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Information on EC 3.2.1.113 - mannosyl-oligosaccharide 1,2-alpha-mannosidase and Organism(s) Candida albicans and UniProt Accession Q8J0Q0

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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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Candida albicans
UNIPROT: Q8J0Q0
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The taxonomic range for the selected organisms is: Candida albicans
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
-
(alpha1,2)-mannosidase-I
-
-
-
-
1,2-alpha-mannosidase
-
-
-
-
alpha-1,2-mannosidase
-
-
-
-
alpha-1,2-mannosidase IC
-
-
-
-
alpha1,2-mannosidase
-
-
ER alpha-1,2-mannosidase
-
-
-
-
exo-alpha-1,2-mannanase
-
-
-
-
glycoprotein processing mannosidase I
-
-
-
-
HMIC
-
-
-
-
Man(9)-alpha-mannosidase
-
-
-
-
Man9-mannosidase
-
-
-
-
Man9GlcNAc2-specific processing alpha-mannosidase
-
-
-
-
mannose-9 processing alpha-mannosidase
-
-
-
-
mannosidase 1A
-
-
-
-
mannosidase 1B
-
-
-
-
mannosidase I
-
-
-
-
mannosidase, exo-1,2-alpha-
-
-
-
-
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
4-methylumbelliferyl alpha-D-mannopyranoside + H2O
4-methylumbelliferone + alpha-D-mannopyranose
show the reaction diagram
-
-
-
?
Man9GlcNAc2-Asn + H2O
Man8GlcNAc2-Asn (isomer 8A1,2,3B1,3) + D-mannose
show the reaction diagram
-
-
-
?
4-methylumbelliferyl alpha-D-mannopyranoside + H2O
4-methylumbelliferone + alpha-D-mannopyranose
show the reaction diagram
-
-
-
-
?
Man9GlcNAc2-Asn + 4 H2O
Man5GlcNAc2-Asn + 4 beta-D-mannose
show the reaction diagram
-
-
-
-
?
Man9GlcNAc2-Asn + H2O
Man8GlcNAc2-Asn (isomer 8A1,2,3B1,3) + D-mannose
show the reaction diagram
-
-
-
-
?
additional information
?
-
the enzyme fails to process Man5GlcNAc2-Asn
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-deoxymannojirimycin
-
1-deoxymannojirimycin
-
-
swainsonine
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.07
4-methylumbelliferyl alpha-D-mannopyranoside
at pH 6.0 and 37°C
0.09
4-methylumbelliferyl alpha-D-mannopyranoside
-
at pH 6.0 in 50 mM Tris-MES and at 37°C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.19
1-deoxymannojirimycin
Candida albicans
at pH 6.0 and 37°C
0.62
swainsonine
Candida albicans
at pH 6.0 and 37°C
0.23
1-deoxymannojirimycin
Candida albicans
-
at pH 6.0 in 50 mM Tris-MES and at 37°C
0.47
swainsonine
Candida albicans
-
at pH 6.0 in 50 mM Tris-MES and at 37°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0007
crude enzyme, at pH 6.0 and 37°C
0.1081
after 154fold purification, at pH 6.0 and 37°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
Uniprot
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
the enzyme is involved in the processing of N-linked mannans
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
MNS1_CANAX
565
0
64659
Swiss-Prot
Secretory Pathway (Reliability: 1)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 65000, SDS-PAGE
?
-
x * 52000, SDS-PAGE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
DEAE Bio-Gel A column chromatography and Sephadex G-25 gel filtration
Sepharose CL6B column chromatography, DEAE Bio-Gel A column chromatography, Concanavalin A-Sepharose column chromatography, and Sephadex G-25 gel filtration
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21 Star (DE3) cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Mora-Montes, H.; Lopez-Romero, E.; Zinker, S.; Ponce-Noyola, P.; Flores-Carreon, A.
Purification of soluble alpha1,2-mannosidase from Candida albicans CAI-4
FEMS Microbiol. Lett.
256
50-56
2006
Candida albicans, Candida albicans CAI-4
Manually annotated by BRENDA team
Mora-Montes, H.; Lopez-Romero, E.; Zinker, S.; Ponce-Noyola, P.; Flores-Carreon, A.
Heterologous expression and biochemical characterization of an alpha1,2-mannosidase encoded by the Candida albicans MNS1 gene
Mem. Inst. Oswaldo Cruz
103
724-730
2008
Candida albicans (Q8J0Q0), Candida albicans ATCC 26555 (Q8J0Q0)
Manually annotated by BRENDA team