha-glucosidase, rhgaa, glucosidase i, alpha-glucosidase i, cwh41, knopf, tggaa, processing alpha-glucosidase i, mannosyl-oligosaccharide glucosidase, cwh41p, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
(Glc3)-glucosidase
-
-
-
-
acid alpha-glucosidase
-
-
alpha-glucosidase I
-
-
-
-
Glc I
-
-
-
-
Glc3 oligosaccharide glucosidase
-
-
-
-
Glc3-glucosidase
-
-
-
-
Glc3-oligosaccharide glucosidase
-
-
-
-
Glc3-OS-glucosidase
-
-
-
-
Glc3Man9GlcNAc2 oligosaccharide glucosidase
-
-
-
-
Glc3Man9NAc2 oligosaccharide glucosidase
-
-
-
-
glucosidase 1
-
-
glucosidase I
glucosidase, mannosyloligosaccharide
-
-
-
-
glucosidase-1
-
-
-
-
glycoengineered acid alpha-glucosidase
-
-
mannosyl-oligosaccharide glucosidase
-
-
MOGS
-
-
oxime-neo-rhGAA
-
-
processing alpha-glucosidase I
-
-
-
-
processing exoglucosidase I
-
-
-
-
processing glucosidase I
-
-
-
-
rhGAA
-
-
trimming enzyme I
-
-
-
-
trimming glucosidase I
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of O-glycosyl bond
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -
SYSTEMATIC NAME
IUBMB Comments
Glc3Man9GlcNAc2-[protein] glucohydrolase (configuration-inverting)
This enzyme catalyses the first step in the processing of the N-glycan tetradecasaccharide precursor Glc3Man9GlcNAc2, which takes place in the endoplasmic reticulum, by removing the distal alpha-1,2-linked glucose residue. This and subsequent processing steps are required before complex N-glycans can be synthesized.
CAS REGISTRY NUMBER
COMMENTARY hide
78413-07-7
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-methylumbelliferyl-alpha-D-glucopyranoside + H2O
4-methylumbelliferone + alpha-D-glucose
show the reaction diagram
-
4°C, pH 6.25
-
-
?
Glc3Man9GlcNAc2 + H2O
?
show the reaction diagram
Glc3Man9GlcNAc2 + H2O
D-glucose + Glc2Man9GlcNAc2
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
Glc3Man9GlcNAc2 + H2O
?
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-deoxynojirimycin
castanospermine
-
-
deoxynojirimycin
-
-
N,N-dimethyl-1-deoxynojirimycin
N-butyldeoxynojirimycin
-
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
-
50% increased Km-Value of the modified 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
additional information
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
-
genetic defects in the gene encoding mannosyl-oligosaccharide glucosidase cause the rare congenital disorder of glycosylation type IIb
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
MOGS_HUMAN
837
1
91918
Swiss-Prot
Mitochondrion (Reliability: 3)
A0A384MDR6_HUMAN
837
1
91918
TrEMBL
Mitochondrion (Reliability: 3)
A0A3B3IRI7_HUMAN
113
0
12287
TrEMBL
other Location (Reliability: 5)
A0A8I5KQG9_HUMAN
479
1
52903
TrEMBL
Mitochondrion (Reliability: 3)
Q58F09_HUMAN
837
1
91907
TrEMBL
Mitochondrion (Reliability: 3)
A0A3B3IS52_HUMAN
428
1
46485
TrEMBL
Mitochondrion (Reliability: 3)
A0A8I5KTK5_HUMAN
739
1
81401
TrEMBL
Mitochondrion (Reliability: 3)
B8ZZE2_HUMAN
209
1
22492
TrEMBL
Mitochondrion (Reliability: 3)
C9JDQ1_HUMAN
145
0
15925
TrEMBL
other Location (Reliability: 2)
A0A3B3ITU6_HUMAN
208
1
22646
TrEMBL
Mitochondrion (Reliability: 3)
A0A3B3ITC1_HUMAN
294
1
31960
TrEMBL
Mitochondrion (Reliability: 3)
A0A3B3IRK6_HUMAN
715
1
78574
TrEMBL
Secretory Pathway (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
92000
-
calculated from nucleotide sequence
93000
-
enzyme of 95000 Da degraded by endoglycosidase H, SDS-PAGE
95000
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
additional information
-
chemical conjucation of synthetic oligosaccharides bearing M6P residues, neo-rhGAA
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D404N
-
same mutant as D518N
D518N
-
same mutant as D404N
additional information
-
variant oxime-neo-rhGAA, content of mannose-6-phosphat residues increased, higher affinity for the cation-independent mannose 6-phosphate receptor
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
for 14 days, higher stability of the modified enzyme
4
-
for 90 days, higher stability of the modified enzyme
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cDNA, overexpression in COS 1 cells
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
-
treatment of Pompe Disease
pharmacology
-
glucosidase I may be a target for antiviral and antitumor drugs, glucosidase I inhibitors are potentially useful as antiviral, antitumor and antimetastatic agents
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Herscovics, A.
Importance of glycosidases in mammalian glycoprotein biosynthesis
Biochim. Biophys. Acta
1473
96-107
1999
Homo sapiens, Mammalia
Manually annotated by BRENDA team
Kalz-Fuller, B.; Bieberich, E.; Bause, E.
Cloning and expression of glucosidase I from human hippocampus
Eur. J. Biochem.
231
344-351
1995
Homo sapiens, Sus scrofa
Manually annotated by BRENDA team
Kalz-Fuller, B.; Heidrich-Kaul, C.; Nthen, M; Bause, E.; Schwanitz, G.
Localization of the human glucosidase I gene to chromosome 2p12-p13 by fluorescence in situ hybridization and PCR analysis of somatic cell hybrids
Genomics
34
442-443
1996
Homo sapiens
Manually annotated by BRENDA team
Bause, E.; Schweden, J.; Gross, A.; Orthen, B.
Purification and characterization of trimming glucosidase I from pig liver
Eur. J. Biochem.
183
661-669
1989
Bos taurus, Homo sapiens, Sus scrofa
Manually annotated by BRENDA team
Ruddock, L.W.; Molinari, M.
N-glycan processing in ER quality control
J. Cell Sci.
119
4373-4380
2006
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Zhu, Y.; Jiang, J.L.; Gumlaw, N.K.; Zhang, J.; Bercury, S.D.; Ziegler, R.J.; Lee, K.; Kudo, M.; Canfield, W.M.; Edmunds, T.; Jiang, C.; Mattaliano, R.J.; Cheng, S.H.
Glycoengineered Acid alpha-Glucosidase With Improved Efficacy at Correcting the Metabolic Aberrations and Motor Function Deficits in a Mouse Model of Pompe Disease
Mol. Ther.
17
954-963
2009
Homo sapiens
Manually annotated by BRENDA team
Sadat, M.A.; Moir, S.; Chun, T.W.; Lusso, P.; Kaplan, G.; Wolfe, L.; Memoli, M.J.; He, M.; Vega, H.; Kim, L.J.; Huang, Y.; Hussein, N.; Nievas, E.; Mitchell, R.; Garofalo, M.; Louie, A.; Ireland, D.C.; Grunes, C.; Cimbro, R.; Patel, V.; Holzapfel, G.; Salahuddin, D.; Bristol, T.; Adams, D.; Marciano, B.E.
Glycosylation, hypogammaglobulinemia, and resistance to viral infections
N. Engl. J. Med.
370
1615-1625
2014
Homo sapiens
Manually annotated by BRENDA team