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Information on EC 3.2.1.113 - mannosyl-oligosaccharide 1,2-alpha-mannosidase and Organism(s) Penicillium citrinum and UniProt Accession P31723

for references in articles please use BRENDA:EC3.2.1.113
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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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Penicillium citrinum
UNIPROT: P31723
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The taxonomic range for the selected organisms is: Penicillium citrinum
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
-
-
-
-
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
-
-
-
-
fungal alpha-1,2-mannosidase
-
-
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
Man9GlcNAc2 + H2O
Man8GlcNAc2 (isomer 8A1,2,3B1,3) + D-mannose
show the reaction diagram
-
-
-
?
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+
inhibitors kifunensine and 1-deoxymannojirimycin bind to the essential Ca2+ ion
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-deoxymannojirimycin
modeling of binding to enzyme
kifunensine
modeling of binding to enzyme
1-deoxymannojirimycin
-
methyl-alpha-D-lyxopyranosyl-(1',2)-alpha-D-mannopyranoside
analogue of the minimal disaccharide substrate mannobiose. Cocrystallization and mass spectrometry data suggest that when methyl-alpha-D-lyxopyranosyl-(1',2)-alpha-D-mannopyranoside is incubated with the mannosidase for long periods of time it is cleaved and that methyl-alpha-D-lyxopyranosyl-(1',2)-alpha-D-mannopyranoside behaves as a substrate
additional information
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.6
methyl-alpha-D-lyxopyranosyl-(1',2)-alpha-D-mannopyranoside
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
comparison of the molecular structure of the Penicillium citrinum Golgi enzyme, and yeast and human endoplasmic reticulum enzymes. There is a greater degree of freedom to bind the oligosaccharide in the active site of the fungal enzyme than in the yeast and human ER alpha1,2-mannosidases
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
MAN12_PENCI
511
0
56570
Swiss-Prot
Secretory Pathway (Reliability: 2)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
x-ray crystallography
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with the substrate analogue methyl-alpha-D-lyxopyranosyl-(1',2)-alpha-D-mannopyranoside, to 1.95 A resolution. The intact disaccharide spans the ?1/+1 subsites, with the D-lyxoside ring in the -1 subsite in the 1C4 chair conformation.The absence of the C5' hydroxymethyl group on the D-lyxoside moiety results in the side chain of Arg407 adopting two alternative conformations, the minor one interacting with Asp375 and the major one interacting with both the D-lyxoside and the catalytic base Glu409, thus disrupting its function
modeling of structure at 2.2 A resolution
crystals of both the native protein and the protein-inhibitor complex. Superimpositions are performed with LSQMAN. Comparison with human alpha-1,2-mannosidase–thiodisaccharide complex
native enzyme and in complexes with the inhibitors 1-deoxymannojirimycin and kifunensine, hanging drop vapor diffusion method, using 17-22% (w/v) polyethylene glycol 6000, 50 mM KH2PO4, pH 4.6
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation and CM-Toyopearl 650M column chromatography
recombinant alpha-1,2-mannosidase is purified from the medium by chromatography on CM-Toyopearl 650M after ammonium sulfate precipitation
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA of the Penicillium citrinum alpha-1,2 mannosidase gene lacking the signal sequence is cloned downstream of the Aspergillus amylase promoter and of the aspergillopepsin signal sequence. The resulting fungal expression vector pTAPM1 is transfected into Aspergillus oryzae strain MS2
expressed in Aspergillus oryzae strain MS2
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Lobsanov, Y.D.; Yoshida, T.; Desmet, T.; Nerinckx, W.; Yip, P.; Claeyssens, M.; Herscovics, A.; Howell, P.L.
Modulation of activity by Arg407: structure of a fungal alpha-1,2-mannosidase in complex with a substrate analogue
Acta Crystallogr. Sect. D
64
227-236
2008
Penicillium citrinum, Penicillium citrinum (P31723)
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
Penicillium citrinum, Penicillium citrinum (P31723)
Manually annotated by BRENDA team