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Information on EC 3.2.1.113 - mannosyl-oligosaccharide 1,2-alpha-mannosidase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P32906

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EC Tree
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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Saccharomyces cerevisiae
UNIPROT: P32906
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The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
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
(alpha1,2)-mannosidase-I
-
-
-
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1,2-alpha-mannosidase
-
-
-
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alpha-(1->2)-mannosidase I
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alpha-1,2-mannosidase
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-
-
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alpha-1,2-mannosidase IC
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-
-
-
alpha1,2-mannosidase
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-
ER alpha-1,2-mannosidase
-
-
-
-
exo-alpha-1,2-mannanase
-
-
-
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glycoprotein processing mannosidase I
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-
-
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HMIC
-
-
-
-
Man(9)-alpha-mannosidase
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-
-
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Man9 processing alpha-mannosidase
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-
Man9-alpha-mannosidase
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-
Man9-mannosidase
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-
-
-
Man9GlcNAc2-specific processing alpha-mannosidase
-
-
-
-
mannose-9 processing alpha-mannosidase
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-
-
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mannosidase 1A
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-
-
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mannosidase 1B
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-
-
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mannosidase I
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-
-
-
mannosidase, exo-1,2-alpha-
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-
-
-
N-glycan processing class I alpha-1,2-mannosidase
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-
-
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processing alpha-1,2-mannosidase IC
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-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Man9GlcNAc2-[protein] + 4 H2O = Man5GlcNAc2-[protein] + 4 beta-D-mannopyranose
show the reaction diagram
model for substrate and conformer selectivity, mechanism, computational study
-
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
Glc3Man9GlcNAc2 from oligosaccharide-lipid + H2O
?
show the reaction diagram
-
good substrate
-
-
?
lipid-linked Man7GlcNAc2 (isomer 7A1,3B1,3) + H2O
?
show the reaction diagram
-
10% activity compared to Man9GlcNAc2
-
-
?
Man9GlcNAc2 + H2O
Man8GlcNAc2 (isomer 8A1,2,3B1,3) + D-mannose
show the reaction diagram
-
-
-
-
?
Man9GlcNAc2-[thyroglobulin] + H2O
Man8GlcNAc2-[thyroglobulin] + D-mannose
show the reaction diagram
-
good substrate
-
-
?
additional information
?
-
-
the enzyme does not hydrolyze invertase Man9GlcNAc, Manlalpha2ManlalphaOCH3 or 4-nitrophenyl alpha-D-mannopyranoside
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-
?
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
-
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
0.01 mM Ca2+ stimulates the enzyme activity to 77%, while 0.1 mM Ca2+ restores nearly 90% of the original activity
Zn2+
-
0.1 mM Zn2+ stimulates the enzyme activity by 30%
additional information
-
not stimulated by Mg2+ or Mn2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
EGTA
-
complete inhibition at 5 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.2
Man9GlcNAc2-[thyroglobulin]
-
at pH 6.5, temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
model for substrate and conformer specificity, computational study
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 6.8
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50% of the enzyme activity remains at pH 6.0 and 6.8, and activity falls off rapidly above and below these values
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.3
-
isoelectric focusing
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
66000
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 63000, SDS-PAGE
heterodimer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
-
-
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
trypsin digestion of intact, osmotically supported membranes has no effect on the subsequent release of active enzyme by CHAPS, while digestion in the presence of CHAPS with trypsin at only 0.01 mg/ml inactivates more than 80% of the enzyme during the 1 h incubation
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
25°C, in 1 mM CHAPS at pH 6.5-6.7, several days, about 50% loss of activity
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4°C, in 1 mM CHAPS at pH 6.5-6.7, several weeks, no loss of activity
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Q-Sepharose column chromatography and TSK 3000 matrix gel filtration
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Mulakala, C.; Reilly, P.J.
Understanding protein structure-function relationships in family 47 a-1,2-mannosidases through computational docking of ligands
Proteins Struct. Funct. Genet.
49
125-134
2002
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Mulakala, C.; Nerinckx, W.; Reilly, P.
The fate of beta-D-mannopyranose after its formation by endoplasmic reticulum alpha-(1->2)-mannosidase I catalysis
Carbohydr. Res.
342
163-169
2007
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Massaad, M.; Franzusoff, A.; Herscovics, A.
The processing alpha1,2-mannosidase of Saccharomyces cerevisiae depends on Rer1p for its localization in the endoplasmic reticulum
Eur. J. Cell Biol.
78
435-440
1999
Saccharomyces cerevisiae, Saccharomyces cerevisiae TH2-lOD
Manually annotated by BRENDA team
Ziegler, F.; Trimble, R.
Glycoprotein biosynthesis in yeast Purification and characterization of the endoplasmic reticulum Man9 processing alpha-mannosidase
Glycobiology
1
605-612
1991
Saccharomyces cerevisiae
Manually annotated by BRENDA team