Information on EC 3.2.1.113 - mannosyl-oligosaccharide 1,2-alpha-mannosidase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY
3.2.1.113
-
RECOMMENDED NAME
GeneOntology No.
mannosyl-oligosaccharide 1,2-alpha-mannosidase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Hydrolysis of the terminal (1->2)-linked alpha-D-mannose residues in the oligo-mannose oligosaccharide Man9(GlcNAc)2
show the reaction diagram
mechanism
-
Hydrolysis of the terminal (1->2)-linked alpha-D-mannose residues in the oligo-mannose oligosaccharide Man9(GlcNAc)2
show the reaction diagram
structure and function of enzyme from subgroups 1 to 3, overview
-
Hydrolysis of the terminal (1->2)-linked alpha-D-mannose residues in the oligo-mannose oligosaccharide Man9(GlcNAc)2
show the reaction diagram
model for substrate and conformer selectivity, mechanism, computational study
-
Hydrolysis of the terminal (1->2)-linked alpha-D-mannose residues in the oligo-mannose oligosaccharide Man9(GlcNAc)2
show the reaction diagram
mechanism: ordered equilibrium
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of O-glycosyl bond
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Metabolic pathways
-
-
N-Glycan biosynthesis
-
-
Various types of N-glycan biosynthesis
-
-
SYSTEMATIC NAME
IUBMB Comments
2-alpha-mannosyl-oligosaccharide alpha-D-mannohydrolase
Involved in the synthesis of glycoproteins.
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
(alpha1,2)-mannosidase-I
-
-
-
-
1,2-alpha-mannosidase
-
-
-
-
alpha-1,2-mannosidase
-
-
-
-
alpha-1,2-mannosidase IC
-
-
-
-
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
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9068-25-1
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
two isoforms of enzyme
-
-
Manually annotated by BRENDA team
M-90
-
-
Manually annotated by BRENDA team
Bacillus sp. M-90
M-90
-
-
Manually annotated by BRENDA team
calf
-
-
Manually annotated by BRENDA team
wild-type, N2 strain
-
-
Manually annotated by BRENDA team
Caenorhabditis elegans N2 Bristol
wild-type, N2 strain
-
-
Manually annotated by BRENDA team
; strain ATCC26555, CAI4, SC5314, NGY152, HMY5, HMY6
Uniprot
Manually annotated by BRENDA team
ATCC 26555
-
-
Manually annotated by BRENDA team
fragment; isoform Mns1
UniProt
Manually annotated by BRENDA team
strains CAI-4 and ATCC 26555
-
-
Manually annotated by BRENDA team
Candida albicans ATCC26555
strain ATCC26555, CAI4, SC5314, NGY152, HMY5, HMY6
Uniprot
Manually annotated by BRENDA team
very similar (> 60%) to other fungal 1,2-alpha-mannosidases; silveira strain, formerly known as the non-California Coccidioides immitis
UniProt
Manually annotated by BRENDA team
expression in Escherichia coli
-
-
Manually annotated by BRENDA team
recombinant
SwissProt
Manually annotated by BRENDA team
strain Guy11
-
-
Manually annotated by BRENDA team
Magnaporthe oryzae Guy11
strain Guy11
-
-
Manually annotated by BRENDA team
CD1 and C3H/An
-
-
Manually annotated by BRENDA team
Golgi alpha1,2-mannosidase IA
UniProt
Manually annotated by BRENDA team
Golgi alpha1,2-mannosidase IB
UniProt
Manually annotated by BRENDA team
isoforms Ia, IB, expressed and secreted in Pichia pastoris
-
-
Manually annotated by BRENDA team
recombinant
UniProt
Manually annotated by BRENDA team
male; Sprague-Dawley
-
-
Manually annotated by BRENDA team
male; Wistar
-
-
Manually annotated by BRENDA team
Rattus norvegicus Sprague-Dawley
Sprague-Dawley
-
-
Manually annotated by BRENDA team
Rattus norvegicus Wistar
Wistar
-
-
Manually annotated by BRENDA team
castor bean
-
-
Manually annotated by BRENDA team
IPLB-SF-21AE, baculovirus-infected
-
-
Manually annotated by BRENDA team
Sporothrix schenckii EH206
-
-
-
Manually annotated by BRENDA team
intracellular protozoan, causes Chagas disease in humans, epimastigote stage
-
-
Manually annotated by BRENDA team
two isoforms
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
blocking alpha-1,2-mannosidase in regulatory T cells results in the migration of significantly lower numbers to the peripheral lymph nodes in skin grafted mice following adoptive transfer
malfunction
-
endoplasmic reticulum mannosidase I knockdown does not affect binding of an endoplasmic reticulum-associated degradation substrate glycoprotein to EDEM1
metabolism
-
part of N-glycan pathway
physiological function
-
alpha-1,2-mannosidase function is not required for the suppressive capacity of regulatory T cells in vitro, but influences regulatory T cell adherence in vitro andmigration in vivo
physiological function
-
class I alpha-mannosidases are essential for early N-glycan processing and are required for root development and cell wall biosynthesis in Arabidopsis thaliana
physiological function
-
either isozyme MANIa or MANIb can function as the Golgi alpha-mannosidase I that produces the Man5GlcNAc2 N-glycan structure necessary for complex N-glycan synthesis
physiological function
-
Htm1 protein generates the N-glycan signal for glycoprotein degradation in the endoplasmic reticulum. Htm1p physically interacts with Pdi1p via its C-terminal domain
physiological function
-
endoplasmic reticulum mannosidase I activity is not required for association of H2a with EDEM1
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(Glc)1(Man)9(GlcNAc)2 + H2O
? + D-mannose
show the reaction diagram
-
removal of one alpha1,2-linked mannose
-
-
-
(Glc)3(Man)9(GlcNAc)2 + H2O
? + D-mannose
show the reaction diagram
-
removal of one alpha1,2-linked mannose
-
-
-
(Manalpha(1-2))nManalpha(1-6)(Manalpha(1-3))Manalpha(1-6)(Manalpha(1-3)) Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + H2O
Manalpha1-6(Manalpha1-3)Manalpha1-6(Manalpha1-3)Manbeta1-4GlcNAc beta1-4GlcNAc + D-mannose
show the reaction diagram
-
-
-
?
1,2-alpha-D-mannobiose + H2O
D-mannose
show the reaction diagram
-
-
-
-
?
1,2-alpha-mannobiose + H2O
D-mannose
show the reaction diagram
-
-
-
-
?
2-O-alpha-D-mannopyranosyl-alpha-D-mannopyranose + H2O
2 alpha-D-mannose
show the reaction diagram
-
-
-
-
?
2-O-alpha-D-mannopyranosyl-D-mannose + H2O
D-mannose
show the reaction diagram
-
-
-
?
2-O-alpha-D-mannopyranosyl-D-mannose + H2O
D-mannose
show the reaction diagram
-
i.e. alpha-D-Man-(1-2)-D-Man
-
-
?
4-methylumbelliferyl alpha-D-mannopyranoside + H2O
4-methylumbelliferone + alpha-D-mannopyranoside
show the reaction diagram
Sporothrix schenckii, Sporothrix schenckii EH206
-
-
-
-
?
4-methylumbelliferyl-alpha-D-mannopyranoside
4-methylumbelliferone + D-mannose
show the reaction diagram
-
MUaMan, fluorogenic substrate
-
-
?
4-methylumbelliferyl-alpha-D-mannopyranoside + H2O
4-methylumbelliferone + D-mannose
show the reaction diagram
-
MUaMan fluorogenic substrate to measure enzyme activity
-
-
?
4-methylumbelliferyl-alpha-D-mannopyranoside + H2O
4-methylumbelliferone + alpha-D-mannose
show the reaction diagram
Q8J0Q0
-
-
-
?
4-methylumbelliferyl-alpha-D-mannopyranoside + H2O
4-methylumbelliferone + D-mannopyranose
show the reaction diagram
Q9Y8A9
-
-
-
?
4-nitrophenyl alpha-D-mannopyranoside + H2O
4-nitrophenol + alpha-D-mannopyranoside
show the reaction diagram
Sporothrix schenckii, Sporothrix schenckii EH206
-
-
-
-
?
alpha-1,2-linked mannotetraose + H2O
? + D-mannose
show the reaction diagram
Bacillus sp., Bacillus sp. M-90
-
-
-
-
?
alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,6)]-alpha-D-mannopyranosyl-(1,6)]-beta-D-mannopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranose + H2O
alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,6)]-alpha-D-mannopyranosyl-(1,6)]-beta-D-mannopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranose + D-mannose
show the reaction diagram
-
-
-
-
?
alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,6)]-alpha-D-mannopyranosyl-(1,6)]-beta-D-mannopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranose + H2O
alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,6)]-alpha-D-mannopyranosyl-(1,6)]-beta-D-mannopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranose + D-mannose
show the reaction diagram
-
-
-
-
?
alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,6)]-alpha-D-mannopyranosyl-(1,6)]-beta-D-mannopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranose + H2O
alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,6)]-alpha-D-mannopyranosyl-(1,6)]-beta-D-mannopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranose + D-mannose
show the reaction diagram
-
-
-
-
?
alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,6)]-alpha-D-mannopyranosyl-(1,6)]-beta-D-mannopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranose + H2O
? + D-mannose
show the reaction diagram
-
to measure enzyme activity
-
-
?
alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,6)]-alpha-D-mannopyranosyl-(1,6)]-beta-D-mannopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranose + H2O
alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,6)]-alpha-D-mannopyranosyl-(1,6)]-beta-D-mannopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranose + D-mannose
show the reaction diagram
-
-
-
-
?
alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,6)]-alpha-D-mannopyranosyl-(1,6)]-beta-D-mannopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranose + H2O
alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,6)]-alpha-D-mannopyranosyl-(1,6)]-beta-D-mannopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranose + D-mannose
show the reaction diagram
-
-
-
-
?
alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,6)]-alpha-D-mannopyranosyl-(1,6)]-beta-D-mannopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranose + H2O
alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,6)]-alpha-D-mannopyranosyl-(1,6)]-beta-D-mannopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranose + D-mannose
show the reaction diagram
-
-
-
-
?
alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,6)]-alpha-D-mannopyranosyl-(1,6)]-beta-D-mannopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranose + H2O
alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,6)]-alpha-D-mannopyranosyl-(1,6)]-beta-D-mannopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranose + D-mannose
show the reaction diagram
-
-
-
-
?
alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,6)]-alpha-D-mannopyranosyl-(1,6)]-beta-D-mannopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranose + H2O
alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,6)]-alpha-D-mannopyranosyl-(1,6)]-beta-D-mannopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranose + D-mannose
show the reaction diagram
Q9SEH8
-
-
-
?
alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,6)]-alpha-D-mannopyranosyl-(1,6)]-beta-D-mannopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranose + H2O
alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,6)]-alpha-D-mannopyranosyl-(1,6)]-beta-D-mannopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranose + D-mannose
show the reaction diagram
-
-
-
-
?
alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,6)]-alpha-D-mannopyranosyl-(1,6)]-beta-D-mannopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranose + H2O
alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,6)]-alpha-D-mannopyranosyl-(1,6)]-beta-D-mannopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranose + D-mannose
show the reaction diagram
-
-
-
-
?
alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,6)]-alpha-D-mannopyranosyl-(1,6)]-beta-D-mannopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranose + H2O
? + D-mannose
show the reaction diagram
-
to measure enzyme activity
-
-
?
alpha-D-Manp-(1-2)-D-Manp + H2O
D-mannose + ?
show the reaction diagram
Magnaporthe oryzae, Magnaporthe oryzae Guy11
-
-
-
-
?
alpha1-antitrypsin null (Hong Kong) + H2O
? + D-mannose
show the reaction diagram
-
-
-
-
?
alpha1-antitrypsin null + H2O
? + D-mannose
show the reaction diagram
-
-
-
-
?
alpha1-antitrypsin null + H2O
? + D-mannose
show the reaction diagram
P39098, P45700
-
-
-
?
alpha1-antitrypsin null + H2O
alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,6)]-alpha-D-mannopyranosyl-(1,6)]-beta-D-mannopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranose + D-mannose
show the reaction diagram
-
-
-
-
?
alpha1-antitrypsin null + H2O
alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,6)]-alpha-D-mannopyranosyl-(1,6)]-beta-D-mannopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranose + D-mannose
show the reaction diagram
P39098, P45700
-
-
-
?
alpha1-antitrypsin null + H2O
alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,6)]-alpha-D-mannopyranosyl-(1,6)]-beta-D-mannopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranose + D-mannose
show the reaction diagram
-
-
-
-
?
alpha1-antitrypsin null + H2O
alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,6)]-alpha-D-mannopyranosyl-(1,6)]-beta-D-mannopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranose + D-mannose
show the reaction diagram
P39098, P45700
-
-
-
?
alpha1-antitrypsin null + H2O
alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,6)]-alpha-D-mannopyranosyl-(1,6)]-beta-D-mannopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranose + D-mannose
show the reaction diagram
-
-
-
-
?
alpha1-antitrypsin null + H2O
alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,6)]-alpha-D-mannopyranosyl-(1,6)]-beta-D-mannopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranose + D-mannose
show the reaction diagram
P39098, P45700
-
-
-
?
alpha1-antitrypsin null + H2O
alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,6)]-alpha-D-mannopyranosyl-(1,6)]-beta-D-mannopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranose + D-mannose
show the reaction diagram
-
-
-
-
?
alpha1-antitrypsin null + H2O
alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,6)]-alpha-D-mannopyranosyl-(1,6)]-beta-D-mannopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranose + D-mannose
show the reaction diagram
P39098, P45700
-
-
-
?
alpha1-antitrypsin null + H2O
alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,6)]-alpha-D-mannopyranosyl-(1,6)]-beta-D-mannopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranose + D-mannose
show the reaction diagram
-
overexpression of each Golgi alpha1,2-mannosidase enhances alpha1-antitrypsin null degradation and trimming of its N-glycans to alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,6)]-alpha-D-mannopyranosyl-(1,6)]-beta-D-mannopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranose
-
-
?
alpha1-antitrypsin null + H2O
alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,6)]-alpha-D-mannopyranosyl-(1,6)]-beta-D-mannopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranose + D-mannose
show the reaction diagram
P39098, P45700
overexpression of each Golgi alpha1,2-mannosidase enhances alpha1-antitrypsin null degradation and trimming of its N-glycans to alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,6)]-alpha-D-mannopyranosyl-(1,6)]-beta-D-mannopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranose
-
-
?
baker's yeast mannan + H2O
? + D-mannose
show the reaction diagram
-
-
-
-
?
baker's yeast mannan + H2O
? + D-mannose
show the reaction diagram
-
-
-
-
?
baker's yeast mannan + H2O
? + D-mannose
show the reaction diagram
-
releases 9.2% of total mannose
-
-
?
baker's yeast mannan + H2O
? + D-mannose
show the reaction diagram
Bacillus sp., Bacillus sp. M-90
-
alpha-1,2-linked side-chains
-
-
?
Glcalpha(1-3)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)[Manalpha(1-2)Manalpha(1-3)[Manalpha(1-2)Manalpha(1-6)]Manalpha(1-6)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + H2O
Glcalpha(1-3)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)[Manalpha(1-2)Manalpha(1-3)[Manalpha(1-6)]Manalpha(1-6)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + D-mannose
show the reaction diagram
-
-
-
-
-
GlcNAc-(Man)5GlcNAc + H2O
? + D-mannose
show the reaction diagram
-
poor substrate
-
-
?
high mannose chains of thyroglobulin and phytohemagglutinin-P + H2O
? + D-mannose
show the reaction diagram
-
thyroglobulin: 70% of alpha1,2-mannose residues accessible
-
-
-
Man-alpha-1,2-Man-alpha-O-CH3 + H2O
methyl alpha-D-mannopyranoside + D-mannose
show the reaction diagram
-
-
-
-
-
Man8GlcNAc2 + H2O
Man5GlcNAc2 + D-mannose
show the reaction diagram
-
-
-
-
?
Man8GlcNAc2 + H2O
Man7GlcNAc2 + D-mannose
show the reaction diagram
-
-
-
-
?
Man9GlcNAc2 + H2O
Man5GlcNAc2 + D-mannose
show the reaction diagram
-
-
-
-
?
Manalpha(1,2)Man-O-Me + H2O
?
show the reaction diagram
-
-
-
-
?
Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)[Manalpha(1-2)Manalpha(1-3)[Manalpha(1-2)Manalpha(1-6)]Manalpha(1-6)]Manbeta(1-4)GlcNACbeta(1-4)GlcNAc + H2O
Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)[Manalpha(1-2)Manalpha(1-6)[Manalpha(1-3)]Manalpha(1-6)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + D-mannose
show the reaction diagram
-
the reaction is performed by ER-type alpha-mannosidase I protein MNS3
-
-
?
Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)[Manalpha(1-2)Manalpha(1-3)[Manalpha(1-2)Manalpha(1-6)]Manalpha(1-6)]Manbeta(1-4)GlcNACbeta(1-4)GlcNAc + H2O
Manalpha(1-3)[Manalpha(1-3)[Manalpha(1-6)]Manalpha(1-6)]Manbeta(1-4)GlcNACbeta(1-4)GlcNAc + 4 D-mannose
show the reaction diagram
-
-
-
-
-
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)GlcNAc + H2O
Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)[Manalpha(1-2)Manalpha(1-6)[Manalpha(1-3)]Manalpha(1-6)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + D-mannose
show the reaction diagram
Q9Y8A9
-
-
-
?
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)GlcNAc + H2O
Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)[Manalpha(1-6)[Manalpha(1-2)Manalpha(1-3)]Manalpha(1-6)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + alpha-D-mannose
show the reaction diagram
-
-
-
-
?
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)GlcNAc + H2O
Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)[Manalpha(1-6)[Manalpha(1-3)]Manalpha(1-6)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + 2 alpha-D-mannose
show the reaction diagram
-
-
-
-
?
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)GlcNAc + H2O
Manalpha(1-2)Manalpha(1-3)[Manalpha(1-6)[Manalpha(1-3)]Manalpha(1-6)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + 3 alpha-D-mannose
show the reaction diagram
-
-
-
-
?
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)GlcNAc + H2O
Manalpha(1-3)[Manalpha(1-6)[Manalpha(1-3)]Manalpha(1-6)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + 4 alpha-D-mannose
show the reaction diagram
-
-
-
-
?
Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)[Manalpha(1-2)Manalpha(1-6)[Manalpha(1-3)]Manalpha(1-6)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + H2O
Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)[Manalpha(1-6)[Manalpha(1-3)]Manalpha(1-6)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + D-mannose
show the reaction diagram
Q8J0Q0
cytosolic isoform E-I
-
-
?
Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)[Manalpha(1-2)Manalpha(1-6)[Manalpha(1-3)]Manalpha(1-6)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + H2O
Manalpha(1-2)Manalpha(1-3)[Manalpha(1-2)Manalpha(1-6)[Manalpha(1-3)]Manalpha(1-6)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + D-mannose
show the reaction diagram
-
-
-
-
-
Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)[Manalpha(1-2)Manalpha(1-6)[Manalpha(1-3)]Manalpha(1-6)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + H2O
Manalpha(1-3)[Manalpha(1-3)[Manalpha(1-6)]Manalpha(1-6)]Manbeta(1-4)GlcNACbeta(1-4)GlcNAc + 3 D-mannose
show the reaction diagram
-
-
-
-
-
Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)[Manalpha(1-2)Manalpha(1-6)[Manalpha(1-3)]Manalpha(1-6)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + H2O
Manalpha(1-3)[Manalpha(1-3)[Manalpha(1-6)]Manalpha(1-6)]Manbeta(1-4)GlcNACbeta(1-4)GlcNAc + 3 D-mannose
show the reaction diagram
-
the reaction is performed by Golgi-alpha-mannosidase I proteins MNS1 and MNS2
-
-
?
Manalpha(1-2)Manalpha(1-3)Manalpha(1-6)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAc + 2 H2O
(Man)5GlcNAc + 2 D-mannose
show the reaction diagram
-
-
-
-
?
Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAc + H2O
? + 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
-
-
-
?
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
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
-
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
-
-
-
?
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
-
-
-
?
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
-
-
-
-
-
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
-
-
-
-
?
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
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
first product is Man6GlcNAc, followed by slower conversion to Man5GlcNAc
?
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
-
-
after long-term incubation
?
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
Q9UKM7
-
product is Man8GlcNAc
?
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)GlcNAc + 4 H2O
(Man)5GlcNAc + 4 D-mannose
show the reaction diagram
-
-
and (Man)6GlcNAc
?
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
-
-
product is Man6GlcNAc
?
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
-
-
product is Man6GlcNAc
?
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
-
-
(Man)7GlcNAc and (Man)6GlcNAc after 4 h, (Man)8GlcNAc, (Man)7GlcNAc, (Man)6GlcNAc and (Man)5GlcNAc after 12 h incubation
?
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
-
best substrate
-
-
-
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
-
i.e. (Man)9GlcNAc, specific for alpha-1,2-linked mannose residues
-
?
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
-
i.e. (Man)9GlcNAc, specific for alpha-1,2-linked mannose residues
and (Man)6GlcNAc
?
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
-
the terminal mannose on the middle antenna appears to be the most susceptible residue
-
-
-
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
P32906
mutant R273L
product of mutant R273L, product of wild type is Man8GlcNAc
-
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
-
removes all 4 alpha1,2-linked mannosyl residues
-
?
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
-
removes all 4 alpha1,2-linked mannosyl residues
-
?
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
-
function of enzyme from subgroup 1 to 3
-
-
?
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
Q9UKM7
pyridylamine-tagged Man9GlcNAc2
-
-
?
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
Rattus norvegicus Sprague-Dawley
-
i.e. (Man)9GlcNAc, specific for alpha-1,2-linked mannose residues
and (Man)6GlcNAc
?
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
Bacillus sp. M-90
-
i.e. (Man)9GlcNAc, specific for alpha-1,2-linked mannose residues
-
?
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
Rattus norvegicus Wistar
-
best substrate
-
-
-
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(1-2)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
-
removes 3 of the 4 alpha1,2-linked mannosyl residues
-
-
?
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
-
removes 3 of the 4 alpha1,2-linked mannosyl residues
-
?
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
-
removes 3 of the 4 alpha1,2-linked mannosyl residues
-
?
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
-
highly active on alpha(1-2) linked mannooligosaccharides
-
-
?
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
-
highly active on alpha(1-2) linked mannooligosaccharides
-
-
?
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
-
enzyme from endoplasmic reticulum removes only 1 or 2 alpha1,2-linked mannose residues
-
-
?
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
-
intact chitobiose core affects Man9-mannosidase specificity: reduction or removal of terminal N-acetylglucosamine residue increases hydrolytic susceptibility of the fourth alpha1,2-mannosyl-linkage
-
?
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-hexapeptide + H2O
(Man)6(GlcNAc)2-hexapeptide + D-mannose
show the reaction diagram
-
substrate specificity not influenced by peptide moiety, removes 3 mannose residues
-
?
Manalpha(1-2)Manalpha(1-6)(Manalpha(1-3))Manalpha(1-6)(Manalpha(1-2)Manalpha(1-2))Manalpha(1-3)Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc-peptide + H2O
(Man)5(GlcNAc)-peptide + D-mannose
show the reaction diagram
Rattus norvegicus, Rattus norvegicus Sprague-Dawley
-
-
-
?
Manalpha(1-2)Manalpha(1-6)(Manalpha(1-3))Manalpha(1-6)(Manalpha(1-2)Manalpha(1-2)Manalpha(1-3))Manbeta(1-4)GlcNAc + H2O
? + D-mannose
show the reaction diagram
-
-
-
-
?
Manalpha(1-2)Manalpha(1-6)(Manalpha(1-3))Manalpha(1-6)(Manalpha(1-2)Manalpha(1-2)Manalpha(1-3))Manbeta(1-4)GlcNAc + H2O
? + D-mannose
show the reaction diagram
Rattus norvegicus Sprague-Dawley
-
-
-
-
?
Manalpha(1-2)Manalpha(1-6)(Manalpha(1-3))Manalpha(1-6)(Manalpha(1-2)Manalpha(1-2)Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + H2O
? + D-mannose
show the reaction diagram
-
-
-
-
?
Manalpha(1-2)Manalpha(1-6)(Manalpha(1-3))Manalpha(1-6)(Manalpha(1-2)Manalpha(1-2)Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + H2O
? + D-mannose
show the reaction diagram
-
-
-
-
?
Manalpha(1-2)Manalpha(1-6)(Manalpha(1-3))Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manbeta(1-4)GlcNA + H2O
? + D-mannose
show the reaction diagram
-
-
-
-
?
Manalpha(1-2)Manalpha(1-6)(Manalpha(1-3))Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manbeta(1-4)GlcNA + H2O
? + D-mannose
show the reaction diagram
-
hydrolysis at 39% (mannosidase IB) or 67% (mannosidase IA) the rate of (Man)9GlcNAc hydrolysis
-
-
?
Manalpha(1-2)Manalpha(1-6)(Manalpha(1-3))Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manbeta(1-4)GlcNA + H2O
? + D-mannose
show the reaction diagram
Rattus norvegicus Sprague-Dawley
-
-
-
-
?
Manalpha(1-2)Manalpha(1-6)(Manalpha(1-3))Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manbeta(1-4)GlcNA + H2O
? + D-mannose
show the reaction diagram
Rattus norvegicus Wistar
-
hydrolysis at 39% (mannosidase IB) or 67% (mannosidase IA) the rate of (Man)9GlcNAc hydrolysis
-
-
?
Manalpha(1-2)Manalpha(1-6)(Manalpha(1-3))Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + H2O
? + D-mannose
show the reaction diagram
-
-
-
-
?
Manalpha(1-2)Manalpha(1-6)(Manalpha(1-3))Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + H2O
? + D-mannose
show the reaction diagram
-
-
-
-
?
Manalpha(1-6)(Manalpha(1-3))Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manbeta(1-4)GlcNAc + H2O
(Man)5(GlcNAc)2 + D-mannose
show the reaction diagram
-
very poor substrate
-
-
?
Manalpha(1-6)(Manalpha(1-3))Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manbeta(1-4)GlcNAc + H2O
(Man)5(GlcNAc)2 + D-mannose
show the reaction diagram
-
preferred substrate
-
?
Manalpha(1-6)(Manalpha(1-3))Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manbeta(1-4)GlcNAc + H2O
(Man)5(GlcNAc)2 + D-mannose
show the reaction diagram
-
as in Taka-amylase A
-
-
?
Manalpha(1-6)(Manalpha(1-3))Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manbeta(1-4)GlcNAc + H2O
(Man)5(GlcNAc)2 + D-mannose
show the reaction diagram
-
pyridylamino derivative of Manalpha(1-6)(Manalpha(1-3))Manalpha(1-6)Manalpha(1-2)Manalpha(1-3)ManbetaGlcNAc2
i.e. pyridylamino derivative of (Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc
?
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
-
?
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(1-6)(Manalpha(1-3))Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc-Asn + H2O
? + D-mannose
show the reaction diagram
-
-
-
-
?
Manalpha(1-6)(Manalpha(1-3))Manalpha(1-6)(Manalpha(1-2)Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc-Asn + H2O
? + D-mannose
show the reaction diagram
Rattus norvegicus, Rattus norvegicus Wistar
-
hydrolysis at 18-25% the rate of (Man)9GlcNAc hydrolysis
-
-
?
Manalpha(1-6)(Manalpha(1-3))Manalpha(1-6)(Manalpha(1-3))Manbeta(1-4)GlcNAc + H2O
(Man)4GlcNAc + (Man)3GlcNAc + D-mannose
show the reaction diagram
-
without alpha1,2-linked mannose residues: poor substrate
-
?
Manalpha(1-6)(Manalpha(1-3))Manalpha(1-6)(Manalpha(1-3))Manbeta(1-4)GlcNAc + H2O
(Man)4GlcNAc + (Man)3GlcNAc + D-mannose
show the reaction diagram
-
without alpha1,2-linked mannose residues: poor substrate
-
-
?
Manalpha(1-6)(Manalpha(1-3))Manalpha(1-6)(Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + H2O
(Man)4(GlcNAc)2 + (Man)3(GlcNAc)2 + D-mannose
show the reaction diagram
-
without alpha-1,2-linked mannose residues: no substrate
-
-
-
Manalpha(1-6)(Manalpha(1-3))Manalpha(1-6)(Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + H2O
(Man)4(GlcNAc)2 + (Man)3(GlcNAc)2 + D-mannose
show the reaction diagram
-
i.e. Manalpha(1-2)Manalpha(1-2)Manalpha(1-3) (Manalpha(1-6))ManbetaGlcNAc-betaGlcNAc
-
?
Manalpha(1-6)(Manalpha(1-3))Manalpha(1-6)(Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + H2O
(Man)4(GlcNAc)2 + (Man)3(GlcNAc)2 + D-mannose
show the reaction diagram
-
i.e. Manalpha(1-2)Manalpha(1-2)Manalpha(1-3) (Manalpha(1-6))ManbetaGlcNAc-betaGlcNAc
-
-
?
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->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
O60476, Q9NR34
-
-
-
?
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
Sporothrix schenckii EH206
-
-
-
-
?
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
O60476, Q9NR34
-
-
-
?
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
O60476, Q9NR34
-
-
-
?
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
O60476, Q9NR34
-
-
-
?
Manalpha(1->3)[Manalpha(1->6)[Manalpha(1->2)Manalpha(1->3)]Manalpha(1->6)]Manbeta(1->4)GlcNAcbeta(1->4)GlcNAcbeta-Asn + H2O
Manalpha(1->3)[Manalpha(1->6)[Manalpha(1->3)]Manalpha(1->6)]Manbeta(1->4)GlcNAcbeta(1->4)GlcNAcbeta + D-mannose
show the reaction diagram
Sporothrix schenckii, Sporothrix schenckii EH206
-
-
-
-
?
methyl 2-O-alpha-D-mannopyranosyl-alpha-D-mannopyranoside + H2O
? + D-mannose
show the reaction diagram
Q3HYC1
used in a spectrophotometric assay
-
-
?
ovalbumin glycopeptide + H2O
? + D-mannose
show the reaction diagram
-
-
-
-
-
ovalbumin glycopeptide + H2O
? + D-mannose
show the reaction diagram
-
glycopeptide IV
-
-
-
p-nitrophenyl-alpha-D-mannoside + H2O
4-nitrophenol + D-mannose
show the reaction diagram
-
-
-
-
?
p-nitrophenyl-alpha-D-mannoside + H2O
4-nitrophenol + D-mannose
show the reaction diagram
-
-
-
-
?
p-nitrophenyl-alpha-D-mannoside + H2O
4-nitrophenol + D-mannose
show the reaction diagram
-
mannosidase IB: poor substrate, mannosidase IA: no substrate
-
-
?
pyridylamino derivative of (Man)9(GlcNAc)2 + H2O
pyridylamino derivative of (Man)5(GlcNAc)2 + D-mannose
show the reaction diagram
-
-
product is pyridylamino derivative of (Man)8(GlcNAc)2
?
pyridylamino derivative of (Man)9(GlcNAc)2 + H2O
pyridylamino derivative of (Man)5(GlcNAc)2 + D-mannose
show the reaction diagram
-
-
after 120 h incubation, via specific intermediates: overview
?
methyl-2-O-alpha-D-mannopyranosyl-alpha-D-mannopyranoside + H2O
? + D-mannose
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
no hydrolysis of alpha1,3-linkages
-
-
-
additional information
?
-
-
no hydrolysis of alpha1,3-linkages
-
-
-
additional information
?
-
-
no hydrolysis of alpha1,3-linkages
-
-
-
additional information
?
-
-
more specific towards Man-alpha-1,2-bonds, but also hydrolysis of alpha-1,3- and of alpha-1,6-bonds
-
-
-
additional information
?
-
-
effect of the alpha-1,2-mannosidic linkage in the alpha-1,3-branch of Man6GlcNAc2 on enzyme activity
-
-
-
additional information
?
-
-
no substrate: GP III
-
-
-
additional information
?
-
-
no substrate: (Man)4-(GlcNAc)2
-
-
-
additional information
?
-
-
little or no activity with 4-methylumbelliferyl-alpha-mannoside, aryl-alpha-D-mannosides
-
-
-
additional information
?
-
-
no substrate: 4-methylumbelliferyl-alpha-mannoside
-
-
-
additional information
?
-
-
no substrate: (Man)5(GlcNAc)2-Asn (i.e. GPI)
-
-
-
additional information
?
-
-
no substrate: 3-O-alpha- and 6-O-alpha-D-mannobioses
-
-
-
additional information
?
-
-
substrate specificity and function of enzyme from subgroups 1 to 3, overview
-
-
-
additional information
?
-
-
pig liver enzyme substrate specificity resembles that of calf liver enzyme
-
-
-
additional information
?
-
-
no hydrolysis of alpha1,6-linkages
-
-
-
additional information
?
-
-
no hydrolysis of alpha1,6-linkages
-
-
-
additional information
?
-
-
no hydrolysis of alpha1,6-linkages
-
-
-
additional information
?
-
-
no hydrolysis of alpha1,6-linkages
-
-
-
additional information
?
-
-
mannosidase IA and B are quite similar in substrate specificity
-
-
-
additional information
?
-
-
no substrate: 1,2-alpha-D-mannobiitol
-
-
-
additional information
?
-
-
no activity with p-nitrophenyl-alpha-mannoside, Manalpha(1-3)Man-OMe or Manalpha(1-6)Man-OMe
-
-
-
additional information
?
-
-
generating the signal that targets misfolded glycoproteins for endoplasmic reticulum-associated protein degradation (ERAD)
-
-
-
additional information
?
-
P39098, P45700
generating the signal that targets misfolded glycoproteins for endoplasmic reticulum-associated protein degradation (ERAD)
-
-
-
additional information
?
-
-
targets misfolded glycoproteins for dislocation into the cytosol and destruction by 26 S proteasomes
-
-
-
additional information
?
-
Q9Y8A9
enzyme is involved in the processing of N-linked mannans
-
-
-
additional information
?
-
Q8J0Q0
cytosolic isoform E-I trims free Man8GlcNac2 isomer B into Man7GlcNac2 isomer B
-
-
-
additional information
?
-
Q9Y8A9
no substrate: Man5glcNAc2-Asn
-
-
-
additional information
?
-
-
methyl-3-O-alpha-D-mannopyranosyl-alpha-D-mannopyranoside is not cleaved by MNS1, MNS2, and MNS3
-
-
-
additional information
?
-
-
the enzyme does not hydrolyze alpha-D-Manp-(1-3)-D-Manp and alpha-D-Manp-(1-6)-D-Manp
-
-
-
additional information
?
-
-
the Htm1p exomannosidase activity requires processing of the N-glycan by glucosidase I, glucosidase II, and mannosidase I
-
-
-
additional information
?
-
-
when being targeted to endoplasmic reticulum-associated degradation, a misfolded glycoprotein undergoes endoplasmic reticulum mannosidase I-dependent trimming to yield the N-linked oligosaccharide structures Manalpha(1->3)[Manalpha(1->6)[Manalpha(1->3)]Manalpha(1->6)]Manbeta(1->4)GlcNAcbeta(1->4)GlcNAcbeta-2-pyridylamine and Manalpha(1->3)[Manalpha(1->6)[Manalpha(1->2)Manalpha(1->3)]Manalpha(1->6)]Manbeta(1->4)GlcNAcbeta(1->4)GlcNAcbeta-2-pyridylamine
-
-
-
additional information
?
-
Bacillus sp. M-90
-
no substrate: 1,2-alpha-D-mannobiitol
-
-
-
additional information
?
-
Rattus norvegicus Wistar
-
mannosidase IA and B are quite similar in substrate specificity
-
-
-
additional information
?
-
Magnaporthe oryzae Guy11
-
the enzyme does not hydrolyze alpha-D-Manp-(1-3)-D-Manp and alpha-D-Manp-(1-6)-D-Manp
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,6)]-alpha-D-mannopyranosyl-(1,6)]-beta-D-mannopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranose + H2O
alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,3)-[alpha-D-mannopyranosyl-(1,2)-alpha-D-mannopyranosyl-(1,6)]-alpha-D-mannopyranosyl-(1,6)]-beta-D-mannopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1,4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranose + D-mannose
show the reaction diagram
-
-
-
-
?
alpha1-antitrypsin null + H2O
? + D-mannose
show the reaction diagram
-
-
-
-
?
alpha1-antitrypsin null + H2O
? + D-mannose
show the reaction diagram
P39098, P45700
-
-
-
?
Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)[Manalpha(1-2)Manalpha(1-6)[Manalpha(1-3)]Manalpha(1-6)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + H2O
Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)[Manalpha(1-6)[Manalpha(1-3)]Manalpha(1-6)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + D-mannose
show the reaction diagram
Q8J0Q0
cytosolic isoform E-I
-
-
?
Manalpha(1-2)Manalpha(1-3)Manalpha(1-6)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAc + 2 H2O
(Man)5GlcNAc + 2 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
-
-
-
?
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
-
-
-
?
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
-
-
-
-
-
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
-
-
-
?
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
-
-
-
?
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
-
-
-
-
-
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
-
-
-
?
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
-
-
and (Man)6GlcNAc
?
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
-
function of enzyme from subgroup 1 to 3
-
-
?
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
Rattus norvegicus Sprague-Dawley
-
-
and (Man)6GlcNAc
?
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
Bacillus sp. M-90
-
-
-
?
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
Rattus norvegicus Wistar
-
-
-
-
-
additional information
?
-
-
generating the signal that targets misfolded glycoproteins for endoplasmic reticulum-associated protein degradation (ERAD)
-
-
-
additional information
?
-
P39098, P45700
generating the signal that targets misfolded glycoproteins for endoplasmic reticulum-associated protein degradation (ERAD)
-
-
-
additional information
?
-
-
targets misfolded glycoproteins for dislocation into the cytosol and destruction by 26 S proteasomes
-
-
-
additional information
?
-
Q9Y8A9
enzyme is involved in the processing of N-linked mannans
-
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
-
requirement
Ca2+
-
activation; microsomal enzyme, activation
Ca2+
-
5 mM; activation
Ca2+
-
activation; most effective cation
Ca2+
-
activation
Ca2+
-
mechanism; requirement
Ca2+
-
activation; slight activation
Ca2+
-
activation
Ca2+
-
not
Ca2+
-
requirement, protects from thermal inactivation, Km value 0.5 mM
Ca2+
-
activation
Ca2+
-
10 mM, completely recovers activity after treatment with EDTA
Ca2+
P45700
the enzyme assumes an (alphaalpha)7 barrel structure with a Ca2+ ion coordinated at the bas of the barrel
Ca2+
-
required for activity, isozyme MANIa shows 450% relative activity at 15 mM Ca2+, isozyme MANIb shows 600% relative activity at 15 mM Ca2+
Ca2+
O60476, Q9NR34
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; required for activity. Optimum concentration 15 mM. the activity of soform ManIA2 is significantly decreased after incubation at 30C without Ca2+, which is about 30% compared with the activity of the enzyme after incubation at 5C. The enzyme activity of ManIA2 increases with increasing Ca2+ concentration until 12 mM
Cd2+
-
activation, 1 mM, inhibits at 10 mM
Co2+
-
slight activation
Co2+
-
activation
Cu2+
-
slight activation
Divalent cations
-
requirement
Divalent cations
-
not
Fe2+
-
slight activation
Mg2+
-
activation; slight
Mg2+
-
activation; less effective than Ca2+
Mg2+
-
10 mM, recovers activity to 43% after treatment with EDTA
Mn2+
-
slight activation
Ni2+
-
activation
Zn2+
-
activation, less effective than Ca2+
Zn2+
O60476, Q9NR34
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
-
requirement of divalent cations
additional information
-
Co2+, Cu2+, Mg2+, Mn2+, and Zn2+ have no effect on activity
additional information
-
although MNS1, MNS2, and MNS3 do not display any specific preference for Ca2+ over Mn2+, the activity is restored to a much lower degree in the presence of Mg2+
additional information
O60476, Q9NR34
isoform ManIA2 shows no activity in the presence of Co2+, Mn2+, and Cu2+; isoform ManIC shows no activity in the presence of Co2+ and Mn2+
additional information
-
the enzyme activity os not sensitive to the presence of Ca2+, Mg2+ and Mn2+ at concentrations up to 3 mM
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1,4-Dideoxy-1,4-imino-D-mannitol
-
in vitro and in vivo
1,4-Dideoxy-1,4-imino-D-mannitol
-
not
1,4-Dideoxy-1,4-imino-D-mannitol
-
not
1-Cyclohexyl-3-(2-morpholinyl-4-ethyl)carbodiimide/glycine methylester
-
-
1-deoxymannojirimycin
-
-
1-deoxymannojirimycin
-
-
1-deoxymannojirimycin
-
-
1-deoxymannojirimycin
-
-
1-deoxymannojirimycin
-
reversible
1-deoxymannojirimycin
-
mannose analog, in vivo and in vitro; reversible (not by Ca2+)
1-deoxymannojirimycin
-
-
1-deoxymannojirimycin
-
mannose analog, in vivo and in vitro; rat liver enzyme
1-deoxymannojirimycin
-
strong
1-deoxymannojirimycin
-
not, enzyme from endoplasmic reticulum
1-deoxymannojirimycin
-
-
1-deoxymannojirimycin
-
not
1-deoxymannojirimycin
-
10% residual activity at 0.0002 mM
1-deoxymannojirimycin
-
-
1-deoxymannojirimycin
-
-
1-deoxymannojirimycin
-
not significantly
1-deoxymannojirimycin
-
-
1-deoxymannojirimycin
-
0.2 mM, 50% inhibition
1-deoxymannojirimycin
-
trimming is inhibited preferentially by 1-deoxymannojirimycin, inhibits hydrolysis of 4-methylumbelliferyl-alpha-D-mannopyranoside
1-deoxymannojirimycin
-
mannose analogue, specific inhibitor of alpha1,2-mannosidase. Focus on the effect of blocking alpha-mannosidases I in human hepatocarcinoma 7721 cells concerning with endoplasmic reticulum stress. Observed that 1-deoxymannojirimycin can also be a radical stimulus in inducing endoplasmic reticulum stress
1-deoxymannojirimycin
-
found in crystal structures of the active site
1-deoxymannojirimycin
-
DMJ, inhibition of 4-methylumbelliferyl-alpha-D-mannopyranoside hydrolysis
1-deoxymannojirimycin
-
-
1-deoxymannojirimycin
-
-
1-deoxymannojirimycin
-
isozyme MANIa shows 20% residual activity at 0.1 mM 1-deoxymannojirimycin, isozyme MANIb shows 45% residual activity at 0.1 mM 1-deoxymannojirimycin
1-deoxymannojirimycin
-
-
1-deoxymannojirimycin
O60476, Q9NR34
no activity at 0.01 mM; no activity at 0.01 mM
1-deoxymannojirimycin
-
the enzyme is inhibited preferentially by 1-deoxymannojirimycin
2-O-alpha-D-mannopyranosyl-alpha-D-mannopyranoside
-
in decreasing order of efficiency: alpha1,2, alpha 1,3 and alpha1,6-mannosylmannose
3-O-alpha-D-mannopyranosyl-alpha-D-mannopyranoside
-
in decreasing order of efficiency: alpha1,2, alpha 1,3 and alpha1,6-mannosylmannose
-
6-O-alpha-D-mannopyranosyl-alpha-D-mannopyranoside
-
in decreasing order of efficiency: alpha1,2, alpha 1,3 and alpha1,6-mannosylmannose
alpha1,2-Linked oligosaccharides
-
-
alpha1,3-Linked oligosaccharides
-
-
Ba2+
-
10 mM
BAPTA
-
i.e. 1,2-bis(2-aminophenoxy) ethane N,N,N',N'-tetraacetic acid
Basic sugar analogs of mannose
-
strong
-
brefeldin A
-
known inhibitor of vesicle transport, ablated intracellular turnover of the radiolabeled molecules. Plus digestion with potato acid phosphatase implies that phosphorylation of ER mannosidase I is responsible for the altered electrophoretic mobility
Cd2+
-
10 mM, activation at 1 mM
Cd2+
-
strong
Chloroquine
-
lysosomotrophic amine capable of raising the pH of acidic intracellular compartments, added to the medium with weak inhibition
Chloroquine
-
lysosomotrophic amine capable of raising the pH of acidic intracellular compartments, effect on the intracellular fate of endogenous mouse ER mannosidase I
Co2+
-
50% reduction in alpha-mannosidase activity is observed after addition of 3 mM CoCl2
Cu2+
-
10 mM
Cu2+
-
-
Cu2+
-
-
Cu2+
-
strong
cycloheximide
-
inhibitory effect like kifunensine
D-mannono-delta-lactam
-
-
D-mannono-gamma-lactone
-
-
D-mannono-gamma-lactone
-
-
D-Mannonolactam amidrazone
-
mannosidase inhibitor, MDCK-cells: in vivo and in vitro
deoxymannojirimycin
-
degradation is inhibited by the the mannosidase inhibitor
deoxymannojirimycin
-
-
deoxymannojirimycin hydrochloride
Q3HYC1
inhibitor at a final concentration of 0.5 mM, reduces the activity by 80%
dithiothreitol
-
loss of activity with first-order kinetics
EDTA
-
Ca2+ restores
EDTA
-
Ca2+ restores
EDTA
-
Ca2+ restores
EDTA
-
-
EDTA
-
Ca2+ restores
EDTA
-
Ca2+ restores
EDTA
-
complete inactivation at 1.7 mM, Ca2+ restores
EDTA
-
strong
EDTA
-
complete inactivition, Zn2+ restores, Ca2+, Cd2+, Mg2+, Ni2+, Na+ or Cu2+ restore partly
EDTA
-
enzyme loses 96% activity after dialysis in 50 mM PIPES buffer, pH 6.0, containing 2 mM EDTA. Addition of 10 mM Ca2+ recovers activity to 100%, addition of 10 mM Mg2+ recovers activity to 43%
EDTA
-
isozyme MANIa shows 20% residual activity at 1 mM EDTA, isozyme MANIb shows 35% residual activity at 1 mM EDTA, isozyme MANIb activity in the presence of 1 mM EDTA is restored by the addition of Ca2+
EDTA
-
partial inhibition
EGTA
-
ethylene glycol-bis(beta-aminoethylether)-N,N,N',N'-tetraacetic acid
EGTA
-
complete loss of acvtivity at 0.1 mM, Ca2+ restores
Fe2+
-
strong
Fe3+
-
strong
Hg2+
-
strong
iodoacetic acid
-
monoiodoacetic acid, 1 mM, weak
iodoacetic acid
-
-
kifunensine
-
plant and animal Golgi mannosidase I
kifunensine
-
-
kifunensine
-
mannosidase I, not enzyme from endoplasmic reticulum
kifunensine
-
10% residual activity at 0.0002 mM
kifunensine
-
50% inhibition at 0.0001 mM
kifunensine
-
-
kifunensine
-
0.0015 mM, 50% inhibition
kifunensine
-
inhibits Golgi alpha1,2-mannosidase. Addition of kifunensine completely inhibits mannose trimming from alpha1-antitrypsin null (Hong Kong) in mock transfected cells. Kifunensine inhibits alpha1-antitrypsin null (Hong Kong) degradation in cells co-transfected with the Golgi mannosidases
kifunensine
P39098
inhibits Golgi alpha1,2-mannosidase. Addition of kifunensine completely inhibits mannose trimming from alpha1-antitrypsin null (Hong Kong) in mock transfected cells. Kifunensine inhibits alpha1-antitrypsin null (Hong Kong)degradation in cells co-transfected with the Golgi mannosidases; inhibits Golgi alpha1,2-mannosidase. Addition of kifunensine completely inhibits mannose trimming from alpha1-antitrypsin null (Hong Kong) in mock transfected cells. Kifunensine inhibits alpha1-antitrypsin null (Hong Kong)degradation in cells co-transfected with the Golgi mannosidases
kifunensine
-
found in crystal structures of the active site
kifunensine
-
general membrane-permeable inhibitor of alpha-mannosidase activity
kifunensine
-
general membrane-permeable inhibitor of alpha-mannosidase activity, effect on the intracellular fate of endogenous mouse ER mannosidase I
kifunensine
-
degradation is inhibited by the the mannosidase inhibitor
kifunensine
-
-
kifunensine
-
complete inhibition at 0.04 mM
kifunensine
-
-
kifunensine
O60476, Q9NR34
no activity at 0.01 mM; no activity at 0.01 mM
lactacystin
-
irreversible inhibitor of multicatalytic proteasomes, only a minor effect on the disappearance of radiolabeled human ER mannosidase I
lactacystin
-
irreversible inhibitor of multicatalytic proteasomes, effect on the intracellular fate of endogenous mouse ER mannosidase I
Leupeptin
-
lysosomal protease inhibitor, intracellular turnover of pulse-radiolabeled recombinant human ER mannosidase I is substantially inhibited
Leupeptin
-
lysosomal protease inhibitor, effect on the intracellular fate of endogenous mouse ER mannosidase I
mannosamine
-
not
Mannosyl-mannose disaccharide
-
in decreasing order of efficiency: alpha1,2, alpha 1,3 and alpha1,6-mannosylmannose
-
methyl-alpha-D-lyxopyranosyl-(1',2)-alpha-D-mannopyranoside
P31723
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
methyl-alpha-mannoside
-
-
methyl-alpha-mannoside
-
not
N-5-Carboxypentyldeoxymannojirimycin
-
-
N-5-Carboxypentyldeoxymannojirimycin
-
strong
N-carbobenzoxyl-leucinyl-leucinyl-leucinal
-
degradation is inhibited by the proteasomal inhibitor
N-Methyl-deoxymannojirimycin
-
-
N-Methyl-deoxymannojirimycin
-
-
N-Methyl-deoxymannojirimycin
-
-
Na+
-
1 mM, weak, not at 10 mM
Ni2+
-
-
p-Chloromercuriphenylsulfonic acid
-
-
PCMB
-
Ca2+ protects
pepstatin A
-
in the presence of mixed membrane fraction from strain ATTC 26555, the 52 kDa polypeptide is converted into a 43 kDa active product. Protease inhibitors, such as phenylmethylsulphonylfluoride, trans-epoxysuccinyl-L-leucylamido(4-guanidino)butane and 1,10-phenantroline, fail to prevent proteolysis. Pepstatin A, an aspartyl protease inhibitor, fully blocked enzyme processing
phosphatidylinositol
-
CaCl2 or NaCl restores
Sn2+
-
strong
swainsonine
-
-
swainsonine
-
complete inhibition
swainsonine
-
inhibits hydrolysis of 4-methylumbelliferyl-alpha-D-mannopyranoside
swainsonine
-
SW, inhibition of 4-methylumbelliferyl-alpha-D-mannopyranoside hydrolysis
swainsonine
-
-
swainsonine
O60476, Q9NR34
isoform ManIC shows 86% activity at 0.5 mM swainsonine
swainsonine
-
-
Ti4+
-
strong
Tris
-
in vivo and in vitro
Tris/maleate
-
-
Zn2+
-
reversible by Ca2+
Zn2+
-
50% reduction in alpha-mannosidase activity is observed after addition of 3 mM ZnCl2
additional information
-
no inhibition by 4-nitrophenyl-alpha-mannoside, mannitol, L-mannono-1,4-lactone, PMSF
-
additional information
-
mannosidase IA and B are quite similar in response to inhibitors
-
additional information
-
no inhibition by L-cysteine
-
additional information
-
no inhibition by mannose, alpha1,6-linked mannose oligosaccharide, castanospermine, deoxynojirimycin, 2,5-dihydroxymethyl-3,4-dihydroxypyrrolidine
-
additional information
-
no inhibition by swainsonine; no or little inhibition by N,N-dimethyl-1-deoxymannojirimycin
-
additional information
-
no inhibition by Ca2+; no inhibition by Mg2+
-
additional information
-
no inhibition by Mg2+
-
additional information
-
-
-
additional information
-
-
-
additional information
-
no inhibition by mannostatin A
-
additional information
-
-
-
additional information
-
no inhibition by mannostatin A
-
additional information
-
-
-
additional information
-
no inhibition by swainsonine
-
additional information
-
no inhibition by swainsonine
-
additional information
P31723
comparison with 1-deoxymannojirimycin and kifunensine
-
additional information
-
staurosporine and genistein have an effect, tesing arrested intracellular turnover in response to selective inhibition of serine kinase activity
-
additional information
-
shift in migration is due to mannose trimming. Effects are not observed with the class II mannosidase inhibitor swainsonine
-
additional information
-
cycloheximide, protein synthesis inhibitor. After a 2 h treatment with the protein synthesis inhibitor cycloheximide, ER and Golgi labeling observed with ManI-GFP fusion remains unchanged, showing that the steady state localization of ManI-GFP is the Golgi and the ER
-
additional information
-
not inhibited by swainsonine
-
additional information
-
MNS1, MNS2, and MNS3 are not sensitive to inhibition by swainsonine
-
additional information
O60476, Q9NR34
isoform ManIA2 is not influenced by swainsonine
-
additional information
-
not affected by EDTA
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
phosphatidylcholine
-
activation, with acyl-chains of different lengths, above C-4
phosphatidylethanolamine
-
activation, in the presence of 3.5 mM Triton X-100
Triton X-100
-
activation together with zwitterionic phospholipids
Triton X-100
-
0.1%; activation
Triton X-100
-
0.12%, no activation at 0.07% and below; requirement
Zwitterionic phospholipids
-
activation, required for solubilized and purified enzyme, independent of acyl chain length or degree of saturation, an ordered lipid structure of either micelles or bilayers, mixed micelles together with Triton X-100
-
additional information
-
no activation by negatively charged phospholipids, dibutyryl-phosphocholine
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.26
(Man)6GlcNAc
-
40C, pH 5.5
0.1
(Man)8GlcNAc
-
37C, pH 6.5
0.3
(Man)9GlcNAc
-
-
0.3
(Man)9GlcNAc
-
pH 6.5
0.57
2-O-alpha-D-Mannopyranosyl-D-mannose
-
37C, pH 5.3
0.04
4-methylumbelliferyl alpha-D-mannopyranoside
-
at pH 7.0 in 50 mM MES-Tris buffer and at 37C
0.07
4-methylumbelliferyl-alpha-D-mannopyranoside
Q9Y8A9
-
0.09
4-methylumbelliferyl-alpha-D-mannopyranoside
-
hydrolysis of the fluorogenic substrate follows hyperbolic kinetics
0.11
4-methylumbelliferyl-alpha-D-mannopyranoside
-
MUaMan, fluorogenic substrate. Vmax 36.2 nmol of 4-methylumbelliferone min-1 mg-1 of protein
0.55
glycoprotein IV from ovalbumin
-
pH 6.0
-
0.296
Manalpha(1,2)Man-O-Me
-
pH 5.0, 30C, mutant enzyme C334A
0.719
Manalpha(1,2)Man-O-Me
-
pH 5.0, 30C, mutant enzyme C443A; pH 5.0, 30C, wild-type enzyme
0.78
Manalpha(1,2)Man-O-Me
-
pH 5.0, 30C, mutant enzyme C363A
0.015
Manalpha(1-2)Manalpha(1-3)Manalpha(1-6)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAc
-
37C, pH 6.5, mutant enzyme T688A
0.068
Manalpha(1-2)Manalpha(1-3)Manalpha(1-6)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAc
-
37C, pH 5.3, mutant enzyme E330Q
0.11
Manalpha(1-2)Manalpha(1-3)Manalpha(1-6)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAc
-
37C, pH 7.0, wild-type enzyme
0.12
Manalpha(1-2)Manalpha(1-3)Manalpha(1-6)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAc
-
37C, pH 6.8, mutant enzyme F659A
0.33
Manalpha(1-2)Manalpha(1-3)Manalpha(1-6)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAc
-
37C, pH 6.5, mutant enzyme R461L
0.47
Manalpha(1-2)Manalpha(1-3)Manalpha(1-6)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAc
-
37C, pH 6.5, mutant enzyme R597A
0.51
Manalpha(1-2)Manalpha(1-3)Manalpha(1-6)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAc
-
37C, pH 6.5, mutant enzyme R461A
1.25
Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAc
-
-
0.068
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
-
37C, pH 5.3, pyridylamine-tagged Man9GlcNAc2, mutant enzyme E330Q
0.09
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
-
37C, pH 7.1, pyridylamine-tagged Man9GlcNAc2, mutant enzyme E330Q
0.11
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
-
37C, pH 6.8, pyridylamine-tagged Man9GlcNAc2, mutant enzyme D463N; 37C, pH 7.1, pyridylamine-tagged Man9GlcNAc2, wild-type enzyme
0.15
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
-
37C, pH 6.6, pyridylamine-tagged Man9GlcNAc2, mutant enzyme E330Q/E599Q
0.16
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
-
37C, pH 6.7, pyridylamine-tagged Man9GlcNAc2, mutant enzyme E599Q
0.21
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
-
37C, pH 6.9, pyridylamine-tagged Man9GlcNAc2, mutant enzyme H524A
0.26
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
-
37C, pH 6.6, pyridylamine-tagged Man9GlcNAc2, mutant enzyme D463N/E599Q
0.67
mannobiose
-
pH 5.0
0.087
p-nitrophenyl-alpha-D-mannoside
-
37C, pH 6.1
0.6
methyl-mannopyranosyl-mannopyranoside
-
37C, pH 6.0
-
additional information
additional information
-
kinetic constants of various substrate derivatives
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3.87
Manalpha(1,2)Man-O-Me
-
pH 5.0, 30C, mutant enzyme C334A
6.67
Manalpha(1,2)Man-O-Me
-
pH 5.0, 30C, mutant enzyme C443A
8.51
Manalpha(1,2)Man-O-Me
-
pH 5.0, 30C, wild-type enzyme
9.48
Manalpha(1,2)Man-O-Me
-
pH 5.0, 30C, mutant enzyme C363A
0.03
Manalpha(1-2)Manalpha(1-3)Manalpha(1-6)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAc
-
37C, pH 6.8, mutant enzyme F659A
0.06
Manalpha(1-2)Manalpha(1-3)Manalpha(1-6)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAc
-
37C, pH 6.5, mutant enzyme T688A
0.07
Manalpha(1-2)Manalpha(1-3)Manalpha(1-6)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAc
-
37C, pH 6.5, mutant enzyme R461L
0.084
Manalpha(1-2)Manalpha(1-3)Manalpha(1-6)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAc
-
37C, pH 5.3, mutant enzyme E330Q
0.11
Manalpha(1-2)Manalpha(1-3)Manalpha(1-6)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAc
-
37C, pH 6.5, mutant enzyme R597A
0.6
Manalpha(1-2)Manalpha(1-3)Manalpha(1-6)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAc
-
37C, pH 6.5, mutant enzyme R461A
3.7
Manalpha(1-2)Manalpha(1-3)Manalpha(1-6)Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAc
-
37C, pH 7.0, wild-type enzyme
0.000026
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
-
37C, pH 6.7, pyridylamine-tagged Man9GlcNAc2, mutant enzyme E599Q
0.000027
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
-
37C, pH 6.6, pyridylamine-tagged Man9GlcNAc2, mutant enzyme D463N/E599Q
0.00028
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
-
37C, pH 6.6, pyridylamine-tagged Man9GlcNAc2, mutant enzyme E330Q/E599Q
0.0046
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
-
37C, pH 6.8, pyridylamine-tagged Man9GlcNAc2, mutant enzyme D463N
0.018
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
-
37C, pH 7.1, pyridylamine-tagged Man9GlcNAc2, mutant enzyme E330Q
0.084
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
-
37C, pH 5.3, pyridylamine-tagged Man9GlcNAc2, mutant enzyme E330Q
0.86
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
-
37C, pH 6.9, pyridylamine-tagged Man9GlcNAc2, mutant enzyme H524A
3.7
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
-
37C, pH 7.1, pyridylamine-tagged Man9GlcNAc2, wild-type enzyme
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.002
D-mannono-delta-lactam
-
pH 6.1, 37C
0.006
kifunensine
-
pH 6.1, 37C
0.6
methyl-alpha-D-lyxopyranosyl-(1',2)-alpha-D-mannopyranoside
P31723
-
0.0001
swainsonine
-
pH 6.1, 37C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.019
1-deoxymannojirimycin
Q9Y8A9
-
0.03
1-deoxymannojirimycin
-
class I alpha-mannosidase MNS1, using methyl-2-O-alpha-D-mannopyranosyl-alpha-D-mannopyranoside as substrate
0.035
1-deoxymannojirimycin
-
class I alpha-mannosidase MNS3, using methyl-2-O-alpha-D-mannopyranosyl-alpha-D-mannopyranoside as substrate
0.04
1-deoxymannojirimycin
-
class I alpha-mannosidase MNS2, using methyl-2-O-alpha-D-mannopyranosyl-alpha-D-mannopyranoside as substrate
0.12
1-deoxymannojirimycin
-
at pH 7.0 in 50 mM MES-Tris buffer and at 37C
0.22
1-deoxymannojirimycin
Q8J0Q0
-
0.23
1-deoxymannojirimycin
-
inhibition of 4-methylumbelliferyl-alpha-D-mannopyranoside hydrolysis
0.2
1-deoxymmanojirimycin
-
inhibits hydrolysis of 4-methylumbelliferyl-alpha-D-mannopyranoside
-
0.0003
kifunensine
-
class I alpha-mannosidase MNS3, using methyl-2-O-alpha-D-mannopyranosyl-alpha-D-mannopyranoside as substrate
0.00035
kifunensine
-
class I alpha-mannosidase MNS1, using methyl-2-O-alpha-D-mannopyranosyl-alpha-D-mannopyranoside as substrate
0.00047
kifunensine
-
class I alpha-mannosidase MNS2, using methyl-2-O-alpha-D-mannopyranosyl-alpha-D-mannopyranoside as substrate
0.47
swainsonine
-
inhibition of 4-methylumbelliferyl-alpha-D-mannopyranoside hydrolysis
0.54
swainsonine
Q8J0Q0
-
0.55
swainsonine
-
inhibits hydrolysis of 4-methylumbelliferyl-alpha-D-mannopyranoside
0.56
swainsonine
-
at pH 7.0 in 50 mM MES-Tris buffer and at 37C
0.62
swainsonine
Q9Y8A9
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0000036
-
40C, pH 5.5
0.00003
-
purification of soluble alpha-mannosidase from CAI-4 strain, High-speed supernatant used to measure alpha-mannosidase activity
0.00008
-
purification of soluble alpha-mannosidase from CAI-4 strain, Sepharose CL6B
0.0002
-
mixed membrane fraction (MMF) of ATCC 26555 supernatant, expressed as nanomol of methylumbelliferone min-1mg-1 of protein
0.0005
-
mixed membrane fraction (MMF) of CAI-4 and ATCC 26555 plus 1 mM pepstatin supernatant, expressed as nanomol of methylumbelliferone min-1mg-1 of protein; mixed membrane fraction (MMF) of CAI-4 supernatant, expressed as nanomol of methylumbelliferone min-1mg-1 of protein
0.0012
-
mixed membrane fraction (MMF) of CAI-4 and ATCC 26555 pellet, expressed as nanomol of methylumbelliferone min-1mg-1 of protein
0.0019
-
mixed membrane fraction (MMF) of ATCC 26555 pellet, expressed as nanomol of methylumbelliferone min-1mg-1 of protein
0.0021
-
purification of soluble alpha-mannosidase from CAI-4 strain, DEAE Bio-Gel A
0.0022
-
mixed membrane fraction (MMF) of CAI-4 and ATCC 26555 plus 1 mM pepstatin pellet, expressed as nanomol of methylumbelliferone min-1mg-1 of protein
0.0026
-
mixed membrane fraction (MMF) of CAI-4 pellet, expressed as nanomol of methylumbelliferone min-1mg-1 of protein
0.003
-
purification of soluble alpha-mannosidase from CAI-4 strain, Sephadex G-25
0.0047
-
mixed membrane fraction (MMF) of CAI-4 and ATCC 26555 supernatant, expressed as nanomol of methylumbelliferone min-1mg-1 of protein
0.0057
-
purification of soluble alpha-mannosidase from CAI-4 strain, DEAE Bio-Gel A
0.0101
-
purification of soluble alpha-mannosidase from CAI-4 strain, Con A-Sepharose
0.0108
-
purification of soluble alpha-mannosidase from CAI-4 strain, Sephadex G-25
0.0908
Q8J0Q0
Candida albicans kex-2-delta-mutant
0.0946
Q8J0Q0
Candida albicans strain CAI4
34.6
-
37C, pH 5.0
4000
-
37C, pH 7.0
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
model for substrate and conformer specificity, computational study
additional information
-
modeling studies, molecular basis of difference in specificity, distinction of subgroup 1 and 2
additional information
-
-
additional information
-
hydrolysis of the fluorogenic substrate 4-methylumbelliferyl-alpha-D-mannopyranoside follows hyperbolic kinetics and LineweaverBurk plots reveals Vmax values of 30.9 nmol of methylumbelliferone min-1 mg-1 of protein
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.9 - 5.3
-
2-O-alpha-D-mannopyranosyl-D-mannose as substrate
5 - 6
-
in the presence of 10 mM CaCl2
5
-
Manalpha(1-2)Man as substrate
5.3
Q9UKM7
mutant enzyme E330Q
5.5 - 6
-
-
5.5 - 6.5
-
in the presence of egg yolk lyso-phosphatidylcholine
5.5
-
hydrolysis of 1,2-alpha-mannobiose
5.9 - 6.5
-
-
6 - 6.2
-
-
6 - 6.5
-
(Man)8(GlcNAc)2-peptide as substrate
6 - 6.5
O60476, Q9NR34
isoform ManIC
6
-
mannosidase IA and B
6
-
optimum activity
6
-
isozyme MANIb
6.5 - 7
O60476, Q9NR34
isoform ManIA2
6.5
-
in the presence of soybean phosphatidylinositol
6.5
-
mutant enzyme T688A, R461A and R461L
6.6
-
mutant enzyme E330Q/E599Q and D463N/E599Q
6.7
-
mutant enzyme E599Q
6.8
-
mutant enzyme D463N
6.8
-
mutant enzyme F659A
6.9
-
mutant enzyme H524A
7
-
wild-type enzyme
7
-
isozyme MANIa
7.1
-
wild-type enzyme
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 5.8
-
about half-maximal activity at pH 4 and 5.8, 0.1 M acetate buffer
4.8 - 6.8
-
about half-maximal activity at pH 4.8 and 6.8
5.2 - 6.7
-
about half-maximal activity at pH 5.2 and 6.7
5.2 - 7.3
-
about half-maximal activity at pH 5.2 and 7.3, in the presence of egg yolk lyso-phosphatidylcholine
5.3 - 6.6
-
about half-maximal activity at pH 5.3 and 6.6
5.5 - 7
-
about half-maximal activity at pH 5.5 and 7; (Man)8(GlcNAc)2-peptide as substrate
5.5 - 7
-
about half-maximal activity at pH 5.5 and 7
5.5 - 7.5
-
about half-maximal activity at pH 5.5 and 7.5, in the presence of soybean phosphatidylinositol
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
-
isozymes MANIa and MANIb
35
O60476, Q9NR34
isoform ManIC
37
-
assay at
37
-
assay at
37
-
assay at
37
-
assay at
37
-
assay at
37
-
assay at
37
-
assay at
37
-
optimum activity
37
-
1 h incubation
37
Q9Y8A9
-
40
-
assay at
40
O60476, Q9NR34
isoform ManIA2
45
-
hydrolysis of 1,2-alpha-mannobiose
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
45 - 60
-
45C: optimum, 60C: 60% of maximal activity, 65C: 14% of maximal activity, hydrolysis of 1,2-alpha-mannobiose
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3.6
-
isoelectric focussing
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
P39098, P45700
In situ hybridization shows high levels of alpha1,2-mannosidase IB
Manually annotated by BRENDA team
P39098, P45700
levels of Golgi alpha1,2-mannosidase IC are similar in most tissues, with the exception of placenta and liver
Manually annotated by BRENDA team
-
Taka-diastase, enzyme-product from Sankyo Co.
Manually annotated by BRENDA team
-
commercially available under the name of Morushin
Manually annotated by BRENDA team
Bacillus sp. M-90
-
-
-
Manually annotated by BRENDA team
P39098, P45700
In situ hybridization shows high levels of alpha1,2-mannosidase IA
Manually annotated by BRENDA team
P39098, P45700
In situ hybridization shows high levels of alpha1,2-mannosidase IB
Manually annotated by BRENDA team
P39098, P45700
Golgi alpha1,2-mannosidase IA
Manually annotated by BRENDA team
P39098, P45700
Golgi alpha1,2-mannosidase IA
Manually annotated by BRENDA team
P39098, P45700
In situ hybridization shows high levels of alpha1,2-mannosidase IB
Manually annotated by BRENDA team
P39098, P45700
levels of Golgi alpha1,2-mannosidase IC are similar in most tissues, with the exception of placenta and liver
Manually annotated by BRENDA team
P39098, P45700
Golgi alpha1,2-mannosidase IA
Manually annotated by BRENDA team
P39098, P45700
In situ hybridization shows high levels of alpha1,2-mannosidase IA
Manually annotated by BRENDA team
Rattus norvegicus Sprague-Dawley, Rattus norvegicus Wistar
-
-
-
Manually annotated by BRENDA team
P39098, P45700
Golgi alpha1,2-mannosidase I displays distinct developmental and tissue-specific expression. Expression of Golgi alpha 1,2-mannosidases (IA, IB, IC) investigated by Nothern blot analysis and in situ hybridization
Manually annotated by BRENDA team
P39098, P45700
Golgi alpha1,2-mannosidase I displays distinct developmental and tissue-specific expression. Expression of Golgi alpha 1,2-mannosidases (IA, IB, IC) investigated by Nothern blot analysis and in situ hybridization. In situ hybridization shows high levels of alpha1,2-mannosidase IB
Manually annotated by BRENDA team
P39098, P45700
Golgi alpha1,2-mannosidase I displays distinct developmental and tissue-specific expression. Expression of Golgi alpha 1,2-mannosidases (IA, IB, IC) investigated by Nothern blot analysis and in situ hydridization
Manually annotated by BRENDA team
-
commercially available under the name of Morushin
Manually annotated by BRENDA team
P39098, P45700
Golgi alpha1,2-mannosidase IA
Manually annotated by BRENDA team
P39098, P45700
Golgi alpha1,2-mannosidase IB
Manually annotated by BRENDA team
P39098, P45700
Golgi alpha1,2-mannosidase IA
Manually annotated by BRENDA team
P39098, P45700
In situ hybridization shows high levels of alpha1,2-mannosidase IB
Manually annotated by BRENDA team
P39098, P45700
Golgi alpha1,2-mannosidase IA
Manually annotated by BRENDA team
P39098, P45700
Golgi alpha1,2-mannosidase IB
Manually annotated by BRENDA team
P39098, P45700
Golgi alpha1,2-mannosidase IA
Manually annotated by BRENDA team
P39098, P45700
In situ hybridization shows high levels of alpha1,2-mannosidase IA
Manually annotated by BRENDA team
P39098, P45700
In situ hybridization shows high levels of alpha1,2-mannosidase IB, Golgi alpha1,2-mannosidase IB
Manually annotated by BRENDA team
P39098, P45700
Golgi alpha1,2-mannosidase IA
Manually annotated by BRENDA team
P39098, P45700
Golgi alpha1,2-mannosidase IB
Manually annotated by BRENDA team
additional information
Q3HYC1
detected in the coccidioidal T27K vaccine
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
2 enzymes: a membrane-bound microsomal and a soluble cytoplasmic one
Manually annotated by BRENDA team
Q8J0Q0
isoform E-I
Manually annotated by BRENDA team
Q8J0Q0
65000 Da membrane-bound isoform
Manually annotated by BRENDA team
-
pericentriolar endoplasmic reticulum-derived quality control compartment
Manually annotated by BRENDA team
-
with the catalytic domain within the lumen of this compartment
Manually annotated by BRENDA team
Caenorhabditis elegans N2 Bristol
-
-
-
Manually annotated by BRENDA team
Sporothrix schenckii EH206
-
with the catalytic domain within the lumen of this compartment
-
Manually annotated by BRENDA team
-
with strain 22A1, the ratio of intracellular to extracellular 1,2-alpha-mannosidase activity is about 4:1
-
Manually annotated by BRENDA team
-
different fusion proteins analyzed to determine if the portion of ManI located in the Golgi lumen plays a role in the targeting of this glycosidase to the Golgi and the ER membranes
Manually annotated by BRENDA team
Q9SEH8
different fusion proteins analyzed to determine if the portion of ManI located in the Golgi lumen plays a role in the targeting of this glycosidase to the Golgi and the ER membranes
Manually annotated by BRENDA team
-
different fusion proteins analyzed to determine if the portion of ManI located in the Golgi lumen plays a role in the targeting of this glycosidase to the Golgi and the ER membranes
Manually annotated by BRENDA team
Rattus norvegicus Sprague-Dawley, Rattus norvegicus Wistar
-
-
-
Manually annotated by BRENDA team
Q8J0Q0
presence of a 65000 Da membrane-bound isoform that is cleaved by protease Kex2 to soluble 52000 Da isoform E-I
-
Manually annotated by BRENDA team
-
with strain 22A1, the ratio of intracellular to extracellular 1,2-alpha-mannosidase activity is about 4:1
Manually annotated by BRENDA team
Caenorhabditis elegans N2 Bristol
-
-
-
Manually annotated by BRENDA team
-
type II membrane protein
Manually annotated by BRENDA team
-
type II membrane protein
Manually annotated by BRENDA team
-
2 enzymes: a membrane-bound microsomal and a soluble cytoplasmic one
Manually annotated by BRENDA team
Rattus norvegicus Sprague-Dawley, Rattus norvegicus Wistar
-
-
-
Manually annotated by BRENDA team
-
2 enzymes: a membrane-bound microsomal and a soluble cytoplasmic one
-
Manually annotated by BRENDA team
-
trans-membrane protein with cytosolic domain
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
23000
-
analytical electrophoresis of the purified enzyme reveals two polypeptides of 52 and 23 kDa, 52000 Da polypeptide being responsible for enzyme activity as revealed by zymogram analysis
677614
27000
-
analytical electrophoresis of the purified preparation reveals two polypeptides
679890
39000
-
cytosolic enzyme, gel filtration
646575
40000
-
gel filtration
646584
43000
-
Candida albicans CAI-4 mutant generating an active 43 kDa polypeptide. Zymogram analysis shows that the single proteolytic product of 43 kDa is able to hydrolyze the fluorogenic substrate and, this is not observed when proteolysis is blocked by pepstatin; purified alpha-mannosidase E-II remains unaltered after treatment with aspartyl protease and retains full activity on artificial substrate 4-methylumbelliferyl-alpha-D-mannopyranoside
677614
43000
-
converting the 52 kDa alpha-mannosidase into a polypeptide of 43 kDa retaining full enzyme activity demonstrated in membranes of ATCC 26555, support a precursor-product relationship between soluble alpha1,2-mannosidase E-I (52 kDa) and alpha1,2-mannosidase E-II (43 kDa)
679890
49000
-
gel filtration
136000
49200
-
sedimentation analysis
646584
50000
-
gel filtration
646606
52000
-
alpha1,2-mannosidase E-I. Analytical electrophoresis of the purified enzyme reveals two polypeptides of 52 and 23 kDa, 52000 Da polypeptide being responsible for enzyme activity as revealed by zymogram analysis
677614
52000
-
analytical electrophoresis of the purified preparation reveals two polypeptides. Responsible for enzyme activity. Active on the fluorogenic substrate 4-methylumbelliferyl-alpha-D-mannopyranoside as revealed by zymogram analysis
679890
52000
Q8J0Q0
E-I, cytosoloc fraction, Golgi-derived vesicles, SDS-PAGE; gel fitlration, isoform E-I
700048
56920
Q3HYC1
theoretical molecular weight. SDS-PAGE, Western blot analysis. A highly purified fraction is obtained after FPLC
677573
57000
-
calculated from amino acid sequence
703328
60000
-
His-tagged isozymes MANIa and MANIb, SDS-PAGE
703909
61200
-
MALDI-TOF mass spectrometry
703328
63000
-
Man1p-His6 fusion protein, SDS-PAGE
703328
65000
-
detected in freshly prepared crude microsomal extracts using polyclonal antibodies, during purification the native enzyme, MW 65000, loses a membrane-spanning domain without losing its catalytic activity
646583
65000
Q8J0Q0
membrane bound, SDS-PAGE
700048
79000
-
Western blotting of cell lysates, transiently expressed recombinant human ER mannosidase I is absent from mock transfected cells but detected as a single immunoreactive 79 kDa band following transient expression
680869
82000
-
SDS-PAGE
699109
150000 - 160000
-
gel filtration
646608
230000
-
PAGE
646585
329000
-
gel filtration
646610
380000
-
-
646592
460000
-
microsomal enzyme, gel filtration, presumably in a micelle or aggregate containing detergent, phospholipid or other protein
646575
additional information
-
amino acid composition
135991
additional information
-
amino acid composition
646584
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 56000, SDS-PAGE
?
-
x * 58000, SDS-PAGE
?
-
x * 67000, SDS-PAGE
?
-
x * 63000, SDS-PAGE
?
Q9Y8A9
x * 65000, SDS-PAGE
?
-
x * 75000, SDS-PAGE
?
-
x * 64000, SDS-PAGE
?
-
x * 73000, deduced from gene sequence, type-II transmembrane protein
?
-
x * 71000, deduced from gene sequence, type-II transmembrane protein
?
Sporothrix schenckii EH206
-
x * 75000, SDS-PAGE
-
dimer
-
2 * 76000, SDS-PAGE
dimer
-
2 * 190000
dimer
Bacillus sp. M-90
-
2 * 190000
-
monomer
P31723
-
monomer
-
1 * 42000, SDS-PAGE
monomer
-
1 * 49000, SDS-PAGE
monomer
-
1 * 52000, SDS-PAGE, under reducing and non-reducing conditions
monomer
Q8J0Q0
1 * 52000, SDS-PAGE, isoform E-I
tetramer
-
4 * 57000-58000, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
-
-
glycoprotein
-
19.4% neutral and 3.9% amino sugars
proteolytic modification
Q8J0Q0
converting via Kex2-protease
glycoprotein
-
three potential N-glycosylation sites, one of which is used
glycoprotein
-
-
glycoprotein
Magnaporthe oryzae Guy11
-
-
-
glycoprotein
-
-
glycoprotein
-
-
glycoprotein
-
0.88% hexoses
glycoprotein
-
not glycosilated
glycoprotein
-
-
additional information
-
contains two disulfide bonds and one free thiol group, soluble catalytic domain, recombinant enzyme
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
co-complex with an uncleaved thiodisaccharide substrate analog, hanging drop vapor diffusion method
-
docking studies
-
in complex with kifunensine
-
hanging drop vapor diffusion method, 15 A resolution
P45700
crystals of both the native protein and the protein-inhibitor complex. Superimpositions are performed with LSQMAN. Comparison with human alpha-1,2-mannosidasethiodisaccharide complex; 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
P31723
native protein and in complex with inhibitor kifunensine or 1-deoxymannojirimycin
-
docking studies, twelve of the 38 possible conformers of beta-D-mannopyranosyl-1C4 optimally docked in subsite-1 of the active site
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5 - 6.5
-
isozyme MANIb
703909
5 - 10
-
isozyme MANIa
703909
5
-
above, stable
646584
5.5 - 6
O60476, Q9NR34
isoform ManIC is stable (more than 75% activity) in the pH range of 5.5-6.0 at 37C for 90 min
715684
6.5 - 8
O60476, Q9NR34
isoform ManIA2 is stable (more than 75% activity) in the pH range of 6.5-8.0 at 37C for 90 min
715684
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 30
O60476, Q9NR34
isoform ManIA2 shows more than 75% activity at 30C in the presence of Ca2+, and more than 75% activity at 20C in the absence of Ca2+
715684
25
-
isozymes MANIa and MANIb are relatively stable at lower temperature and still retain 50% of their original activities after incubation at 25C for 1 h and show a significant decrease of activities at higher temperatures with 10% activity at 30C
703909
37
-
24 h, in 0.1 M sodium acetate buffer, pH 5.8, 30% loss of activity
135998
40
O60476, Q9NR34
isoform ManIC shows more than 75% activity at 40C in the absence and presence of Ca2+
715684
50
-
mannosidase IB less stable than IA
135998
50
-
1 h, in 0.1 M acetate buffer, pH 5, 10% loss of activity
136000
50
-
90 min, about 60-70% loss of activity
646570
50
-
Tm-value of mutant enzyme C443G, C334A, C363A and C443S
664373
52
-
Tm-value of mutant enzyme C443A
664373
53
-
Tm-value of mutant enzyme C443T
664373
56
-
Tm-value of wild-type enzyme
664373
additional information
-
mannosidase IA and B differ in thermostability
135998
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
ER degradation-enhancing-mannosidase-like protein
-
mannosidase IA and B differ in sensitivity to storage in liver cytoplasmic extracts, no interconversion between mannosidase IA and IB during cellulose phosphate chromatography
-
enzyme loses a membrane-spanning domain during purification which does not alter its catalytic properties
-
native enzyme protein is highly susceptible to proteolytic cleavage, not by glucopeptidase F
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4C, pH 4.5-6, at least 6 months
-
-20C, in 10 mM sodium acetate buffer, pH 5, with or without 1 mM CaCl2, at least 4 months
-
4C, in 10 mM sodium acetate buffer, pH 5, with or without 1 mM CaCl2, at least 4 months
-
-20C, in 10 mM HEPES/NaOH, pH 7.5, 2 mM MgCl2, 0.1% Nonidet-P40, 0.2 M NaCl, less than 10% loss of activity within 3 months
-
0-4C, in 10 mM potassium phosphate buffer, pH 7.2, 0.5% Triton X-100, 4-6 months
-
2-4C, in 10 mM potassium phosphate buffer, pH 7.2, 1% Triton X-100, 20% loss within 4 weeks
-
4C, 1 mg protein/ml, in 50 mM phosphate buffer, pH 6.5, 5 mM MgCl2, 0.1% Triton X-100, 30 days
-
0-4C, in buffer with 10% glycerol, purified enzyme, a few days, partially purified enzyme, at least 2 weeks
-
4C, in buffer with 10% glycerol, a few days, at early stage of purification at least 2 weeks
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Co2+-affinity column chromatography
-
affinity chromatography with baker's yeast mannan gel
-
by conventional methods of protein isolation and affinity chromatography in Concanavalin A-Sepharose 4B. Alpha-mannosidase E-I is purified by a fungal aspartyl protease
-
ion exchange chromatography, used to measure protein and enzyme activity, Sepharose CL6B, DEAE Bio-Gel A, Sephadex G-25, DEAE Bio-Gel A, Con A-Sepharose, Sephadex G-25
-
protein identification by tandem mass spectrometry. Gel filtration
Q3HYC1
partial
-
Talon Co2+ affinity resin column chromatography; Talon Co2+ affinity resin column chromatography
O60476, Q9NR34
Ni-NTA column chromatography
-
partial, solubilization requires non-ionic detergents
-
recombinant alpha-1,2-mannosidase is purified from the medium by chromatography on CM-Toyopearl 650M after ammonium sulfate precipitation
P31723
enzyme from endoplasmic reticulum
-
mannosidase IA
-
recombinant enzyme
-
ultracentrifugation and IgG bead column chromatography
-
DEAE Bio-Gel A column chromatography
-
affinity chromatography on immobilized N-5-carboxypentyl-1-deoxymannojirimycin
-
affinity chromatography on mannan and mannosamine-Sepharose
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Nicotiana benthamiana leaf epidermal cells
-
expressed in Sf9 cells as insoluble forms and in Escherichia coli as soluble forms
-
GFP-fusions are transferred into Agrobacterium tumefaciens by heat shock
-
expression by an Aspergillus host
-
expressed in Escherichia coli
Q8J0Q0
expression in Escherichia coli
Q9Y8A9
expressed in TOP10 chemically competent Escherichia coli cells
Q3HYC1
GFP-fusions are transferred into Agrobacterium tumefaciens by heat shock
Q9SEH8
expressed in Escherichia coli JM109 (DE3) cells; expressed in Escherichia coli JM109 (DE3) cells
O60476, Q9NR34
expressed in Pichia pastoris
-
overexpressed in HEK-293 cells
-
expressed in Pichia pastoris
-
overexpressed in HEK-293 cells; overexpressed in HEK-293 cells
P39098
GFP-fusions are transferred into Agrobacterium tumefaciens by heat shock
-
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
P31723
expressed in Pichia pastoris
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
homozygosity for the minor A allele rs4567(A), but not rs4567(G), suppresses ERManI translation under endoplasmic reticulum stress conditions
-
increased expression after anti-CD3 stimulation
-
T cell receptor signaling enhances mRNA levels of MIa,b,c
-
alpha-1,2-mannosidase expression increases in CD25+CD4+ regulatory T cells when they encounter alloantigen in vivo
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C334A
-
Tm-value of mutant enzyme is 49.6C compared to 55.8C for the wild-type enzyme. Km-value is 2.4fold lower than wild-type value, turnover-number is 2.2fold lower than wild-type value
C363A
-
Tm-value of mutant enzyme is 49.6C compared to 55.8C for the wild-type enzyme. Km-value is 1.1fold higher than wild-type value, turnover-number is 1.1fold lower than wild-type value
C443A
-
Tm-value of mutant enzyme is 51.9C compared to 55.8C for the wild-type enzyme. Km-value is identical to wild-type value, turnover-number is 1.3fold lower than wild-type value
C443D
-
relative activity is less than 50% of wild-tzype activity
C443G
-
Tm-value of mutant enzyme is 50.2C compared to 55.8C for the wild-type enzyme
C443L
-
relative activity is less than 50% of wild-tzype activity
C443M
-
relative activity is less than 50% of wild-tzype activity
C443S
-
Tm-value of mutant enzyme is 50.0C compared to 55.8C for the wild-type enzyme
C443T
-
Tm-value of mutant enzyme is 52.8C compared to 55.8C for the wild-type enzyme
C443V
-
relative activity is less than 50% of wild-tzype activity
EP1130
-
enzyme expression reduced
EP1588
-
enzyme expression reduced
EP1628
-
enzyme expression reduced
D463N
-
pH-optimum is 6.8 compared to 7.1 for wild-type enzyme, kcat/Km is 212500fold lower than wild-type value
D463N
-
binding affinity
D463N/E599Q
-
pH-optimum is 6.6 compared to 7.1 for wild-type enzyme, kcat/Km is 8.3fold lower than wild-type value
E220Q
-
the mutant contains a conserved acidic amino acid mutation that abolishes alpha1,2-mannosidase enzyme activity
E330Q
-
pH-optimum for mutant enzyme is 5.3 compared to 7.0 for wild-type enzyme. kcat/Km is 27.5fold lower than wild-type value. Enzyme possesses increased glycan binding affinity but compromised glycan hydrolysis
E330Q
-
pH-optimum is 5.3 compared to 7.1 for wild-type enzyme, kcat/Km is 809.5fold lower than wild-type value
E330Q
-
catalytic mutant, contributes to general acid function
E330Q/E599Q
-
pH-optimum is 6.6 compared to 7.1 for wild-type enzyme, kcat/Km is 340000fold lower than wild-type value
E599Q
-
pH-optimum is 6.7 compared to 7.1 for wild-type enzyme, kcat/Km is 17895fold lower than wild-type value
E599Q
-
general base
F659A
-
pH-optimum for mutant enzyme is 6.8 compared to 7.0 for wild-type enzyme. kcat/Km is 132fold lower than wild-type value
F659A
-
glycone binding affinity, catalysis
R334A
-
mutant enzyme is not detected in the culture medium, kcat/Km is 28.3fold lower than wild-type value
R461A
-
pH-optimum for mutant enzyme is 6.5 compared to 7.0 for wild-type enzyme. kcat/Km is 27.5fold lower than wild-type value
R461A
-
minor contribution to catalysis, glycan binding affinity
R461L
-
pH-optimum for mutant enzyme is 6.5 compared to 7.0 for wild-type enzyme, mutant enzyme exhibits the ability to readily hydrolyze Man9GlcNAc2 to Man6GlcNAc2. kcat/Km is 157fold lower than wild-type value
R461L
-
branch specificity/steric hindrance
R597A
-
pH-optimum for mutant enzyme is 6.5 compared to 7.0 for wild-type enzyme. kcat/Km is 143fold lower than wild-type value
R597A
-
minor contribution to catalysis
T688A
-
pH-optimum for mutant enzyme is 6.5 compared to 7.0 for wild-type enzyme. kcat/Km is 8.25fold lower than wild-type value
T688A
-
Ca2+ tethering, catalysis
F468L
-
naturally occuring mutation, retains enzymic activity but defective in secretion of enzyme
F592S
-
naturally occuring mutation, no enzymic activity
C340S
-
no mutant protein detectable
C385S
-
no mutant protein detectable
C468S
-
Km is 0.7 mM for (Man)9GlcNAc, same specificity as wild type
C471S
-
Km is 0.7 mM for (Man)9GlcNAc, same specificity as wild type
C485S
-
Km is 0.4 mM for (Man)9GlcNAc, same specificity as wild type
D121A
-
putative EF hand Ca2+ binding loop, no effect on Ca2+ binding
D121A/E132V
-
putative EF hand Ca2+ binding loop, no effect on Ca2+ binding
D121N
-
putative EF hand Ca2+ binding loop, no effect on Ca2+ binding
D275N
-
no ability of Ca2+ binding
D86N
-
retains ability of Ca2+ binding, Km value 0.007 mM
E132Q
-
putative EF hand Ca2+ binding loop, no effect on Ca2+ binding, retains ability of Ca2+ binding, Km value 0.3 mM
E132V
-
putative EF hand Ca2+ binding loop, no effect on Ca2+ binding
E279Q
-
no ability of Ca2+ binding
E438Q
-
no ability of Ca2+ binding
E503Q
-
retains ability of Ca2+ binding, but completely inactive
E526Q
-
retains ability of Ca2+ binding, Km value 4 mM
additional information
-
ManI fusion constructs are derived from the full-length GFP fusion
EP982
-
enzyme expression reduced
additional information
Q9SEH8
ManI fusion constructs are derived from the full-length GFP fusion
H524A
-
pH-optimum is 6.9 compared to 7.1 for wild-type enzyme, kcat/Km is 28.3fold lower than wild-type value
additional information
-
genetic-engineered removal of the amino-terminal cytoplasmic tail. Removal of the tail does not influence the remaining structure of the molecule, including the original transmembrane domain, noncleavable ER sorting signal, and proposed stem and catalytic domains. Synthesized with slightly different molecular weights, its absence did not diminish the efficiency of protein translation. Investigation of involvement of the tail by fluorescent fusion proteins
additional information
-
the missense mutations G1418A (DeltaW473), G1189A (E397K) and C1000T (R334C) segregates with nonsyndromic autosomal-recessive intellectual disability
M411T
-
naturally occuring mutation, retains enzymic activity but defective in secretion of enzyme
additional information
P39098, P45700
alpha1,2-mannosidase IB null mice (-/-). Null mice with normal gross appearance at birth, but they display respiratory distress and die within a few hours with evident lung hemorrhage. Demonstrates the specific role of Golgi alpha1,2-mannosidase IB in pulmonary function and development. Histological comparison of lungs from wild type (+/+) and alpha1,2-mannosidase IB null mice (-/-)
additional information
-
knockdown experiments show that ERManI is indeed involved in mannose trimming to Man6-5 leading to endoplasmic reticulum-associated degradation
additional information
-
ManI fusion constructs are derived from the full-length GFP fusion
R273L
-
instead of Man8GlcNAc, substrate is transformed to Man5GlcNAc
additional information
-
ManI fusion constructs are derived from the full-length GFP fusion
additional information
-
deletion of N-terminal 174 amino acids, marginal effects on catalytic properties
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
-
development of anti-cancer therapies