Information on EC 3.2.1.24 - alpha-mannosidase

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

EC NUMBER
COMMENTARY
3.2.1.24
-
RECOMMENDED NAME
GeneOntology No.
alpha-mannosidase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
hydrolysis of terminal, non-reducing alpha-D-mannose residues in alpha-D-mannosides
show the reaction diagram
; also hydrolyses alpha-D-lyxosides and heptopyranosides with the same configuration at C-2, C-3 and C-4 as mannose
-
-
-
hydrolysis of terminal, non-reducing alpha-D-mannose residues in alpha-D-mannosides
show the reaction diagram
active site structure and catalytic residues, e.g. Asn515 involved in substrate binding, reaction mechanism and processing steps, overview
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
hydrolysis of O-glycosyl bond
-
-
-
-
hydrolysis of O-glycosyl bond
-, Q6L2X5
-
hydrolysis of O-glycosyl bond
-
-
transglycosylation
-
-
PATHWAY
KEGG Link
MetaCyc Link
Other glycan degradation
-
SYSTEMATIC NAME
IUBMB Comments
alpha-D-mannoside mannohydrolase
Also hydrolyses alpha-D-lyxosides and heptopyranosides with the same configuration at C-2, C-3 and C-4 as mannose.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
1,2-alpha-D-mannosidase
-
-
-
-
1,2-alpha-mannosidase
-
-
-
-
acid alpha-mannosidase
-
-
acid alpha-mannosidase
-
-
acidic alpha-mannosidase
-
belongs to glycosyl hydrolase 38
acidic alpha-mannosidase
-
-
alpha 1,2-mannosidase
-
-
Alpha mannosidase 6A8B
-
-
-
-
alpha-1,3 mannosidase
Q99YP5
-
alpha-D-mannopyranosidase
-
-
-
-
alpha-D-mannosidase
-
-
-
-
alpha-D-mannosidase
-
-
alpha-D-mannosidase
-
glycohydrolase
Alpha-D-mannoside mannohydrolase
-
-
-
-
alpha-man
-
gene name
alpha-mann
-
-
alpha-mannosidase
-
-
alpha-mannosidase
-
-
alpha-mannosidase
O00754
acidic exoglycosidase, belonging to glycosylhydrolase family 38
alpha-mannosidase
Q68EM8
-
alpha-mannosidase
-
-
alpha-mannosidase
Q6L2X5
-
alpha-mannosidase
Q99YP5
-
alpha-mannosidase C
-
-
alpha-mannosidase E-II
-
-
alpha-mannosidase I
-
-
alpha-mannosidase IA
-
-
alpha-mannosidase III
-
-
alpha1,2-mannosidase
-
-
AMAN
-
-
-
-
class II alpha-mannosidase
-
-
class II alpha-mannosidase
-
-
ER-alpha-mannosidase
-
-
ER-mannosidase II
Q68EM8
-
exo-alpha-mannosidase
-
-
-
-
GH38 alpha-mannosidase
Q97UK5
-
GH38 alpha-mannosidase
Q97UK5
-
-
GH38 alpha-mannosidase II
Q99YP5
-
GH38 class II alpha-mannosidase
Q97UK5
-
GH38 class II alpha-mannosidase
Q97UK5
-
-
GH38 enzyme
Q99YP5
-
Golgi alpha-mannosidase II
-
-
Golgi alpha-mannosidase II
-
-
Golgi alpha-mannosidase II
-
-
Golgi mannosidase IA
-
-
Golgi mannosidase IA
-
-
Golgi mannosidase IB
-
-
Golgi mannosidase IB
-
-
Laman
-
-
-
-
Laman
O00754
-
Lysosomal acid alpha-mannosidase
-
-
-
-
lysosomal alpha-D-mannosidase
-
-
lysosomal alpha-mannosidase
O00754
-
Man2C1
Q68EM8
-
Man2C1 alpha-mannosidase
Q68EM8
-
Man9-alpha-mannosidase
-
-
ManA
Q97UK5
-
-
neutral alpha-mannosidase
-
-
neutral alpha-mannosidase
-
-
neutral alpha-mannosidase
-
-
neutral/cytosol mannosidase
Q68EM8
-
p-nitrophenyl-alpha-mannosidase
-
-
-
-
Ssa-man
Q97UK5
-
Ssa-man
Q97UK5
-
-
SSO3006
Q97UK5
locus name
SSO3006
Q97UK5
locus name; locus name
-
additional information
-
the enzyme belongs to the class 1 alpha1,2-mannosidases of glycosylhydrolase family 47
additional information
Q99YP5
the enzyme belongs to the family GH38 of alpha-mannosidases
additional information
-
the enzyme belongs to the glycoside hydrolase family 38
CAS REGISTRY NUMBER
COMMENTARY
9025-42-7
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
Pekin-type drake
-
-
Manually annotated by BRENDA team
jack bean, stimulates proliferation of B-lymphocytes from mice
-
-
Manually annotated by BRENDA team
two isoforms, enzymes I and II
-
-
Manually annotated by BRENDA team
lysosomal isoform
-
-
Manually annotated by BRENDA team
alpha-mannosidase from Erythrina indica has N-terminal amino acid sequence as DTQEN
-
-
Manually annotated by BRENDA team
chicken
-
-
Manually annotated by BRENDA team
-
Q68EM8
UniProt
Manually annotated by BRENDA team
2 isoforms of neutral alpha-mannosidase
-
-
Manually annotated by BRENDA team
2 isoforms, alpha-mannosidase A, B
-
-
Manually annotated by BRENDA team
MA2B1_HUMAN
UniProt
Manually annotated by BRENDA team
expressed in Pichia pastoris
-
-
Manually annotated by BRENDA team
alfalfa
-
-
Manually annotated by BRENDA team
isoforms A and B
Uniprot
Manually annotated by BRENDA team
alpha-mannosidases I and II
-
-
Manually annotated by BRENDA team
desert and oasis flies studied, male and female, Neot Hakikar (oasis), Jordan Valley spring (wet), Kfar Adumim starved (arid), Jordan Valley autumn (arid)
-
-
Manually annotated by BRENDA team
extremophilic organism belonging to the euryarchaeal phylum
UniProt
Manually annotated by BRENDA team
black cherry
-
-
Manually annotated by BRENDA team
sea squirt
-
-
Manually annotated by BRENDA team
lysosomal type of alpha-D-mannosidase
-
-
Manually annotated by BRENDA team
lysosomal type
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
malfunction
-
alpha-Man RNAi fruits are approximately two times firmer compared with the control and fruit deterioration is delayed by approximately 7 d. It is shown that silencing of alpha-Man enhances fruit shelf life due to the reduced degradation of N-glycoproteins which result in delayed softening
physiological function
Q99YP5
the enzyme is perhaps functioning in the subsequent degradation of extracellular host glycans following their initial digestion by secreted glycosidases
physiological function
-
the enzyme could be putatively involved in the turnover and/or the maturation of glycoprotein
physiological function
-
mutant PBL2025, that misses 50 genes (SSO3004-3050), including genes coding for a multitude of enzymes possibly involved in sugar degradation or metabolism, is complemented with one of the missing proteins, the alpha-mannosidase (SSO3006). The alpha-mannosidase complemented strain resembles the Sulfolobus solfataricus P2 behavior with respect to attachment of cells to glass and growth of cells in static biofilms. During expression of the alpha-mannosidase, glucose and mannose-containing extracellular polymeric substance levels changes in the recombinant strain during surface attachment and biofilm formation. alpha-Mannosidase might be involved in the modulation of the extracellular polymeric substance composition and/or in the de-mannosylation of the glycan tree, which is attached to extracellular glycosylated proteins in Sulfolobus solfataricus
physiological function
-
mutant PBL2025, that misses 50 genes (SSO3004-3050), including genes coding for a multitude of enzymes possibly involved in sugar degradation or metabolism, is complemented with one of the missing proteins, the alpha-mannosidase (SSO3006). The alpha-mannosidase complemented strain resembles the Sulfolobus solfataricus P2 behavior with respect to attachment of cells to glass and growth of cells in static biofilms. During expression of the alpha-mannosidase, glucose and mannose-containing extracellular polymeric substance levels changes in the recombinant strain during surface attachment and biofilm formation. alpha-Mannosidase might be involved in the modulation of the extracellular polymeric substance composition and/or in the de-mannosylation of the glycan tree, which is attached to extracellular glycosylated proteins in Sulfolobus solfataricus; the enzyme could be putatively involved in the turnover and/or the maturation of glycoprotein
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1,2-alpha-D-mannobiose + H2O
alpha-D-mannose
show the reaction diagram
-, Q6L2X5
-
-
-
?
1,3-alpha-D-mannobiose + H2O
alpha-D-mannose
show the reaction diagram
-, Q6L2X5
-
-
-
?
1,6-alpha-D-mannobiose + H2O
alpha-D-mannose
show the reaction diagram
-, Q6L2X5
-
-
-
?
1-naphthyl-alpha-D-mannopyranoside + H2O
1-naphthol + alpha-D-mannopyranose
show the reaction diagram
-
-
-
?
2 Man9GlcNAc + 3 H2O
Man8GlcNAc + Man7GlcNAc + 3 alpha-D-mannopyranose
show the reaction diagram
-
-
products from unbound fraction of cobalt-chelating Sepharose
?
2,4-dinitrophenyl alpha-D-mannopyranoside + H2O
2,4-dinitrophenol + alpha-D-mannopyranose
show the reaction diagram
-
-
-
-
?
2,4-dinitrophenyl alpha-D-mannopyranoside + H2O
2,4-dinitrophenol + alpha-D-mannopyranose
show the reaction diagram
Q99YP5
-
-
-
?
2,4-dinitrophenyl alpha-D-mannoside + H2O
2,4-dinitrophenol + alpha-D-mannose
show the reaction diagram
-
-
-
-
?
2,4-dinitrophenyl-alpha-D-mannopyranoside + H2O
2,4-dinitrophenol + alpha-D-mannopyranose
show the reaction diagram
-
-
-
-
?
2,5-dinitrophenyl-alpha-D-mannopyranoside + H2O
2,4-dinitrophenol + D-mannose
show the reaction diagram
-
-
-
-
?
2-acetamido-4-O-alpha-D-mannopyranosyl-2-deoxy-D-glucose + H2O
alpha-D-mannopyranose + ?
show the reaction diagram
-
-
-
?
2-deoxy-2-fluoro-alpha-D-mannosyl fluoride + H2O
?
show the reaction diagram
-
substrate for wild-type enzyme and very slow substrate of mutant enzyme D341N
-
-
?
2-O-alpha-D-mannopyranosyl-D-mannopyranose + H2O
alpha-D-mannopyranose + D-mannopyranose
show the reaction diagram
-
-
-
?
2-O-alpha-D-mannopyranosyl-D-mannopyranose + H2O
alpha-D-mannopyranose + D-mannopyranose
show the reaction diagram
-
very low activity
-
?
2-O-alpha-D-mannopyranosyl-D-mannopyranose + H2O
alpha-D-mannopyranose + D-mannopyranose
show the reaction diagram
-
highly specific for alpha-1,2-mannosidic linkages
-
?
2-O-alpha-D-mannopyranosyl-D-mannopyranose + H2O
alpha-D-mannopyranose
show the reaction diagram
-
-
-
?
2-O-alpha-D-mannopyranosyl-D-mannopyranose + H2O
alpha-D-mannopyranose
show the reaction diagram
-
very low activity
-
?
2-O-alpha-D-mannopyranosyl-D-mannopyranose + H2O
alpha-D-mannopyranose
show the reaction diagram
-
highly specific for alpha-1,2-mannosidic linkages
-
?
2-O-alpha-D-mannotriose + H2O
alpha-D-mannopyranose + ?
show the reaction diagram
-
highly specific for alpha-1,2-mannosidic linkages
-
?
3-O-alpha-D-mannopyranosyl-alpha-D-mannopyranose + H2O
alpha-D-mannopyranose
show the reaction diagram
Q99YP5
the enzyme is only active with the alpha-1,3-linked disaccharide
-
-
?
3-O-alpha-D-mannopyranosyl-D-mannopyranose + H2O
2 alpha-D-mannopyranose
show the reaction diagram
-
very low activity
-
?
3-O-alpha-D-mannopyranosyl-D-mannopyranose + H2O
2 alpha-D-mannopyranose
show the reaction diagram
-
very low activity
-
?
4-methylumbelliferyl alpha-D-mannopyranoside + H2O
4-methylumbelliferone + alpha-D-mannopyranose
show the reaction diagram
-
-
-
-
?
4-methylumbelliferyl alpha-D-mannopyranoside + H2O
4-methylumbelliferone + alpha-D-mannose
show the reaction diagram
-
pH 6.5, 50C, 15 min, reaction stopped with Na2CO3
-
-
?
4-methylumbelliferyl alpha-D-mannopyranoside + H2O
4-methylumbelliferol + alpha-D-mannopyranose
show the reaction diagram
Q99YP5
-
-
-
?
4-methylumbelliferyl-alpha-D-mannopyranoside
?
show the reaction diagram
O00754
-
-
-
?
4-methylumbelliferyl-alpha-D-mannopyranoside + H2O
4-methylumbelliferone + alpha-D-mannopyranose
show the reaction diagram
O09159
-
-
?
4-methylumbelliferyl-alpha-D-mannopyranoside + H2O
4-methylumbelliferone + alpha-D-mannopyranose
show the reaction diagram
-
-
-
?
4-methylumbelliferyl-alpha-D-mannopyranoside + H2O
4-methylumbelliferone + alpha-D-mannopyranose
show the reaction diagram
-
-
-
?
4-methylumbelliferyl-alpha-D-mannopyranoside + H2O
4-methylumbelliferone + alpha-D-mannopyranose
show the reaction diagram
-
-
-
?
4-methylumbelliferyl-alpha-D-mannopyranoside + H2O
4-methylumbelliferone + alpha-D-mannopyranose
show the reaction diagram
-
-
-
?
4-methylumbelliferyl-alpha-D-mannopyranoside + H2O
4-methylumbelliferone + alpha-D-mannopyranose
show the reaction diagram
-
-
-
?
4-methylumbelliferyl-alpha-D-mannopyranoside + H2O
4-methylumbelliferone + alpha-D-mannopyranose
show the reaction diagram
-
-
-
?
4-methylumbelliferyl-alpha-D-mannopyranoside + H2O
4-methylumbelliferone + alpha-D-mannopyranose
show the reaction diagram
-
-
-
?
4-methylumbelliferyl-alpha-D-mannopyranoside + H2O
4-methylumbelliferone + alpha-D-mannopyranose
show the reaction diagram
-
-
-
?
4-methylumbelliferyl-alpha-D-mannopyranoside + H2O
4-methylumbelliferone + alpha-D-mannopyranose
show the reaction diagram
-
-
-
?
4-methylumbelliferyl-alpha-D-mannopyranoside + H2O
4-methylumbelliferone + alpha-D-mannopyranose
show the reaction diagram
-
-
-
-
?
4-methylumbelliferyl-alpha-D-mannopyranoside + H2O
4-methylumbelliferone + alpha-D-mannopyranose
show the reaction diagram
-
-
-
?
4-methylumbelliferyl-alpha-D-mannopyranoside + H2O
4-methylumbelliferone + alpha-D-mannopyranose
show the reaction diagram
-
-
-
?
4-methylumbelliferyl-alpha-D-mannopyranoside + H2O
4-methylumbelliferone + alpha-D-mannopyranose
show the reaction diagram
-
-
-
?
4-methylumbelliferyl-alpha-D-mannopyranoside + H2O
4-methylumbelliferone + alpha-D-mannopyranose
show the reaction diagram
-
-
-
?
4-methylumbelliferyl-alpha-D-mannopyranoside + H2O
4-methylumbelliferone + D-mannose
show the reaction diagram
-
-
-
-
?
4-nitrophenyl alpha-D-mannopyranoside + H2O
4-nitrophenol + alpha-D-mannopyranose
show the reaction diagram
Q99YP5
-
-
-
?
4-nitrophenyl alpha-D-mannopyranoside + H2O
4-nitrophenol + D-mannose
show the reaction diagram
-
-
-
-
?
4-nitrophenyl alpha-D-mannopyranoside + H2O
4-nitrophenol + D-mannose
show the reaction diagram
-
-
-
-
?
4-nitrophenyl alpha-D-mannoside + H2O
4-nitrophenol + alpha-D-mannose
show the reaction diagram
-
-
-
-
?
4-nitrophenyl alpha-D-mannoside + H2O
4-nitrophenol + alpha-D-mannose
show the reaction diagram
Q97UK5, -
no hydrolysis observed on 4-nitrophenyl alpha-D-glucoside, 4-nitrophenyl alpha-D-galactoside, 4-nitrophenyl alpha-D-xyloside, 4-nitrophenyl alpha-L-arabinoside, 4-nitrophenyl alpha-L-rhamnoside, 4-nitrophenyl alpha-L-fucoside, and 4-nitrophenyl beta-L-fucoside
-
-
?
4-nitrophenyl alpha-D-mannoside + H2O
4-nitrophenol + alpha-D-mannose
show the reaction diagram
Q97UK5
no hydrolysis observed on 4-nitrophenyl alpha-D-glucoside, 4-nitrophenyl alpha-D-galactoside, 4-nitrophenyl alpha-D-xyloside, 4-nitrophenyl alpha-L-arabinoside, 4-nitrophenyl alpha-L-rhamnoside, 4-nitrophenyl alpha-L-fucoside, and 4-nitrophenyl beta-L-fucoside
-
-
?
4-nitrophenyl alpha-D-mannoside + H2O
4-nitrophenol + alpha-D-mannose
show the reaction diagram
-
-
-
-
?
4-nitrophenyl-alpha-D-mannopyranoside + H2O
4-nitrophenol + alpha-D-mannopyranose
show the reaction diagram
-
-
-
-
?
4-nitrophenyl-alpha-D-mannopyranoside + H2O
4-nitrophenol + alpha-D-mannopyranose
show the reaction diagram
-
able to protect enzyme from quenching of fluorescence
-
-
?
4-nitrophenyl-alpha-D-mannopyranoside + H2O
4-nitrophenol + alpha-D-mannopyranose
show the reaction diagram
-
activity measured in whole fly homogenates, substrate concentration of 60 mM in citrate buffer, female oasis flies have 90% less alpha-mannosidase than females from the arid desert, flies of arid regions tend to produce more alpha-mannosidase activity than those originating in sugar-rich environments
-
-
?
4-nitrophenyl-alpha-D-mannopyranoside + H2O
4-nitrophenol + D-mannose
show the reaction diagram
-
-
-
-
?
4-nitrophenyl-alpha-D-mannopyranoside + H2O
4-nitrophenyl + alpha-D-mannose
show the reaction diagram
-
-
-
-
?
4-nitrophenyl-alpha-D-mannoside + H2O
4-nitrophenol + alpha-D-mannose
show the reaction diagram
-
-
-
-
-
4-nitrophenyl-alpha-D-mannoside + H2O
4-nitrophenol + alpha-D-mannose
show the reaction diagram
Q68EM8
pNP-alpha-Man, used for enzyme activity test
-
-
?
4-O-alpha-D-mannopyranosyl-D-mannopyranose + H2O
2 alpha-D-mannopyranose
show the reaction diagram
-
specific cleavage of alpha-1,4- or alpha-1,6-linkages
-
?
5-fluoro-beta-L-gulosyl fluoride + H2O
?
show the reaction diagram
-
acts as a slow substrate for the D341 mutant enzyme, with deglycosylation as the rate-limiting step. Inactivation is only observed when assayed at low temperatures such that deglycosylation is slow relative to the assay time
-
-
?
6-bromo-2-naphthyl-alpha-D-mannopyranoside + H2O
6-bromo-2-naphthol + alpha-D-mannopyranose
show the reaction diagram
-
-
-
?
6-O-alpha-D-mannopyranosyl-D-mannopyranose + H2O
alpha-D-mannopyranose
show the reaction diagram
-
very low activity
-
?
6-O-alpha-D-mannopyranosyl-D-mannopyranose + H2O
alpha-D-mannopyranose
show the reaction diagram
-
specific cleavage of alpha-1,4- or alpha-1,6-linkages
-
?
alpha-(1-2)-mannobiose + H2O
alpha-D-mannopyranose
show the reaction diagram
-
-
-
?
alpha-(1-2)-mannobiose + H2O
alpha-D-mannopyranose + D-mannopyranose
show the reaction diagram
-
-
-
?
alpha-(1-3)-mannobiose + H2O
alpha-D-mannopyranose
show the reaction diagram
-
highest activity and affinity
-
?
alpha-(1-3)-mannobiose + H2O
alpha-D-mannopyranose + D-mannopyranose
show the reaction diagram
-
highest activity and affinity
-
?
alpha-(1-6)-mannobiose
alpha-D-mannopyranose + D-mannopyranose
show the reaction diagram
-
low activity
-
?
alpha-(1-6)-mannobiose + H2O
alpha-D-mannopyranose
show the reaction diagram
-
low activity
-
?
alpha-conglutin + H2O
alpha-D-mannopyranose + ?
show the reaction diagram
-
lupin seed storage glycoprotein, not active to beta- or gamma-conglutin
-
?
alpha-D-Man-(1-2)-alpha-D-Man-(1-2)-alpha-D-Man-(1-3)-[alpha-D-Man-(1-2)-alpha-D-Man-(1-3)-[alpha-D-Man-(1-2)-alpha-D-Man-(1-6)]-alpha-D-Man-(1-6)]-beta-D-Man-(1-4)-beta-D-GlcNAc + 6 H2O
6 alpha-D-mannopyranose + alpha-D-Man-(1-6)-[alpha-D-Man-(1-3)]-beta-D-Man-(1-4)-beta-D-GlcNAc
show the reaction diagram
-
-
-
?
alpha-D-Man-(1-2)-alpha-D-Man-(1-2)-alpha-D-Man-(1-3)-[alpha-D-Man-(1-2)-alpha-D-Man-(1-3)-[alpha-D-Man-(1-2)-alpha-D-Man-(1-6)]-alpha-D-Man-(1-6)]-beta-D-Man-(1-4)-beta-D-GlcNAc + 6 H2O
6 alpha-D-mannopyranose + alpha-D-Man-(1-6)-[alpha-D-Man-(1-3)]-beta-D-Man-(1-4)-beta-D-GlcNAc
show the reaction diagram
-
-
end products
?
alpha-D-Man-(1-2)-alpha-D-Man-(1-2)-alpha-D-Man-(1-3)-[alpha-D-Man-(1-6)-[alpha-D-Man-(1-2)-alpha-D-Man-(1-3)]-alpha-D-Man-(1-6)]-beta-D-Man-(1-4)-beta-D-GlcNAc + H2O
alpha-D-Man-(1-6)-[alpha-D-Man-(1-3)]-beta-D-Man-(1-4)-beta-D-GlcNAc + alpha-D-Man-(1-3)-[alpha-D-Man-(1-6)]-alpha-D-Man-(1-6)-beta-D-Man
show the reaction diagram
-
cleaves asparagine-linked high mannose oligosaccharides to form the core Man3GlcNAc2
-
?
alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-D-GlcNAc + H2O
alpha-D-mannose + ?
show the reaction diagram
Q97UK5, -
-
-
-
?
alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-D-GlcNAc + H2O
alpha-D-mannose + ?
show the reaction diagram
Q97UK5
-
-
-
?
alpha-D-Man-(1->2)-D-Man + H2O
2 alpha-D-mannose
show the reaction diagram
Q97UK5, -
-
-
-
?
alpha-D-Man-(1->2)-D-Man + H2O
2 alpha-D-mannose
show the reaction diagram
-
-
-
-
?
alpha-D-Man-(1->2)-D-Man + H2O
2 alpha-D-mannose
show the reaction diagram
Q97UK5
-
-
-
?
alpha-D-Man-(1->2)-D-Man + H2O
2 alpha-D-mannose
show the reaction diagram
-
-
-
-
?
alpha-D-Man-(1->3)-D-Man + H2O
2 alpha-D-mannose
show the reaction diagram
Q97UK5, -
-
-
-
?
alpha-D-Man-(1->3)-D-Man + H2O
2 alpha-D-mannose
show the reaction diagram
-
-
-
-
?
alpha-D-Man-(1->3)-D-Man + H2O
2 alpha-D-mannose
show the reaction diagram
Q97UK5
-
-
-
?
alpha-D-Man-(1->3)-D-Man + H2O
2 alpha-D-mannose
show the reaction diagram
-
-
-
-
?
alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-D-GlcNAc + H2O
alpha-D-mannose + ?
show the reaction diagram
Q97UK5, -
-
-
-
?
alpha-D-Man-(1->4)-D-Man + H2O
2 alpha-D-mannose
show the reaction diagram
-
-
-
-
?
alpha-D-Man-(1->6)-D-Man + H2O
2 alpha-D-mannose
show the reaction diagram
Q97UK5, -
-
-
-
?
alpha-D-Man-(1->6)-D-Man + H2O
2 alpha-D-mannose
show the reaction diagram
-
-
-
-
?
alpha-D-mannopyranoside + H2O
alpha-D-mannopyranose + ?
show the reaction diagram
O09159
-
-
?
alpha-D-mannosidosis fibroblasts + H2O
Manbeta(1-4)GlcNAc + ?
show the reaction diagram
-, O09159
-
-
?
alpha-D-mannosidosis fibroblasts + H2O
Man7-2GlcNAc + ?
show the reaction diagram
-
-
-
?
alpha3,alpha6-D-mannopentaose + H2O
alpha-D-mannose
show the reaction diagram
-, Q6L2X5
-
-
-
?
beta-glucuronidase peptide + H2O
alpha-D-mannopyranose + ?
show the reaction diagram
-
-
-
?
beta-glucuronidase peptide + H2O
alpha-D-mannopyranose + ?
show the reaction diagram
-
-
-
?
GDP-mannosylpyranose + H2O
alpha-D-mannosylpyranose + GDP
show the reaction diagram
-
-
-
?
GDP-mannosylpyranose + H2O
alpha-D-mannosylpyranose + GDP
show the reaction diagram
-
-
-
?
GDP-mannosylpyranose + H2O
alpha-D-mannopyranose + GDP
show the reaction diagram
-
-
-
?
GDP-mannosylpyranose + H2O
alpha-D-mannopyranose + GDP
show the reaction diagram
-
-
-
?
Glc3Man9GlcNAc2 + H2O
alpha-D-mannopyranose + ?
show the reaction diagram
-
from oligosaccharide-lipid
-
?
GlcNAcMan5GlcNAc + H2O
alpha-D-mannopyranose + ?
show the reaction diagram
-
-
-
?
GlcNAcMan5GlcNAc + H2O
alpha-D-mannopyranose + ?
show the reaction diagram
-
low activity
-
?
glycopeptide + H2O
alpha-D-mannopyranose + ?
show the reaction diagram
-
-
-
?
glycopeptide + H2O
alpha-D-mannopyranose + ?
show the reaction diagram
-
from ovalbumin
-
?
glycopeptide + H2O
alpha-D-mannopyranose + ?
show the reaction diagram
-
from ovalbumin
-
?
glycopeptide + H2O
alpha-D-mannopyranose + ?
show the reaction diagram
-
from ovalbumin
-
?
glycopeptide + H2O
alpha-D-mannopyranose + ?
show the reaction diagram
-
from ovalbumin
-
?
glycopeptide + H2O
alpha-D-mannopyranose + ?
show the reaction diagram
-
from ovalbumin
-
?
glycopeptide + H2O
alpha-D-mannopyranose + ?
show the reaction diagram
-
from ovalbumin
-
?
glycopeptide + H2O
alpha-D-mannopyranose + ?
show the reaction diagram
-
from ovalbumin
-
?
glycopeptide + H2O
alpha-D-mannopyranose + ?
show the reaction diagram
-
from ovalbumin
-
?
glycopeptide + H2O
alpha-D-mannopyranose + ?
show the reaction diagram
-
from ovalbumin
-
?
glycopeptide + H2O
alpha-D-mannopyranose + ?
show the reaction diagram
-
faster hydrolysis than for glycoprotein
-
?
glycopeptide + H2O
alpha-D-mannopyranose + ?
show the reaction diagram
-
contains only alpha-1,2-linked mannose residues, highly specific on alpha-1,2-linked mannooligosaccharides
-
?
glycopeptide + H2O
alpha-D-mannopyranose + ?
show the reaction diagram
-
stem bromelain
-
?
glycoprotein + H2O
alpha-D-mannopyranose + ?
show the reaction diagram
-
-
-
?
glycoprotein + H2O
alpha-D-mannopyranose + ?
show the reaction diagram
-
-
-
?
glycoprotein + H2O
alpha-D-mannopyranose + ?
show the reaction diagram
-
ovomucoid, orosomucoid, ovalbumin
-
?
high mannose N-glycan + H2O
?
show the reaction diagram
Q99YP5
-
-
-
?
Man-alpha(1-3)Man + H2O
alpha-D-mannose
show the reaction diagram
-
pH 6.5, 50C, 20 min
-
-
?
Man-alpha(1-6)Man + H2O
alpha-D-mannose
show the reaction diagram
-
pH 6.5, 50C, 20 min
-
-
?
Man-alpha-(1-2)-Man-alpha-(1-6)-[Man-alpha-(1-2)-Man-alpha-(1-3)]-Manalpha-(1-6)-[Man-alpha-(1-2)-Man-alpha-(1-2)-Man-alpha-(1-3)]-Man-beta(1-4)GlcNAc + H2O
?
show the reaction diagram
-
-
-
-
?
Man-alpha-(1-2)-Man-alpha-(1-6)-[Man-alpha-(1-2)-Man-alpha-(1-3)]-Manalpha-(1-6)-[Man-alpha-(1-2)-Man-alpha-(1-2)-Man-alpha-(1-3)]-Man-beta(1-4)GlcNAc + H2O
Man-alpha-(1-6)-[Man-alpha-(1-2)-Man-alpha-(1-2)-Man-alpha(1-3)]-Man-beta-(1-4)-GlcNAc + alpha-mannose
show the reaction diagram
-
-
end product in presence of Co2+. Before treatment with Co(II) the enzyme is able to cleave a single Manalpha1-2 residue from the substrate to give Man-alpha(1-6)-[Man-alpha-(1-2)-Man-alpha-(1-3)]Man-alpha-(1-6)-[Man-alpha-(1-2)-Man-alpha-(1-2)-Man-alpha-(1-3)]Man-beta-(1-4)-GlcNAc as the end product
-
?
Man-glycopeptide + H2O
alpha-D-mannopyranose + ?
show the reaction diagram
-
low activity
-
?
Man3GlcNAc2 + H2O
Man2GlcNAc2 + alpha-D-mannopyranose
show the reaction diagram
-
Man-1,6-linkage only hydrolysed after its Man-1,3-residue is removed
-
?
Man5-9GlcNAc + H2O
alpha-D-mannopyranose + ?
show the reaction diagram
-
low activity for Man5GlcNAc
-
?
Man5GlcNAc + 2 H2O
Man3GlcNAc + 2 alpha-D-mannopyranose
show the reaction diagram
-
-
-
?
Man5GlcNAc2 + H2O
Man4GlcNAc2 + alpha-D-mannopyranose
show the reaction diagram
-
cleaves Man-alpha-(1-3)-linkage 10times faster than the Man-1,6 and the Man-1,2-linkages
mixture of three isomeric oligosaccharides
?
Man5GlcNAc2 + H2O
Man3GlcNAc2 + alpha-D-mannopyranose
show the reaction diagram
-
-
-
?
Man5GlcNAc2 + H2O
Man-GlcNAc2 + mannose
show the reaction diagram
-
-
-
-
?
Man5GlcNAc2 + H2O
Man3GlcNAc2 + mannose
show the reaction diagram
-
-
-
-
?
Man6 + H2O
alpha-D-mannose + ?
show the reaction diagram
-
derived from ovalbumin, alpha-1,2: 1,3: 1,6-linkages, more than 10fold higher specific activity for isoform EII than for EI
-
?
Man6-glycopeptide + H2O
alpha-D-mannopyranose + ?
show the reaction diagram
-
-
-
?
Man6GlcNAc + H2O
alpha-D-mannopyranose + ?
show the reaction diagram
-
-
-
?
Man6GlcNAc + H2O
alpha-D-mannopyranose + ?
show the reaction diagram
-
ordered hydrolysis of alpha(1-2)-residues followed by hydrolysis of alpha(1-3)- and alpha(1-6)-linked residues
-
?
Man6GlcNAc2 + H2O
Man-GlcNAc2 + mannose
show the reaction diagram
-
-
-
-
?
Man6GlcNAc2 + H2O
Man5GlcNAc2 + mannose
show the reaction diagram
-
slow reaction of the Golgi alpha-mannosidase in vitro
-
-
?
Man7GlcNAc + 2 H2O
Man5GlcNAc + 2 alpha-D-mannopyranose
show the reaction diagram
-
-
-
?
Man7GlcNAc2 + H2O
alpha-D-mannopyranose + ?
show the reaction diagram
-
from oligosaccharide-lipid, very low activity
-
?
Man7GlcNAc2 + H2O
Man-GlcNAc2 + mannose
show the reaction diagram
-
-
-
-
?
Man8GlcNAc + 3 H2O
Man5GlcNAc + 3 alpha-D-mannopyranose
show the reaction diagram
-
-
-
?
Man8GlcNAc2 + 3 H2O
Man5GlcNAc2 + 3 alpha-D-mannopyranose
show the reaction diagram
-
-
-
?
Man8GlcNAc2 + 3 H2O
Man5GlcNAc2 + 3 D-mannose
show the reaction diagram
-
Golgi alpha-mannosidase in vivo, slow reaction of the endoplasmic reticulum alpha-mannosidase in vitro
-
-
?
Man8GlcNAc2 + H2O
Man-GlcNAc2 + mannose
show the reaction diagram
-
-
-
-
?
Man9-5GlcNAc + 4 H2O
Man5-3GlcNAc + 4 alpha-D-mannopyranose
show the reaction diagram
-
different product composition for alpha-mannosidases IA, IB and II
-
?
Man9-glycopeptide + H2O
alpha-D-mannopyranose + ?
show the reaction diagram
-
-
-
?
Man9GlcNAc + 4 H2O
Man5GlcNAc + 4 alpha-D-mannopyranose
show the reaction diagram
-
-
-
?
Man9GlcNAc + 4 H2O
Man5GlcNAc + 4 alpha-D-mannopyranose
show the reaction diagram
-
-
end product for Tris-eluted isoform, representing the Man5-oligosaccharide chain of the dolichol pathway formed in the cytosolic compartment during biosynthesis of N-glycosylprotein glycans
?
Man9GlcNAc + 4 H2O
Man5GlcNAc + 4 alpha-D-mannopyranose
show the reaction diagram
-
hydrolyses alpha-1,2- and alpha-1,3-linkages
after 24 h incubation, specifically removes alpha-1,2-linked mannoses
?
Man9GlcNAc + H2O
Manalpha(1-6)[Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)]Manbeta(1-4)GlcNAc + alpha-D-mannopyranose
show the reaction diagram
-
Co2+ activated alpha-mannosidase
end products
?
Man9GlcNAc + H2O
Man8GlcNAc + alpha-D-mannopyranose
show the reaction diagram
-
-
-
-
-
Man9GlcNAc + H2O
Man8GlcNAc + alpha-D-mannopyranose
show the reaction diagram
-
highly specific soluble catalytic domain of a larger membrane-bound form, does not act on synthetic substrates
releases only one specific mannopyranose residue
?
Man9GlcNAc2 + H2O
Man5-8GlcNAc2 + alpha-D-mannopyranose
show the reaction diagram
-
-
major product: Man5GlcNAc2, involved in Asn-linked oligosaccharide maturation
?
Man9GlcNAc2 + H2O
Man5-8GlcNAc2 + alpha-D-mannopyranose
show the reaction diagram
-
from thyroglobulin or oligosaccharide-lipid, trimming the substrate to Man8GlcNAc2, the substrate for oligosaccharide elongation
only alpha-(1-2)-linked terminal mannoses on the alpha-3-branch of the Man9GlcNAc precursor dispensable
?
Man9GlcNAc2 + H2O
Man5-8GlcNAc2 + alpha-D-mannopyranose
show the reaction diagram
-
involved in N-glycan processing to form oligomannosidic glycans during glycoprotein biosynthesis, cleaves three of the four alpha-1,2-mannosidic linkages
major product: Man6GlcNAc2
?
Man9GlcNAc2 + H2O
Man-GlcNAc2 + mannose
show the reaction diagram
-
-
-
-
?
Man9GlcNAc2 + H2O
Man8GlcNAc2 + mannose
show the reaction diagram
-
-
-
-
?
Man9GlcNAc2 + H2O
Man8GlcNAc2 + mannose
show the reaction diagram
-
-
Man8GlcNAc B isomer + mannose is produced after 12 h at 37C. Prolonged incubation results in accumulation after 24 h of Man7GlcNAc2 and probably Man6GlcNAc2
-
?
Man9GlcNAc2 + H2O
Man8GlcNAc2 + mannose
show the reaction diagram
-
endoplasmic reticulum alpha-mannosidase in vivo, fast reaction of the endoplasmic reticulum alpha-mannosidase in vitro
-
-
?
Man9GlcNAc2 + H2O
Man6GlcNAc2 + mannose
show the reaction diagram
-
fast reaction of the Golgi alpha-mannosidase in vitro
-
-
?
Manalpha(1-2)Man + H2O
D-mannose
show the reaction diagram
-
-
-
-
-
Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAc + H2O
alpha-D-mannopyranose + ?
show the reaction diagram
-
-
-
?
Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)[Man(1-6)]ManbetaGlcNac-betaGlcNAc + H2O
alpha-D-mannopyranose + ?
show the reaction diagram
-
-
-
?
Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)[Manbeta(1-6)]ManbetaGlcNAc-beta-GlcNAc + H2O
alpha-D-mannopyranose + ?
show the reaction diagram
-
-
-
?
Manalpha(1-2)Manalpha(1-2)Manalpha(1-6)Manalpha(1-4)-anhydromannitol + H2O
Manalpha(1-2)Manalpha(1-6)Manalpha(1-4)-anhydromannitol + Manalpha(1-6)Manalpha(1-4)-anhydromannitol + Manalpha(1-4)anhydromannitol + anhydromannitol + alpha-D-mannose
show the reaction diagram
-
-
equal amounts, but only traces of Manalpha(1-4)-anhydromannitol
?
Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAc + H2O
alpha-D-mannopyranose + ?
show the reaction diagram
-
-
-
?
Manalpha(1-2)Manalpha(1-3)[Man(1-6)]ManbetaGlcNAc-betaGlcNAc + H2O
alpha-D-mannopyranose + ?
show the reaction diagram
-
-
-
?
Manalpha(1-3)GlcNAc + H2O
alpha-D-mannopyranose + 2-acetylamino-2-deoxy-D-glucose
show the reaction diagram
-
-
-
?
Manalpha(1-3)GlcNAc + H2O
alpha-D-mannopyranose + N-acetyl-D-glucosamine
show the reaction diagram
-
-
-
?
Manalpha(1-3)Man + H2O
D-mannose
show the reaction diagram
-
-
-
-
-
Manalpha(1-3)[Man(1-6)]ManbetaGlcNAc-betaGlcNAc + H2O
alpha-D-mannopyranose + ?
show the reaction diagram
-
-
-
?
Manalpha(1-4)Manbeta(1-4)Man + H2O
alpha-D-mannopyranose + Manbeta(1-4)Man
show the reaction diagram
-
-
-
?
Manalpha(1-6)GlcNAc + H2O
alpha-mannopyranose + 2-acetylamino-2-deoxy-D-glucose
show the reaction diagram
-
-
-
?
Manalpha(1-6)GlcNAc + H2O
alpha-mannopyranose + N-acetyl-D-glucosamine
show the reaction diagram
-
-
-
?
Manalpha(1-6)Man + H2O
D-mannose
show the reaction diagram
-
-
-
-
-
Manalpha(1-6)[Manalpha(1-3)]Manalpha(1-6)[Manalpha(1-)]Manbeta(1-4)GlcNAc + H2O
alpha-D-mannopyranose + ?
show the reaction diagram
-
4 times faster hydrolysis than Manalpha(1-6)[Manalpha(1-3)]Manalpha(1-6)[Manalpha(1-3)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc
-
?
Manalpha(1-6)[Manalpha(1-3)]Manalpha(1-6)[Manalpha(1-3)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + H2O
alpha-D-mannopyranose + ?
show the reaction diagram
-
-
-
?
Manalpha1-2Man + H2O
alpha-mannose
show the reaction diagram
-
-
-
-
?
Manalpha1-3Man + H2O
alpha-mannose
show the reaction diagram
-
-
-
-
?
Manalpha1-6Man + H2O
alpha-mannose
show the reaction diagram
-
-
-
-
?
mannan + H2O
alpha-D-mannose + ?
show the reaction diagram
-
very low activity
-
?
mannan + H2O
alpha-D-mannose + ?
show the reaction diagram
-
very low activity
-
?
mannan + H2O
alpha-D-mannose + ?
show the reaction diagram
-
yeast alpha-mannan, main product: alpha-D-mannose, hydrolysis of linear and branched mannans containing terminal alpha-1,2- and alpha-1,3-linked mannopyranosyl residues
-
?
mannan + H2O
alpha-D-mannose + ?
show the reaction diagram
-
from yeast
-
?
mannan + H2O
alpha-D-mannose + ?
show the reaction diagram
-
from yeast
-
?
mannan + H2O
alpha-D-mannose + ?
show the reaction diagram
-
from yeast
-
?
mannan + H2O
alpha-D-mannose + ?
show the reaction diagram
-
from yeast
only mannose librated
?
mannan + H2O
alpha-D-mannose + ?
show the reaction diagram
-
from baker's and sake yeast
-
?
mannan + H2O
alpha-D-mannose + ?
show the reaction diagram
-
from baker's and sake yeast
-
?
mannan + H2O
alpha-D-mannose + ?
show the reaction diagram
-
specific for alpha-1,2-linked mannopyranosyl residues
-
?
mannan + H2O
alpha-D-mannose + ?
show the reaction diagram
-
derived from wild type or mutant strains of Saccharomyces cerevisiae, different specific activities for isoforms EI and EII, depending on the type of alpha-D-linkages of mutant substrates, preference for cleavage of alpha-1,6- and alpha-1,3-linkages
-
?
mannobiose + H2O
alpha-D-mannopyranose
show the reaction diagram
-
-
-
?
mannobiose + H2O
alpha-D-mannopyranose
show the reaction diagram
-
-
-
?
mannobiose + H2O
alpha-D-mannopyranose + D-mannopyranose
show the reaction diagram
-
-
-
?
mannobiose + H2O
alpha-D-mannopyranose + D-mannopyranose
show the reaction diagram
-
-
-
?
mannopyranosyl-oligosaccharides + H2O
alpha-D-mannopyranose + ?
show the reaction diagram
-
from yeast mannan, hydrolysis of alpha-1,2- and alpha-1,3-linkages
-
?
mannopyranosyl-oligosaccharides + H2O
alpha-D-mannopyranose + ?
show the reaction diagram
-
from yeast mannan, hydrolysis of alpha-1,2- and alpha-1,3-linkages
-
?
mannopyranosyl-oligosaccharides + H2O
alpha-D-mannopyranose + ?
show the reaction diagram
-
from yeast mannan, a tetrasaccharide terminating in a mannopyranosyl residue linked to C-3 of its neighbour is not hydrolysed
-
?
mannopyranosyl-oligosaccharides + H2O
alpha-D-mannopyranose + ?
show the reaction diagram
-
reverse action on alpha-D-mannopyranose, 85%, w/w, yields 0.93 M disaccharide with 4 different isomers, 0.61 M trisaccharide, 0.25 M tetrasaccharide and higher oligosaccharides, retention of anomeric configuration
-
r
mannosyl rhamnose + H2O
alpha-D-mannopyranose + rhamnose
show the reaction diagram
-
part of the repeating oligosaccharide unit of the O-antigenic lipopolysaccharide in Salmonella typhimurium
-
?
mannosyl(5)-N-acetyl-glucosamine-pyridylamino + H2O
mannosyl(4)-N-acetyl-glucosamine-pyridylamino + mannosyl(3)-N-acetyl-glucosamine-pyridylamino
show the reaction diagram
Q68EM8
-
occurrence of mannosyl(4)-N-acetyl-glucosamine-pyridylamino (32%) and mannosyl(3)-N-acetyl-glucosamine-pyridylamino (8.1%) are observed only in the presence of Co2+
-
?
mannosyl(9)-N-acetyl-glucosamine + H2O
mannosyl(5)-N-acetyl-glucosamine + alpha-D-mannose
show the reaction diagram
Q68EM8
in presence of Co2+
-
-
?
mannosyl(9)-N-acetyl-glucosamine + H2O
mannosyl(8)-N-acetyl-glucosamine + alpha-D-mannose
show the reaction diagram
Q68EM8
absence of Co2+
-
-
?
mannotetraose + H2O
alpha-D-mannopyranose + mannotriose
show the reaction diagram
-
-
-
?
mannotetraose + H2O
alpha-D-mannopyranose + mannotriose
show the reaction diagram
-
-
-
?
mannotriose + H2O
alpha-D-mannopyranose + mannobiose
show the reaction diagram
-
-
-
?
methyl-2,4,6-tri-O-methyl-D-mannopyranoside + H2O
2,4,6-tri-O-methyl-D-mannopyranose + methanol
show the reaction diagram
-
-
-
?
methyl-2-O-alpha-D-mannopyranosyl-D-mannopyranoside + H2O
alpha-D-mannopyranose + ?
show the reaction diagram
-
very low activity
-
?
methyl-4-O-alpha-D-mannopyranosyl-D-mannopyranoside + H2O
alpha-D-mannopyranose + ?
show the reaction diagram
-
-
-
?
methyl-alpha-D-mannnopyranose + H2O
alpha-D-mannopyranose + methanol
show the reaction diagram
-
-
-
?
methyl-alpha-D-mannopyranoside + H2O
alpha-D-mannopyranose + methanol
show the reaction diagram
-
-
-
?
methyl-alpha-D-mannopyranoside + H2O
alpha-D-mannopyranose + methanol
show the reaction diagram
-
-
-
?
methyl-alpha-D-mannopyranoside + H2O
alpha-D-mannopyranose + methanol
show the reaction diagram
-
-
-
?
methyl-alpha-D-mannopyranoside + H2O
alpha-D-mannopyranose + methanol
show the reaction diagram
-
-
-
?
methyl-alpha-D-mannopyranoside + H2O
alpha-D-mannopyranose + methanol
show the reaction diagram
-
-
-
?
p-nitrophenyl alpha-D-rhamnopyranoside + ethyl 1-thio-alpha-D-rhamnopyranoside
p-nitrophenol + ethyl alpha-D-rhamnopyranosyl-(1-2)-1-thio-alpha-D-rhamnopyranoside
show the reaction diagram
-
-
-
-
?
p-nitrophenyl alpha-mannoside + H2O
p-nitrophenol + alpha-mannose
show the reaction diagram
-
-
-
-
?
p-nitrophenyl-alpha-D-mannopyranoside + H2O
p-nitrophenol + alpha-D-mannopyranose
show the reaction diagram
-
-
-
?
p-nitrophenyl-alpha-D-mannopyranoside + H2O
p-nitrophenol + alpha-D-mannopyranose
show the reaction diagram
-
-
-
?
p-nitrophenyl-alpha-D-mannopyranoside + H2O
p-nitrophenol + alpha-D-mannopyranose
show the reaction diagram
-
-
-
?
p-nitrophenyl-alpha-D-mannopyranoside + H2O
p-nitrophenol + alpha-D-mannopyranose
show the reaction diagram
-, O09159
-
-
?
p-nitrophenyl-alpha-D-mannopyranoside + H2O
p-nitrophenol + alpha-D-mannopyranose
show the reaction diagram
-
-
-
?
p-nitrophenyl-alpha-D-mannopyranoside + H2O
p-nitrophenol + alpha-D-mannopyranose
show the reaction diagram
-
-
-
?
p-nitrophenyl-alpha-D-mannopyranoside + H2O
p-nitrophenol + alpha-D-mannopyranose
show the reaction diagram
-
-
-
?
p-nitrophenyl-alpha-D-mannopyranoside + H2O
p-nitrophenol + alpha-D-mannopyranose
show the reaction diagram
-
-
-
?
p-nitrophenyl-alpha-D-mannopyranoside + H2O
p-nitrophenol + alpha-D-mannopyranose
show the reaction diagram
-
-
-
?
p-nitrophenyl-alpha-D-mannopyranoside + H2O
p-nitrophenol + alpha-D-mannopyranose
show the reaction diagram
-
-
-
?
p-nitrophenyl-alpha-D-mannopyranoside + H2O
p-nitrophenol + alpha-D-mannopyranose
show the reaction diagram
-
-
-
?
p-nitrophenyl-alpha-D-mannopyranoside + H2O
p-nitrophenol + alpha-D-mannopyranose
show the reaction diagram
-
-
-
?
p-nitrophenyl-alpha-D-mannopyranoside + H2O
p-nitrophenol + alpha-D-mannopyranose
show the reaction diagram
-
-
-
?
p-nitrophenyl-alpha-D-mannopyranoside + H2O
p-nitrophenol + alpha-D-mannopyranose
show the reaction diagram
-
-
-
?
p-nitrophenyl-alpha-D-mannopyranoside + H2O
p-nitrophenol + alpha-D-mannopyranose
show the reaction diagram
-
-
-
?
p-nitrophenyl-alpha-D-mannopyranoside + H2O
p-nitrophenol + alpha-D-mannopyranose
show the reaction diagram
-
-
-
?
p-nitrophenyl-alpha-D-mannopyranoside + H2O
p-nitrophenol + alpha-D-mannopyranose
show the reaction diagram
-
-
-
?
p-nitrophenyl-alpha-D-mannopyranoside + H2O
p-nitrophenol + alpha-D-mannopyranose
show the reaction diagram
-
-
-
?
p-nitrophenyl-alpha-D-mannopyranoside + H2O
p-nitrophenol + alpha-D-mannopyranose
show the reaction diagram
-
-
-
?
p-nitrophenyl-alpha-D-mannopyranoside + H2O
p-nitrophenol + alpha-D-mannopyranose
show the reaction diagram
-
-
-
?
p-nitrophenyl-alpha-D-mannopyranoside + H2O
p-nitrophenol + alpha-D-mannopyranose
show the reaction diagram
-
-
-
?
p-nitrophenyl-alpha-D-mannopyranoside + H2O
p-nitrophenol + alpha-D-mannopyranose
show the reaction diagram
-
-
-
?
p-nitrophenyl-alpha-D-mannopyranoside + H2O
p-nitrophenol + alpha-D-mannopyranose
show the reaction diagram
-
-
-
?
p-nitrophenyl-alpha-D-mannopyranoside + H2O
p-nitrophenol + alpha-D-mannopyranose
show the reaction diagram
-
-
-
?
p-nitrophenyl-alpha-D-mannopyranoside + H2O
p-nitrophenol + alpha-D-mannopyranose
show the reaction diagram
-
-
-
?
p-nitrophenyl-alpha-D-mannopyranoside + H2O
p-nitrophenol + alpha-D-mannopyranose
show the reaction diagram
-
-
-
?
p-nitrophenyl-alpha-D-mannopyranoside + H2O
p-nitrophenol + alpha-D-mannopyranose
show the reaction diagram
-
-
-
?
p-nitrophenyl-alpha-D-mannopyranoside + H2O
p-nitrophenol + alpha-D-mannopyranose
show the reaction diagram
-
-
-
?
p-nitrophenyl-alpha-D-mannopyranoside + H2O
p-nitrophenol + alpha-D-mannopyranose
show the reaction diagram
-
-
-
?
p-nitrophenyl-alpha-D-mannopyranoside + H2O
p-nitrophenol + alpha-D-mannopyranose
show the reaction diagram
-
-
-
?
p-nitrophenyl-alpha-D-mannopyranoside + H2O
p-nitrophenol + alpha-D-mannopyranose
show the reaction diagram
-
-
-
?
p-nitrophenyl-alpha-D-mannopyranoside + H2O
p-nitrophenol + alpha-D-mannopyranose
show the reaction diagram
-
-
-
?
p-nitrophenyl-alpha-D-mannopyranoside + H2O
p-nitrophenol + alpha-D-mannopyranose
show the reaction diagram
-
-
-
?
p-nitrophenyl-alpha-D-mannopyranoside + H2O
p-nitrophenol + alpha-D-mannopyranose
show the reaction diagram
-
-
-
?
p-nitrophenyl-alpha-D-mannopyranoside + H2O
p-nitrophenol + alpha-D-mannopyranose
show the reaction diagram
-
-
-
?
p-nitrophenyl-alpha-D-mannopyranoside + H2O
p-nitrophenol + alpha-D-mannopyranose
show the reaction diagram
-
-
-
?
p-nitrophenyl-alpha-D-mannopyranoside + H2O
p-nitrophenol + alpha-D-mannopyranose
show the reaction diagram
-
-
-
?
p-nitrophenyl-alpha-D-mannopyranoside + H2O
p-nitrophenol + alpha-D-mannopyranose
show the reaction diagram
-
-
-
?
p-nitrophenyl-alpha-D-mannopyranoside + H2O
p-nitrophenol + alpha-D-mannopyranose
show the reaction diagram
-
-
-
?
p-nitrophenyl-alpha-D-mannopyranoside + H2O
p-nitrophenol + alpha-D-mannopyranose
show the reaction diagram
-
-
-
?
p-nitrophenyl-alpha-D-mannopyranoside + H2O
p-nitrophenol + alpha-D-mannopyranose
show the reaction diagram
-
-
-
?
p-nitrophenyl-alpha-D-mannopyranoside + H2O
p-nitrophenol + alpha-D-mannopyranose
show the reaction diagram
-
-
-
?
p-nitrophenyl-alpha-D-mannopyranoside + H2O
p-nitrophenol + alpha-D-mannopyranose
show the reaction diagram
-
very poor substrate
-
?
p-nitrophenyl-alpha-D-mannopyranoside + H2O
p-nitrophenol + alpha-D-mannopyranose
show the reaction diagram
-
very low activity
-
?
p-nitrophenyl-alpha-D-mannopyranoside + H2O
p-nitrophenol + alpha-D-mannopyranose
show the reaction diagram
-
high amounts of substrate hydrolysed at pH 3.0, at neutral pH very little substrate cleaved
-
?
p-nitrophenyl-alpha-D-mannopyranoside + H2O
p-nitrophenol + alpha-D-mannopyranose
show the reaction diagram
-
different affinities for two isoforms, unbound fraction and Tris-eluted fraction from cobalt-chelating Sepharose
-
?
p-nitrophenyl-alpha-D-mannopyranoside + H2O
p-nitrophenol + alpha-D-mannopyranose
show the reaction diagram
-
most rapidly hydrolysed
-
?
p-nitrophenyl-alpha-D-mannopyranoside + H2O
p-nitrophenol + alpha-D-mannopyranose
show the reaction diagram
-
responsible for the removal of mannose residues from asparagines-linked high-mannose type oligosaccharides prior to their entry into the Golgi
-
?
p-nitrophenyl-alpha-D-mannopyranoside + H2O
p-nitrophenol + alpha-D-mannopyranose
show the reaction diagram
-
isoforms mannosidase IB and II
-
?
p-nitrophenyl-alpha-D-mannopyranoside + H2O
p-nitrophenol + alpha-D-mannose
show the reaction diagram
-
-
-
-
?
p-nitrophenyl-alpha-D-mannopyranoside + H2O
4-nitrophenol + alpha-D-mannose
show the reaction diagram
-, Q6L2X5
-
-
-
?
p-nitrophenyl-alpha-D-mannoside + H2O
p-nitrophenol + alpha-D-mannose
show the reaction diagram
-
-
-
-
?
phenyl-alpha-D-mannopyranoside + H2O
alpha-D-mannopyranose + phenol
show the reaction diagram
-
-
-
?
pyridylamino-glycopeptide + H2O
alpha-D-mannopyranose + ?
show the reaction diagram
-
from ovalbumin
-
?
pyridylamino-Man5GlcNAc + H2O
pyridylamino-Man4GlcNAc + pyridylamino-Man3-2GlcNAc + alpha-D-mannose
show the reaction diagram
-, O09159
-
lesser degree of pyridylamino-Man3-2GlcNAc, stepwise cleavage to Man2GlcNAc structures
?
pyridylamino-Man5GlcNAc + H2O
pyridylamino-Man2GlcNA + alpha-D-mannopyranose
show the reaction diagram
-
-
-
?
pyridylamino-Man9GlcNAc2 + H2O
pyridylamino-Man8GlcNAc2 + alpha-D-mannopyranose
show the reaction diagram
-
high amounts of substrate hydrolysed at neutral pH, very little cleavage at pH 3.0
hydrolysis products within 20 min
?
pyridylamino-Man9GlcNAc2 + H2O
pyridylamino-Man3-8GlcNAc + Man2GlcNAc + alpha-D-mannopyranose
show the reaction diagram
-
-
-
?
pyridylamino-Man9GlcNAc2 + H2O
pyridylamino-Man3-8GlcNAc + Man2GlcNAc + alpha-D-mannopyranose
show the reaction diagram
-, O09159
stepwise cleavage to Man2GlcNAc structures
-
?
ribonuclease B + H2O
oligosaccharide + alpha-D-mannopyranose + ?
show the reaction diagram
-
-
-
-
?
ribonuclease B + H2O
oligosaccharide + alpha-D-mannopyranose + ?
show the reaction diagram
-
from bovine pancreas
single oligosaccharide component
?
RNase-B-Man(n)-glycoform + H2O
RNase-B-Man(n-1)-glycoform + alpha-D-mannose
show the reaction diagram
Q97UK5, -
-
-
-
?
TAKA-amylase A + H2O
alpha-D-mannopyranose + ?
show the reaction diagram
-
-
-
?
TAKA-amylase A + H2O
alpha-D-mannopyranose + ?
show the reaction diagram
-
-
-
?
TAKA-amylase A + H2O
alpha-D-mannopyranose + ?
show the reaction diagram
-
from Aspergillus oryzae, hydrolysis of a single Man-1,2-linkage
-
?
thyroglobulin + H2O
alpha-D-mannopyranose + ?
show the reaction diagram
-
-
-
?
thyroglobulin peptide A + H2O
alpha-D-mannopyranose + ?
show the reaction diagram
-
-
-
?
thyroglobulin peptide A + H2O
alpha-D-mannopyranose + ?
show the reaction diagram
-
-
-
?
methyl-O-1,4-alpha-D-mannobiose + H2O
alpha-D-mannose
show the reaction diagram
-, Q6L2X5
-
-
-
?
additional information
?
-
-
anomalies of the enzyme system detected in patients with amyotrophic lateral sclerosis could reflect a situation of progressive injury of proteins
-
-
-
additional information
?
-
-
key enzyme in N-glycan processing
-
-
-
additional information
?
-
-
the enzyme is required in the degradation of the asparagine-linked carbohydrates of glycoproteins. Deficiency of this enzyme leads to the lysosomal storage disorder alpha-mannosidosis
-
-
-
additional information
?
-
-
digestion of glycopeptides having high mannose-type sugar chains
-
-
-
additional information
?
-
-
no hydrolysis of GlcNAcMan5GlcNAc2
-
-
-
additional information
?
-
-
no hydrolysis of Man6GlcNAc2-ASn, man5-GlcNAc2-ASn, and alpha1,3- and alpha1-6-linked mannobiosides
-
-
-
additional information
?
-
-
class 1 alpha1,2-mannosidases of glycosylhydrolase family 47 play critical roles in the maturation of Asn-linked glycoproteins in the endoplasmic reticulum and Golgi complex as well as in the recognition and timing of disposal of terminally unfolded proteins by ER-associated degradation, overview
-
-
-
additional information
?
-
-
the enzyme is involved in ordered degradation of glycoproteins, inborn enzyme-deficiency results in lysosomal storage disorder alpha-mannosidosis
-
-
-
additional information
?
-
-
the exo-type cytosolic class II enzyme cleaves off alpha-1,2-, alpha-1,3-, and alpha-1,6-mannose residues
-
-
-
additional information
?
-
-
broad substrate specific exoglycosidase
-
-
-
additional information
?
-
-
enzyme hydrolyzes alpha-mannosidase linkages from both high-mannose type and plant complex type N-glycan, but prefers a truncated plant complex type structure to high-mannose type N-glycans bearing alpha-(1,2)-mannosyl residues, enzyme is active toward both high-mannose type and truncated plant complex type N-glycans. It prefers truncated plant complex type N-glycans
-
-
-
additional information
?
-
Q99YP5
higher eukaryotic GH38 alpha-mannosides play a key role in the modification and diversification of hybrid N-glycans, processes with strong cellular links to cancer and autoimmune disease, SpGH38 is an alpha-mannosidase with specificity for alpha-1,3 mannosidic linkages, active site structure, overview
-
-
-
additional information
?
-
-
enzyme cleaves alpha1-2, 1-3 and 1-6 mannosidic linkage from both high-mannose and truncated complex-type N-glycans
-
-
-
additional information
?
-
-
enzyme processes alpha1,6-mannobiose into the product mannose. No activity on alpha1,2-mannobiose, alpha1,3-mannobiose or alpha(1,3)/(1,6)-mannotriose
-
-
-
additional information
?
-
Q97UK5, -
the enzyme could be putatively involved in the turnover and/or the maturation of glycoprotein
-
-
-
additional information
?
-
Q97UK5
the enzyme could be putatively involved in the turnover and/or the maturation of glycoprotein
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2 Man9GlcNAc + 3 H2O
Man8GlcNAc + Man7GlcNAc + 3 alpha-D-mannopyranose
show the reaction diagram
-
-
products from unbound fraction of cobalt-chelating Sepharose
?
2-O-alpha-D-mannopyranosyl-D-mannopyranose + H2O
alpha-D-mannopyranose
show the reaction diagram
-
-
-
?
2-O-alpha-D-mannopyranosyl-D-mannopyranose + H2O
alpha-D-mannopyranose
show the reaction diagram
-
very low activity
-
?
2-O-alpha-D-mannopyranosyl-D-mannopyranose + H2O
alpha-D-mannopyranose
show the reaction diagram
-
highly specific for alpha-1,2-mannosidic linkages
-
?
2-O-alpha-D-mannotriose + H2O
alpha-D-mannopyranose + ?
show the reaction diagram
-
highly specific for alpha-1,2-mannosidic linkages
-
?
3-O-alpha-D-mannopyranosyl-D-mannopyranose + H2O
2 alpha-D-mannopyranose
show the reaction diagram
-
very low activity
-
?
3-O-alpha-D-mannopyranosyl-D-mannopyranose + H2O
2 alpha-D-mannopyranose
show the reaction diagram
-
very low activity
-
?
4-O-alpha-D-mannopyranosyl-D-mannopyranose + H2O
2 alpha-D-mannopyranose
show the reaction diagram
-
specific cleavage of alpha-1,4- or alpha-1,6-linkages
-
?
6-O-alpha-D-mannopyranosyl-D-mannopyranose + H2O
alpha-D-mannopyranose
show the reaction diagram
-
very low activity
-
?
6-O-alpha-D-mannopyranosyl-D-mannopyranose + H2O
alpha-D-mannopyranose
show the reaction diagram
-
specific cleavage of alpha-1,4- or alpha-1,6-linkages
-
?
alpha-(1-2)-mannobiose + H2O
alpha-D-mannopyranose + D-mannopyranose
show the reaction diagram
-
-
-
?
alpha-(1-3)-mannobiose + H2O
alpha-D-mannopyranose + D-mannopyranose
show the reaction diagram
-
highest activity and affinity
-
?
alpha-(1-6)-mannobiose
alpha-D-mannopyranose + D-mannopyranose
show the reaction diagram
-
low activity
-
?
alpha-conglutin + H2O
alpha-D-mannopyranose + ?
show the reaction diagram
-
lupin seed storage glycoprotein, not active to beta- or gamma-conglutin
-
?
alpha-D-Man-(1-2)-alpha-D-Man-(1-2)-alpha-D-Man-(1-3)-[alpha-D-Man-(1-2)-alpha-D-Man-(1-3)-[alpha-D-Man-(1-2)-alpha-D-Man-(1-6)]-alpha-D-Man-(1-6)]-beta-D-Man-(1-4)-beta-D-GlcNAc + 6 H2O
6 alpha-D-mannopyranose + alpha-D-Man-(1-6)-[alpha-D-Man-(1-3)]-beta-D-Man-(1-4)-beta-D-GlcNAc
show the reaction diagram
-
-
-
?
alpha-D-Man-(1-2)-alpha-D-Man-(1-2)-alpha-D-Man-(1-3)-[alpha-D-Man-(1-2)-alpha-D-Man-(1-3)-[alpha-D-Man-(1-2)-alpha-D-Man-(1-6)]-alpha-D-Man-(1-6)]-beta-D-Man-(1-4)-beta-D-GlcNAc + 6 H2O
6 alpha-D-mannopyranose + alpha-D-Man-(1-6)-[alpha-D-Man-(1-3)]-beta-D-Man-(1-4)-beta-D-GlcNAc
show the reaction diagram
-
-
end products
?
alpha-D-Man-(1-2)-alpha-D-Man-(1-2)-alpha-D-Man-(1-3)-[alpha-D-Man-(1-6)-[alpha-D-Man-(1-2)-alpha-D-Man-(1-3)]-alpha-D-Man-(1-6)]-beta-D-Man-(1-4)-beta-D-GlcNAc + H2O
alpha-D-Man-(1-6)-[alpha-D-Man-(1-3)]-beta-D-Man-(1-4)-beta-D-GlcNAc + alpha-D-Man-(1-3)-[alpha-D-Man-(1-6)]-alpha-D-Man-(1-6)-beta-D-Man
show the reaction diagram
-
cleaves asparagine-linked high mannose oligosaccharides to form the core Man3GlcNAc2
-
?
alpha-D-mannopyranoside + H2O
alpha-D-mannopyranose + ?
show the reaction diagram
O09159
-
-
?
alpha-D-mannosidosis fibroblasts + H2O
Manbeta(1-4)GlcNAc + ?
show the reaction diagram
-, O09159
-
-
?
alpha-D-mannosidosis fibroblasts + H2O
Man7-2GlcNAc + ?
show the reaction diagram
-
-
-
?
beta-glucuronidase peptide + H2O
alpha-D-mannopyranose + ?
show the reaction diagram
-
-
-
?
beta-glucuronidase peptide + H2O
alpha-D-mannopyranose + ?
show the reaction diagram
-
-
-
?
GDP-mannosylpyranose + H2O
alpha-D-mannopyranose + GDP
show the reaction diagram
-
-
-
?
GDP-mannosylpyranose + H2O
alpha-D-mannopyranose + GDP
show the reaction diagram
-
-
-
?
Glc3Man9GlcNAc2 + H2O
alpha-D-mannopyranose + ?
show the reaction diagram
-
from oligosaccharide-lipid
-
?
GlcNAcMan5GlcNAc + H2O
alpha-D-mannopyranose + ?
show the reaction diagram
-
-
-
?
GlcNAcMan5GlcNAc + H2O
alpha-D-mannopyranose + ?
show the reaction diagram
-
low activity
-
?
glycopeptide + H2O
alpha-D-mannopyranose + ?
show the reaction diagram
-
-
-
?
glycopeptide + H2O
alpha-D-mannopyranose + ?
show the reaction diagram
-
from ovalbumin
-
?
glycopeptide + H2O
alpha-D-mannopyranose + ?
show the reaction diagram
-
from ovalbumin
-
?
glycopeptide + H2O
alpha-D-mannopyranose + ?
show the reaction diagram
-
from ovalbumin
-
?
glycopeptide + H2O
alpha-D-mannopyranose + ?
show the reaction diagram
-
from ovalbumin
-
?
glycopeptide + H2O
alpha-D-mannopyranose + ?
show the reaction diagram
-
from ovalbumin
-
?
glycopeptide + H2O
alpha-D-mannopyranose + ?
show the reaction diagram
-
from ovalbumin
-
?
glycopeptide + H2O
alpha-D-mannopyranose + ?
show the reaction diagram
-
from ovalbumin
-
?
glycopeptide + H2O
alpha-D-mannopyranose + ?
show the reaction diagram
-
from ovalbumin
-
?
glycopeptide + H2O
alpha-D-mannopyranose + ?
show the reaction diagram
-
from ovalbumin
-
?
glycopeptide + H2O
alpha-D-mannopyranose + ?
show the reaction diagram
-
faster hydrolysis than for glycoprotein
-
?
glycopeptide + H2O
alpha-D-mannopyranose + ?
show the reaction diagram
-
contains only alpha-1,2-linked mannose residues, highly specific on alpha-1,2-linked mannooligosaccharides
-
?
glycopeptide + H2O
alpha-D-mannopyranose + ?
show the reaction diagram
-
stem bromelain
-
?
glycoprotein + H2O
alpha-D-mannopyranose + ?
show the reaction diagram
-
-
-
?
glycoprotein + H2O
alpha-D-mannopyranose + ?
show the reaction diagram
-
-
-
?
glycoprotein + H2O
alpha-D-mannopyranose + ?
show the reaction diagram
-
ovomucoid, orosomucoid, ovalbumin
-
?
high mannose N-glycan + H2O
?
show the reaction diagram
Q99YP5
-
-
-
?
Man-alpha-(1-2)-Man-alpha-(1-6)-[Man-alpha-(1-2)-Man-alpha-(1-3)]-Manalpha-(1-6)-[Man-alpha-(1-2)-Man-alpha-(1-2)-Man-alpha-(1-3)]-Man-beta(1-4)GlcNAc + H2O
?
show the reaction diagram
-
-
-
-
?
Man-glycopeptide + H2O
alpha-D-mannopyranose + ?
show the reaction diagram
-
low activity
-
?
Man3GlcNAc2 + H2O
Man2GlcNAc2 + alpha-D-mannopyranose
show the reaction diagram
-
Man-1,6-linkage only hydrolysed after its Man-1,3-residue is removed
-
?
Man5-9GlcNAc + H2O
alpha-D-mannopyranose + ?
show the reaction diagram
-
low activity for Man5GlcNAc
-
?
Man5GlcNAc + 2 H2O
Man3GlcNAc + 2 alpha-D-mannopyranose
show the reaction diagram
-
-
-
?
Man5GlcNAc2 + H2O
Man4GlcNAc2 + alpha-D-mannopyranose
show the reaction diagram
-
cleaves Man-alpha-(1-3)-linkage 10times faster than the Man-1,6 and the Man-1,2-linkages
mixture of three isomeric oligosaccharides
?
Man5GlcNAc2 + H2O
Man3GlcNAc2 + alpha-D-mannopyranose
show the reaction diagram
-
-
-
?
Man6 + H2O
alpha-D-mannose + ?
show the reaction diagram
-
derived from ovalbumin, alpha-1,2: 1,3: 1,6-linkages, more than 10fold higher specific activity for isoform EII than for EI
-
?
Man6-glycopeptide + H2O
alpha-D-mannopyranose + ?
show the reaction diagram
-
-
-
?
Man6GlcNAc + H2O
alpha-D-mannopyranose + ?
show the reaction diagram
-
-
-
?
Man6GlcNAc + H2O
alpha-D-mannopyranose + ?
show the reaction diagram
-
ordered hydrolysis of alpha(1-2)-residues followed by hydrolysis of alpha(1-3)- and alpha(1-6)-linked residues
-
?
Man7GlcNAc + 2 H2O
Man5GlcNAc + 2 alpha-D-mannopyranose
show the reaction diagram
-
-
-
?
Man7GlcNAc2 + H2O
alpha-D-mannopyranose + ?
show the reaction diagram
-
from oligosaccharide-lipid, very low activity
-
?
Man8GlcNAc + 3 H2O
Man5GlcNAc + 3 alpha-D-mannopyranose
show the reaction diagram
-
-
-
?
Man8GlcNAc2 + 3 H2O
Man5GlcNAc2 + 3 alpha-D-mannopyranose
show the reaction diagram
-
-
-
?
Man8GlcNAc2 + 3 H2O
Man5GlcNAc2 + 3 D-mannose
show the reaction diagram
-
Golgi alpha-mannosidase in vivo
-
-
?
Man9-5GlcNAc + 4 H2O
Man5-3GlcNAc + 4 alpha-D-mannopyranose
show the reaction diagram
-
different product composition for alpha-mannosidases IA, IB and II
-
?
Man9-glycopeptide + H2O
alpha-D-mannopyranose + ?
show the reaction diagram
-
-
-
?
Man9GlcNAc + 4 H2O
Man5GlcNAc + 4 alpha-D-mannopyranose
show the reaction diagram
-
-
-
?
Man9GlcNAc + 4 H2O
Man5GlcNAc + 4 alpha-D-mannopyranose
show the reaction diagram
-
-
end product for Tris-eluted isoform, representing the Man5-oligosaccharide chain of the dolichol pathway formed in the cytosolic compartment during biosynthesis of N-glycosylprotein glycans
?
Man9GlcNAc + 4 H2O
Man5GlcNAc + 4 alpha-D-mannopyranose
show the reaction diagram
-
hydrolyses alpha-1,2- and alpha-1,3-linkages
after 24 h incubation, specifically removes alpha-1,2-linked mannoses
?
Man9GlcNAc + H2O
Manalpha(1-6)[Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)]Manbeta(1-4)GlcNAc + alpha-D-mannopyranose
show the reaction diagram
-
Co2+ activated alpha-mannosidase
end products
?
Man9GlcNAc + H2O
Man8GlcNAc + alpha-D-mannopyranose
show the reaction diagram
-
highly specific soluble catalytic domain of a larger membrane-bound form, does not act on synthetic substrates
releases only one specific mannopyranose residue
?
Man9GlcNAc2 + H2O
Man5-8GlcNAc2 + alpha-D-mannopyranose
show the reaction diagram
-
-
major product: Man5GlcNAc2, involved in Asn-linked oligosaccharide maturation
?
Man9GlcNAc2 + H2O
Man5-8GlcNAc2 + alpha-D-mannopyranose
show the reaction diagram
-
from thyroglobulin or oligosaccharide-lipid, trimming the substrate to Man8GlcNAc2, the substrate for oligosaccharide elongation
only alpha-(1-2)-linked terminal mannoses on the alpha-3-branch of the Man9GlcNAc precursor dispensable
?
Man9GlcNAc2 + H2O
Man5-8GlcNAc2 + alpha-D-mannopyranose
show the reaction diagram
-
involved in N-glycan processing to form oligomannosidic glycans during glycoprotein biosynthesis, cleaves three of the four alpha-1,2-mannosidic linkages
major product: Man6GlcNAc2
?
Man9GlcNAc2 + H2O
Man8GlcNAc2 + mannose
show the reaction diagram
-
endoplasmic reticulum alpha-mannosidase in vivo
-
-
?
Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAc + H2O
alpha-D-mannopyranose + ?
show the reaction diagram
-
-
-
?
Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)[Man(1-6)]ManbetaGlcNac-betaGlcNAc + H2O
alpha-D-mannopyranose + ?
show the reaction diagram
-
-
-
?
Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)[Manbeta(1-6)]ManbetaGlcNAc-beta-GlcNAc + H2O
alpha-D-mannopyranose + ?
show the reaction diagram
-
-
-
?
Manalpha(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAc + H2O
alpha-D-mannopyranose + ?
show the reaction diagram
-
-
-
?
Manalpha(1-2)Manalpha(1-3)[Man(1-6)]ManbetaGlcNAc-betaGlcNAc + H2O
alpha-D-mannopyranose + ?
show the reaction diagram
-
-
-
?
Manalpha(1-3)GlcNAc + H2O
alpha-D-mannopyranose + N-acetyl-D-glucosamine
show the reaction diagram
-
-
-
?
Manalpha(1-3)[Man(1-6)]ManbetaGlcNAc-betaGlcNAc + H2O
alpha-D-mannopyranose + ?
show the reaction diagram
-
-
-
?
Manalpha(1-4)Manbeta(1-4)Man + H2O
alpha-D-mannopyranose + Manbeta(1-4)Man
show the reaction diagram
-
-
-
?
Manalpha(1-6)GlcNAc + H2O
alpha-mannopyranose + N-acetyl-D-glucosamine
show the reaction diagram
-
-
-
?
Manalpha(1-6)[Manalpha(1-3)]Manalpha(1-6)[Manalpha(1-)]Manbeta(1-4)GlcNAc + H2O
alpha-D-mannopyranose + ?
show the reaction diagram
-
4 times faster hydrolysis than Manalpha(1-6)[Manalpha(1-3)]Manalpha(1-6)[Manalpha(1-3)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc
-
?
Manalpha(1-6)[Manalpha(1-3)]Manalpha(1-6)[Manalpha(1-3)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc + H2O
alpha-D-mannopyranose + ?
show the reaction diagram
-
-
-
?
mannan + H2O
alpha-D-mannose + ?
show the reaction diagram
-
very low activity
-
?
mannan + H2O
alpha-D-mannose + ?
show the reaction diagram
-
very low activity
-
?
mannan + H2O
alpha-D-mannose + ?
show the reaction diagram
-
yeast alpha-mannan, main product: alpha-D-mannose, hydrolysis of linear and branched mannans containing terminal alpha-1,2- and alpha-1,3-linked mannopyranosyl residues
-
?
mannan + H2O
alpha-D-mannose + ?
show the reaction diagram
-
from yeast
-
?
mannan + H2O
alpha-D-mannose + ?
show the reaction diagram
-
from yeast
-
?
mannan + H2O
alpha-D-mannose + ?
show the reaction diagram
-
from yeast
-
?
mannan + H2O
alpha-D-mannose + ?
show the reaction diagram
-
from yeast
only mannose librated
?
mannan + H2O
alpha-D-mannose + ?
show the reaction diagram
-
from baker's and sake yeast
-
?
mannan + H2O
alpha-D-mannose + ?
show the reaction diagram
-
from baker's and sake yeast
-
?
mannan + H2O
alpha-D-mannose + ?
show the reaction diagram
-
specific for alpha-1,2-linked mannopyranosyl residues
-
?
mannan + H2O
alpha-D-mannose + ?
show the reaction diagram
-
derived from wild type or mutant strains of Saccharomyces cerevisiae, different specific activities for isoforms EI and EII, depending on the type of alpha-D-linkages of mutant substrates, preference for cleavage of alpha-1,6- and alpha-1,3-linkages
-
?
mannobiose + H2O
alpha-D-mannopyranose + D-mannopyranose
show the reaction diagram
-
-
-
?
mannobiose + H2O
alpha-D-mannopyranose + D-mannopyranose
show the reaction diagram
-
-
-
?
mannopyranosyl-oligosaccharides + H2O
alpha-D-mannopyranose + ?
show the reaction diagram
-
from yeast mannan, hydrolysis of alpha-1,2- and alpha-1,3-linkages
-
?
mannopyranosyl-oligosaccharides + H2O
alpha-D-mannopyranose + ?
show the reaction diagram
-
from yeast mannan, hydrolysis of alpha-1,2- and alpha-1,3-linkages
-
?
mannopyranosyl-oligosaccharides + H2O
alpha-D-mannopyranose + ?
show the reaction diagram
-
from yeast mannan, a tetrasaccharide terminating in a mannopyranosyl residue linked to C-3 of its neighbour is not hydrolysed
-
?
mannopyranosyl-oligosaccharides + H2O
alpha-D-mannopyranose + ?
show the reaction diagram
-
reverse action on alpha-D-mannopyranose, 85%, w/w, yields 0.93 M disaccharide with 4 different isomers, 0.61 M trisaccharide, 0.25 M tetrasaccharide and higher oligosaccharides, retention of anomeric configuration
-
r
mannosyl rhamnose + H2O
alpha-D-mannopyranose + rhamnose
show the reaction diagram
-
part of the repeating oligosaccharide unit of the O-antigenic lipopolysaccharide in Salmonella typhimurium
-
?
mannotetraose + H2O
alpha-D-mannopyranose + mannotriose
show the reaction diagram
-
-
-
?
mannotetraose + H2O
alpha-D-mannopyranose + mannotriose
show the reaction diagram
-
-
-
?
ribonuclease B + H2O
oligosaccharide + alpha-D-mannopyranose + ?
show the reaction diagram
-
-
-
-
?
ribonuclease B + H2O
oligosaccharide + alpha-D-mannopyranose + ?
show the reaction diagram
-
from bovine pancreas
single oligosaccharide component
?
TAKA-amylase A + H2O
alpha-D-mannopyranose + ?
show the reaction diagram
-
-
-
?
TAKA-amylase A + H2O
alpha-D-mannopyranose + ?
show the reaction diagram
-
-
-
?
TAKA-amylase A + H2O
alpha-D-mannopyranose + ?
show the reaction diagram
-
from Aspergillus oryzae, hydrolysis of a single Man-1,2-linkage
-
?
thyroglobulin + H2O
alpha-D-mannopyranose + ?
show the reaction diagram
-
-
-
?
thyroglobulin peptide A + H2O
alpha-D-mannopyranose + ?
show the reaction diagram
-
-
-
?
thyroglobulin peptide A + H2O
alpha-D-mannopyranose + ?
show the reaction diagram
-
-
-
?
mannotriose + H2O
alpha-D-mannopyranose + mannobiose
show the reaction diagram
-
-
-
?
additional information
?
-
-
anomalies of the enzyme system detected in patients with amyotrophic lateral sclerosis could reflect a situation of progressive injury of proteins
-
-
-
additional information
?
-
-
key enzyme in N-glycan processing
-
-
-
additional information
?
-
-
the enzyme is required in the degradation of the asparagine-linked carbohydrates of glycoproteins. Deficiency of this enzyme leads to the lysosomal storage disorder alpha-mannosidosis
-
-
-
additional information
?
-
-
class 1 alpha1,2-mannosidases of glycosylhydrolase family 47 play critical roles in the maturation of Asn-linked glycoproteins in the endoplasmic reticulum and Golgi complex as well as in the recognition and timing of disposal of terminally unfolded proteins by ER-associated degradation, overview
-
-
-
additional information
?
-
-
the enzyme is involved in ordered degradation of glycoproteins, inborn enzyme-deficiency results in lysosomal storage disorder alpha-mannosidosis
-
-
-
additional information
?
-
-
the exo-type cytosolic class II enzyme cleaves off alpha-1,2-, alpha-1,3-, and alpha-1,6-mannose residues
-
-
-
additional information
?
-
Q99YP5
higher eukaryotic GH38 alpha-mannosides play a key role in the modification and diversification of hybrid N-glycans, processes with strong cellular links to cancer and autoimmune disease
-
-
-
additional information
?
-
Q97UK5, -
the enzyme could be putatively involved in the turnover and/or the maturation of glycoprotein
-
-
-
additional information
?
-
Q97UK5
the enzyme could be putatively involved in the turnover and/or the maturation of glycoprotein
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ca2+
-
slight stimulation for enzyme II between 0.5 and 2.5 mM
Ca2+
-
requirement for divalent cations with preference for Ca2+
Ca2+
-
inhibition by EGTA can be 90% restored after addition of 0.1 mM
Ca2+
-
moderate activation at 1 mM
Ca2+
-
20-30% activation at 5 mM
Ca2+
-
28% stimulation at 0.1 mM
Ca2+
-
strong activation
Ca2+
-
is critical in coordination of the enzyme's (alphaalpha)7 barrel structure, located at the base of the barrel
Cd2+
-
maximal activity of 56 U/mg is reached at 1 mM CoCl2. Inactive in absence of metal ion
Cd2+
-
preferred divalent cation
Cd2+
-, Q6L2X5
potent activator at concentration of 1 mM, 12.5fold activation compared to the apoenzyme
Cd2+
-
0.01 and 0.1 mM, activates recombinant enzyme
Cd2+
-
with alpha-1,2-, alpha-1,3-, alpha-1,4-, or alpha-1,6-mannobiose as a substrate, Co2+ is the only metal ion promoting hydrolysis of all substrates. Mn2+, Cd2+, and Zn2+ can substitute to a varying extent
Co2+
-
24fold activation after preincubation with 1 mM
Co2+
-
activation for Tris-eluted isoform from cobalt-chelating Sepharose
Co2+
-
20% activation at 1 mM
Co2+
-
activation after preincubation at 1.4 mM, activation persists even after removal of Co2+
Co2+
-
slight activation for alpha-mannosidase II
Co2+
-
60% activation up to 2.5 mM
Co2+
-
2-3fold increase of activity for neutral alpha-mannosidases
Co2+
-
-
Co2+
-
0.1 mM enhances activity 30.2fold
Co2+
-
maximal activity of 51 U/mg is reached at 1 mM CoCl2. Inactive in absence of metal ion
Co2+
-
activates, purified enzyme carries two Co2+ ions, the enzyme treated with Co2+ carries four. Co2+ regulates the substrate specificity of the enzyme. The Co2+-treated enzyme produces Man-alpha-(1-6)-[Man-alpha-(1-2)-Man-alpha-(1-2)-Man-alpha-(1-3)]-Man-beta-(1-4)-GlcNAc and alpha-D-mannose as end products from Man-alpha-(1-2)-Man-alpha-(1-6)-[Man-alpha-(1-2)-Man-alpha-(1-3)]-Manalpha-(1-6)-[Man-alpha-(1-2)-Man-alpha-(1-2)-Man-alpha-(1-3)]-Man-beta(1-4)GlcNAc in presence of Co2+. Before tretament with Co2+ the enzyme is able to cleave a single Man-alpha-(1-2) residue from Man-alpha-(1-2)-Man-alpha-(1-6)-[Man-alpha-(1-2)-Man-alpha-(1-3)]-Manalpha-(1-6)-[Man-alpha-(1-2)-Man-alpha-(1-2)-Man-alpha-(1-3)]-Man-beta(1-4)GlcNAc to give Man-alpha-(1-6)-[Man-alpha-(1-2)-Man-alpha(1-3)]-Man-alpha-(1-6)-[Man-alpha-(1-2)-Man-alpha-(1-2)-Man-alpha(1-3)]-Man-beta-(1-4)-GlcNAc as the end product
Co2+
-
preferred divalent cation
Co2+
Q68EM8
enhances acivity, alpha-mannosidase in absence of Co2+ only converts mannosyl(9)-N-acetyl-glucosamine into mannosyl(8)-N-acetyl-glucosamine, in presence of Co2+, alpha-mannosidase yields mannosyl(5)-N-acetyl-glucosamine
Co2+
-, Q6L2X5
8.3fold activation at a concentration of 10 mM, resistance of ManA to heat inactivation is increased by presence of Co2+
Co2+
-
0.01 and 0.1 mM, activates recombinant enzyme
Co2+
-
with alpha-1,2-, alpha-1,3-, alpha-1,4-, or alpha-1,6-mannobiose as a substrate, Co2+ is the only metal ion promoting hydrolysis of all substrates. Mn2+, Cd2+, and Zn2+ can substitute to a varying extent
Cr2+
-
weak activation
Fe2+
-, Q6L2X5
4.5fold activation at a concentration of 10 mM
Mg2+
-
slight stimulation for enzyme II between 0.5 and 2.5 mM
Mg2+
-
slight activation at 1 mM
Mg2+
-
moderate activation at 1 mM
Mg2+
-
50% stimulation at 0.1 mM
Mg2+
-
0.1 mM, activates recombinant enzyme
Mn2+
-
1 mM enhances activity 6fold
Mn2+
-, Q6L2X5
3.8fold activation at a concentration of 10 mM
Mn2+
-
1 mM, activates recombinant enzyme
Ni2+
-
0.1 mM, enhances activity to 119% of control
Zn2+
-
30% stimulation of the EGTA-inhibited enzyme at 0.1 mM
Zn2+
-
nearly 80% stimulation at 1 mM
Zn2+
-
25% stimulation
Zn2+
-
25% stimulation
Zn2+
-
10% stimulation at 10 mM
Zn2+
-
enhanced activity at 0.3-1 mM
Zn2+
-
4 mM required for maximum activity
Zn2+
-
slight activation for alpha-mannosidase II
Zn2+
-
maximum activity at 1 mM
Zn2+
-
90% stimulation at 0.1 mM
Zn2+
-
contains 2 mol Zn/mol enzyme
Zn2+
-
30% activation up to 2.5 mM
Zn2+
-
contains 2 mol Zn/mol enzyme
Zn2+
-
slight activation at 0.02 mM
Zn2+
-
weak activation
Zn2+
-
required
Zn2+
-
alpha mannosidase is Zn2+ dependent
Zn2+
Q99YP5
involved in catalysis
Zn2+
-
the enzyme binds Zn2+ in vivo, it contains 2.9 Zn2+ per trimeric enzyme, corresponding to a single atom per subunit. 0.1 mM Zn2+ showes 2fold activation of recombinant enzyme
Zn2+
-
with alpha-1,2-, alpha-1,3-, alpha-1,4-, or alpha-1,6-mannobiose as a substrate, Co2+ is the only metal ion promoting hydrolysis of all substrates. Mn2+, Cd2+, and Zn2+ can substitute to a varying extent
Mn2+
-
with alpha-1,2-, alpha-1,3-, alpha-1,4-, or alpha-1,6-mannobiose as a substrate, Co2+ is the only metal ion promoting hydrolysis of all substrates. Mn2+, Cd2+, and Zn2+ can substitute to a varying extent
additional information
-, Q6L2X5
Zn2+, Ca2+, Mg2+, Ba2+, K+, and Li+ had no significant effect on ManA activity at a concentration of 1 mM or 10 mM
additional information
-
no change in the enzymatic activity is observed with Cu2+ or Ni2+ at 0.001-1 mM
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
(1R,6R,7R,8S)-7,8-dihydroxy-5-thia-1-thioniabicyclo[4.3.0]nonane chloride
-
synthetic inhibitor, selective and potent inhibition at 1 mM, 97% inhibition of the activity of the liver lysosomal fraction at pH 4.0, 100% at pH 6.5
(1S,2R,3R,8R,8aR)-3-[(arylmethoxy)methyl]octahydroindolizine-1,2,8-triol
-
-
(1S,2R,8R,8aR)-octahydroindolizine-1,2,8-triol
-
-
(2R,3R,4S)-2-(aminomethyl)pyrrolidine-3,4-diol
-
1 mM, 81% inhibition, competitive
(2R,3R,4S)-2-(aminomethyl)pyrrolidine-3,4-diol
-
1 mM, 51% inhibition
(2R,3R,4S)-2-([(1R)-2,3-dihydro-1H-inden-1-ylamino]methyl)pyrrolidine-3,4-diol
-
IC50 is 0.017 mM
(2R,3R,4S)-2-([[(1R)-1-hydroxyethyl]amino]methyl)pyrrolidine-3,4-diol
-
1 mM, 75% inhibition, competitive
(2R,3R,4S)-2-([[(1R)-1-hydroxyethyl]amino]methyl)pyrrolidine-3,4-diol
-
1 mM, 39% inhibition
(2R,3R,4S)-2-([[(1R)-2-hydroxy-1-phenylethyl]amino]methyl)pyrrolidine-3,4-diol
-
-
(2R,3R,4S)-2-([[(1S)-1-hydroxyethyl]amino]methyl)pyrrolidine-3,4-diol
-
1 mM, 66% inhibition, competitive
(2R,3R,4S)-2-([[(1S)-1-hydroxyethyl]amino]methyl)pyrrolidine-3,4-diol
-
1 mM, 45% inhibition
(2R,3R,4S)-2-hydroxymethyl-pyrrolidine-3,4-diol
-
1 mM, 54% inhibition
(2R,3R,4S)-2-hydroxymethyl-pyrrolidine-3,4-diol
-
1 mM, 37% inhibition
(2R,3R,4S)-2-phenylaminomethyl-pyrrolidine-3,4-diol
-
1 mM, 92% inhibition, competitive
(2R,3R,4S)-2-phenylaminomethyl-pyrrolidine-3,4-diol
-
1 mM, 69% inhibition, competitive
(2R,3R,4S)-2-[(1-phenyl-ethylamino)-methyl]-pyrrolidine-3,4-diol
-
1 mM, 66% inhibition, competitive
(2R,3R,4S)-2-[(1-phenyl-ethylamino)-methyl]-pyrrolidine-3,4-diol
-
1 mM, 48% inhibition
(2R,3R,4S)-2-[(benzylamino)methyl]pyrrolidine-3,4-diol
-
IC50 is 0.06 mM
(2R,3R,4S)-2-[(cyclopentylamino)methyl]pyrrolidine-3,4-diol
-
1 mM, 60% inhibition
(2R,3R,4S)-2-[(cyclopentylamino)methyl]pyrrolidine-3,4-diol
-
1 mM, 53% inhibition
(2R,3R,4S)-2-[([(1R)-2-benzyloxy-1-phenylethyl]amino)methyl]pyrrolidine-3,4-diol
-
92% inhibition at 1 mM, IC50 is 0.058 mM
(2R,3R,4S)-2-[([(1R)-2-hydroxy-1-phenylethyl]amino)methyl]pyrrolidine-3,4-diol
-
complete and selective inhibition at 1 mM, IC50 is 700 nM
(2R,3R,4S)-2-[([(1R)-2-hydroxy-1-phenylethyl]amino)methyl]pyrrolidine-3,4-diol
-
; potent and selective inhibition
(2R,3R,4S)-2-[([(1R)-2-methoxy-1-phenylethyl]amino)methyl]pyrrolidine-3,4-diol
-
77% inhibition at 1 mM
(2R,3R,4S)-2-[([(1R,2S)-2-hydroxy-1,2-diphenylethyl]amino)methyl]pyrrolidine-3,4-diol
-
88% inhibition at 1 mM, IC50 is 0.11 mM
(2R,3R,4S)-2-[([(1S)-2-hydroxy-1-phenylethyl]amino)methyl]pyrrolidine-3,4-diol
-
92% inhibition at 1 mM, IC50 is 0.1 mM
(2R,3R,4S)-2-[([(1S)-2-hydroxy-1-phenylethyl]amino)methyl]pyrrolidine-3,4-diol
-
-
(2R,3R,4S)-2-[([(1S,2R)-2-hydroxy-1,2-diphenylethyl]amino)methyl]pyrrolidine-3,4-diol
-
84% inhibition at 1 mM, IC50 is 0.128 mM
(2R,3R,4S)-2-[2-(phenylamino)ethyl]pyrrolidine-3,4-diol
-
1 mM, 33% inhibition
(2R,3R,4S)-2-[[(1-benzyl-piperidin-4-ylmethyl)-amino]-methyl]-pyrrolidine-3,4-diol
-
1 mM, 55% inhibition
(2R,3R,4S)-2-[[(1-benzyl-piperidin-4-ylmethyl)-amino]-methyl]-pyrrolidine-3,4-diol
-
1 mM, 59% inhibition
(2R,3R,4S)-2-[[(2H-Imidazol-1-ylmethyl)-amino]-methyl]-pyrrolidine-3,4-diol
-
1 mM, 55% inhibition
(2R,3R,4S)-2-[[(2H-Imidazol-1-ylmethyl)-amino]-methyl]-pyrrolidine-3,4-diol
-
1 mM, 59% inhibition
(2R,3R,4S)-2-[[(furan-2-ylmethyl)-amino]-methyl]-pyrrolidine-3,4-diol
-
1 mM, 49% inhibition
(2R,3R,4S)-2-[[(furan-2-ylmethyl)-amino]-methyl]-pyrrolidine-3,4-diol
-
1 mM, 29% inhibition
(2R,3R,4S)-2-[[(thiophen-2-ylmethyl)-amino]-methyl]-pyrrolidine-3,4-diol
-
1 mM, 89% inhibition, competitive
(2R,3R,4S)-2-[[(thiophen-2-ylmethyl)-amino]-methyl]-pyrrolidine-3,4-diol
-
1 mM, 68% inhibition, competitive
(2R,3R,4S,5R)-2-[(benzylamino)methyl]-5-(hydroxymethyl)pyrrolidine-3,4-diol
-
IC50 is 0.0062 mM
(2R,3S,4R,5R)-2-(hydroxymethyl)-5-[([(1R)-2-hydroxy-1,2-diphenylethyl]amino)methyl]pyrrolidine-3,4-diol
-
98% inhibition at 1 mM, IC50 is 0.0042 mM
(2S)-2-[([(2R,3S,4S)-3,4-dihydroxypyrrolidin-2-yl]methyl)amino]-2-phenylethyl 2-fluorobenzoate
-
83% inhibition at 1 mM, IC50 is 0.063 mM
(2S)-2-[([(2R,3S,4S)-3,4-dihydroxypyrrolidin-2-yl]methyl)amino]-2-phenylethyl 2-fluorobenzoate
-
-
(2S)-2-[([(2R,3S,4S)-3,4-dihydroxypyrrolidin-2-yl]methyl)amino]-2-phenylethyl 3-bromobenzoate
-
79% inhibition at 1 mM
(2S)-2-[([(2R,3S,4S)-3,4-dihydroxypyrrolidin-2-yl]methyl)amino]-2-phenylethyl 3-bromobenzoate
-
-
(2S)-2-[([(2R,3S,4S)-3,4-dihydroxypyrrolidin-2-yl]methyl)amino]-2-phenylethyl 4-bromobenzoate
-
92% inhibition at 1 mM
(2S)-2-[([(2R,3S,4S)-3,4-dihydroxypyrrolidin-2-yl]methyl)amino]-2-phenylethyl 4-bromobenzoate
-
-
(2S)-2-[([(2R,3S,4S)-3,4-dihydroxypyrrolidin-2-yl]methyl)amino]-2-phenylethyl 4-fluorobenzoate
-
92% inhibition at 1 mM, IC50 is 0.060 mM
(2S)-2-[([(2R,3S,4S)-3,4-dihydroxypyrrolidin-2-yl]methyl)amino]-2-phenylethyl 4-fluorobenzoate
-
-
(3R,4R,5R)-3,4-dihydroxy-5-([[(1R)-2-hydroxy-1-phenylethyl]amino]methyl)-1-methylpyrrolidin-2-one
-
-
(3R,4R,5R)-3,4-dihydroxy-5-([[(1R)-2-hydroxy-1-phenylethyl]amino]methyl)pyrrolidin-2-one
-
-
(3S,4R)-pyrrolidine-3,4-diol
-
1 mM, 70% inhibition
(3S,4R)-pyrrolidine-3,4-diol
-
1 mM, 40% inhibition
1,6-dideoxy-1,6-episulfinyl-beta-D-mannose
-
XLM, sulfoxide derivative, thiolevomannosan analog, more potent than kifunensine and deoxymannojirimycin, docking studies with the crystal structure of human alpha-1,2-mannosidase complexed with kifunensine (PDB: 1FO3) as a template
1,6-dideoxy-1,6-episulfonyl-beta-D-mannose
-
NLM, sulfone derivative, thiolevomannosan analog, more potent than kifunensine and deoxymannojirimycin, docking studies with the crystal structure of human alpha-1,2-mannosidase complexed with kifunensine (PDB: 1FO3) as a template
1,6-dideoxy-1,6-epithio-beta-D-mannose
-
thiolevomannosan TLM, docking studies with the crystal structure of human alpha-1,2-mannosidase complexed with kifunensine (PDB: 1FO3) as a template
1-cyclohexyl-3-(2-morpholinyl-4-ethyl)carbodiimide
-
inhibitory at 25 mM, pseudo-first-order kinetic
1-deoxy-mannojirimycin
-
complete inhibition
1-deoxymannojirimicin
-
hydrolysis of 4-methylumbelliferyl-alpha-D-mannnopyranoside, strong inhibition for enzymes I and II at 0.025 mM
1-deoxymannojirimicin
-
complete inhibition at 1 mM
1-deoxymannojirimicin
-
19% inhibition at 0.01 mM
1-deoxymannojirimicin
-
IC50 = 0.01 mM
1-deoxymannojirimicin
-
67% inhibition at 1 mM when 4-methylumbelliferyl-alpha-D-mannopyranoside is used, 15% inhibition when p-nitrophenyl-alpha-D-mannopyranoside is used as substrates
1-deoxymannojirimicin
-
50% inhibition at 0.05 mM
1-deoxymannojirimycin
-
61% inhibition of the activity of the liver lysosomal fraction at pH 4.0, 37% at pH 6.5, at 1 mM
1-deoxymannojirimycin
-
class 1 alpha1,2-mannosidase inhibitor
1-deoxymannojirimycin
-
binding of swainsonine to the enzyme is stronger than bionding of 1-deoxymannojirimycin; competitive inhibitor, low binding up to 40C, increased binding at 50C
1-deoxymannojirimycin
-
pretreatment with 1-deoxymannojirimycin protectes primary cultured mouse cortical neurons from Amyloid beta1-42 toxicity
1-deoxymannojirimycin
-
pretreatment with 100 mM inhibitor 1-deoxymannojirimycin in PC-12 cells significantly attenuates the cytotoxicity by endoplasmic reticulum stressors tunicamycin, thapsigargin, and amyloid bbeta1-42, and reduces caspase-3 activation by tunicamycin and thapsigarin
1-deoxymannojirimycin
-
-
2-(2,2-dihydroxy-ethyl)-pyrrolidine-3,4-diol
-
1 mM, 81% inhibition, mixed type
2-(2,2-dihydroxy-ethyl)-pyrrolidine-3,4-diol
-
1 mM, 56% inhibition
2-amino-2-deoxy-D-glucose
-
competitive inhibition, Ki = 2.8 mM
2-deoxy-2-fluoro-alpha-D-mannosyl fluoride
-
for mutant enzyme D341N, no inhibition of wild-type enzyme
3-bromo-N-[(2S)-2-[([(2R,3S,4R)-3,4-dihydroxypyrrolidin-2-yl]methyl)amino]-2-phenylethyl]benzamide
-
95% inhibition at 1 mM, IC50 is 0.089 mM
3-bromo-N-[(2S)-2-[([(2R,3S,4R)-3,4-dihydroxypyrrolidin-2-yl]methyl)amino]-2-phenylethyl]benzamide
-
-
5-fluoro-beta-L-gulosyl fluoride
-
reversible, acts as a slow substrate for the D341 mutant enzyme, with deglycosylation as the rate-limiting step. Inactivation is only observed when assayed at low temperatures such that deglycosylation is slow relative to the assay time
8,8a-di-epi-swainsonine
-
-
8a-epi-swainsonine
-
-
Ag+
-
slight inhibition at 1 mM for isoforms I, II
Ag+
-
moderate inhibition at 1 mM
Ag+
-
70% inhibition at 1 mM
Ag+
-
97% inhibition at 10 mM
Ag+
-
52% inhibition at 10 mM
Ag+
-, Q6L2X5
strong inhibitor at concentrations of 1 mM or 10 mM
alpha-conglutin
-
11% inhibition at saturation
-
alpha-D-1,2-mannopyranosyl-mannopyranose
-
50% inhibition at 4 mM
alpha-D-1,3-mannopyranosyl-mannopyranose
-
50% inhibition at 18 mM
-
alpha-D-1,6-mannopyranosyl-mannopyranose
-
50% inhibition at 100 mM
alpha-D-mannopyranose
-
55% inhibition at 30 mM
alpha-D-mannopyranose
-
27% inhibition at 10 mM
alpha-D-mannopyranose
-
competitive inhibition, Ki: 22 mM
alpha-D-mannopyranose
-
50% inhibition at 250 mM
alpha-D-mannopyranose
-
29% inhibition at 10 mM
alpha-D-mannopyranose
-
competitive inhibition, Ki: 85 mM
alpha-D-mannopyranose
-
competitive inhibition, Ki: 20 mM
alpha-D-mannopyranose
-
30% inhibition at 250 mM
Ba2+
-
78% inhibition at 10 mM
Ba2+
-
inhibition at 1 mM
Ca2+
-
inhibitory for enzyme I above 5 mM, enzyme II not affected
Ca2+
-
53% inhibition at 0.1 mM
Ca2+
-
slight inhibition at 1 mM
Ca2+
-
inhibition at 0.1 mM
Cd2+
-
54% inhibition at 10 mM, slight stimulation at 1 mM
Cd2+
-
inhibition at 0.1 mM
Co2+
-
46% inhibition at 1 mM
Co2+
-
slight inhibition at 1 mM
Co2+
-
57% inhibition at 1 mM
Co2+
-
slight inhibition at 10 mM
Co2+
-
inhibition of alpha-mannosidases IA and IB
Co2+
-
51% inhibition at 10 mM
Co2+
-
10-30% inhibition for acid alpha-mannosidase
Cu2+
-
complete inhibition of the Co2+ activated enzyme at 0.5 mM
Cu2+
-
complete inhibition at 1 mM
Cu2+
-
complete inhibition at 0.1 mM
Cu2+
-
strong inhibition at 1 mM
Cu2+
-
complete inhibition at 1 mM
Cu2+
-
nearly complete inhibition at 0.01 mM
Cu2+
-
slight inhibition at 0.1 mM
Cu2+
-
strong inhibition at 1 mM
Cu2+
-
slight inhibition at 10 mM
Cu2+
-
inhibition of alpha-mannosidases IA, IB and II
Cu2+
-
10% inhibition at 10 mM, alpha-mannosidase A
Cu2+
-
41% inhibition at 10 mM
Cu2+
-
87% inhibition at 20 mM
Cu2+
-
nearly complete inhibition at 0.005 mM
Cu2+
-
inhibition at 0.1 mM
Cu2+
-
potent inhibitor
Cu2+
-, Q6L2X5
strong inhibitor at concentrations of 1 mM or 10 mM
Cu2+
-
inhibits in presence of Co2+
cysteine
-
31% inhibition at 0.02 mM
D-glucose
-
67% inhibition at 30 mM
D-glucuronic acid
-
slight inhibition at 10 mM
D-mannono-1,4-lactone
-
11% inhibition at 10 mM
D-mannono-1,4-lactone
-
36% inhibition at 10 mM
D-mannono-1,4-lactone
-
Ki: 23.8 mM
D-mannono-1,4-lactone
-
competitive inhibition, Ki: 13 mM
D-Mannono-1,5-lactone
-
50% competitive inhibition at 0.073 mM
D-Mannono-1,5-lactone
-
complete inhibition at 1 mM
D-Mannono-1,5-lactone
-
weak inhibition
D-mannosylamine
-
56% inhibition at 1 mM
D-mannosylamine
-
15% competitive inhibition at 5 mM
D-mannosylamine
-
-
D-mannosylamine
-
competitive inhibition, Ki = 0.007 mM
deoxymannojirimycin
-
-
deoxymannojirimycin
-
-
deoxymannojirimycin
Q68EM8
less effective compared with swainsonine, concentration of 100 microM
deoxymannojirimycin
-
DMJ 3
deoxymannojirimycin
-
-
diisopropylfluorophosphate
-
42% inhibition at 10 mM
EDTA
-
complete inhibition at 20 mM, activity recovered in the presence of Ca2+
EDTA
-
complete inhibition at 0.05 mM
EDTA
-
37% inhibition at 5 mM
EDTA
-
strong inhibition at 1 mM
EDTA
-
complete inhibition at 1 mM, addition of 1 mM Zn2+ fully restores activity for isoforms II, to 69% for isoforms I
EDTA
-
addition of Ca2+ reverses inhibitory effect
EDTA
-
strong inhibition at 1 mM
EDTA
-
addition of Zn2+ restores inhibitory effect
EDTA
-
addition of Zn2+ restores inhibitory effect
EDTA
-
slight inhibition at 1 mM
EDTA
-
60-75% inhibition at 4 mM, activity restored by addition of Ca2+
EDTA
-
addition of Zn2+ restores inhibitory effect
EDTA
-
inhibitory for alpha-mannosidases IA and IB
EDTA
-
addition of Zn2+ restores inhibitory effect
EDTA
-
slight inhibition at 1 mM
EDTA
-
addition of Zn2+ restores inhibitory effect
EDTA
-
addition of Zn2+ restores inhibitory effect
EDTA
-
addition of Zn2+ restores inhibitory effect; strong inhibition at 1 mM
EDTA
-
1 mM, more than 90% inactivation
EDTA
-, Q6L2X5
supplied in equimolar amounts or in excess, neutralizes also effect of resistance of ManA to heat inactivation
EGTA
-
32% inhibition at 5 mM
EGTA
-
complete inhibition at 5 mM
Fe2+
-
54% inhibition at 1 mM
-
Fe2+
-
slight inhibition at 1 mM
-
Fe2+
-
complete inhibition at 1 mM
-
Fe2+
-
nearly complete inhibition at 1 mM
-
Fe2+
-
slight inhibition at 10 mM
-
Fe2+
-
-
-
Fe2+
-
58% inhibition at 10 mM
-
Fe2+
-
-
-
Fe2+
-
22% inhibition at 20 mM
-
Fe2+
-
potent inhibitor
-
Fe3+
-
43% inhibition at 1 mM
-
Fe3+
-
-
-
Fe3+
-
inhibition at 1 mM
-
Fe3+
-, Q6L2X5
strong inhibitor at concentrations of 1 mM or 10 mM
-
gluco-hydroxyiminolactam
-
-
Hg2+
-
complete inhibition at 1 mM
Hg2+
-
slight inhibition at 1 mM for isoforms I,II
Hg2+
-
complete inhibition at 1 mM
Hg2+
-
45% inhibition at 10 mM
Hg2+
-
complete inhibition at 10 mM
Hg2+
-
strong inhibitor
iodoacetamide
-
slight inhibition at 1 mM
iodoacetic acid
-
slight inhibition at 1 mM
iodoacetic acid
-
slight inhibition at 0.1 mM
kifunensine
-
class 1 alpha1,2-mannosidase inhibitor
kifunensine
Q68EM8
little inhibitory effect, concentration of 10 microM
kifunensine
-
Kif 2, docking studies with the crystal structure of human alpha-1,2-mannosidase complexed with kifunensine (PDB: 1FO3) as a template
Li+
-
88% inhibition at 20 mM
Mannan
-
33% inhibition at 50 mM
Mannose
-
relative inhibition of 67.8%, potent inhibitor, three concentrations of 10, 50, and 100 mM tested
methyl-alpha-D-glucoside
-
23% inhibition at 10 mM
methyl-alpha-D-lyxopyranosyl-(1'-2)-alpha-D-mannopyranoside
-
-
methyl-alpha-D-lyxopyranosyl-(1-2)-alpha-D-mannopyranoside
-
potent
methyl-alpha-D-mannopyranoside
-
41% inhibition at 10 mM
methyl-alpha-D-mannopyranoside
-
20% inhibition at 10 mM
methyl-alpha-D-mannopyranoside
-
slight inhibitory for alpha-mannosidases IA and IB
methyl-alpha-D-mannopyranoside
-
37% inhibition at 0.1 mM
methyl-alpha-D-mannopyranoside
-
40-50% inhibition of acid alpha-mannosidase, neutral alpha-mannosidase not affected
Mg2+
-
slight inhibition at 1 mM
Mg2+
-
61% inhibition at 20 mM
Mg2+
-
inhibition at 1 mM
Mn2+
-
inhibitory for enzyme I above 5 mM, slightly inhibitory for enzyme II
Mn2+
-
slight inhibition at 1 mM
Mn2+
-
slight inhibition at 1 mM
Mn2+
-
58% inhibition at 0.1 mM
Mn2+
-
complete inhibition at 1 mM
Mn2+
-
slight inhibition at 1 mM
Mn2+
-
slight inhibition at 1 mM
N-bromosuccinimide
-
N-bromosuccinimide modified inactivation, effect of Trp modification on enzyme activity
N-octyl-6-epi-valienamine
-
-
NaN3
-
slight inhibition at 0.1 mM
Ni2+
-
moderate inhibition at 1 mM
Ni2+
-, Q6L2X5
strong inhibitor at concentrations of 1 mM or 10 mM
Ni2+
-
inhibits in presence of Co2+
p-chloromercuribenzenesulfonic acid
-
complete inhibition at 1 mM
p-chloromercuribenzenesulfonic acid
-
different inhibition rates for alpha-mannosidases IA, IB and II
p-chloromercuribenzenesulfonic acid
-
50% inhibition at 0.35 mM, activity is restored by addition of substrate
p-chloromercuribenzenesulfonic acid
-
strong inhibition at 1 mM
p-nitrophenyl-alpha-D-mannopyranoside
-
substrate inhibition greater than 2 mM
Pb2+
-
complete inhibition of the Co2+ activated enzyme at 0.5 mM
Pb2+
-
moderate inhibition at 1 mM
SDS
-
85% inhibition at 0.05%, w/v
small interfering RNA
Q68EM8
siRNA designed to specifically inhibit Man2C1 gene expression, alpha-mannosidase activity is compromised in siRNA-treated cells. Determination of alteration of siRNA treatment, glycans recovered from membrane glycoproteins are fluorescence-labelled and analysed by HPLC
-
Sr2+
-
inhibition at 1 mM
swainsonine
-
hydrolysis of 4-umbelliferyl-alpha-D-mannopyranoside, strong inhibition for enzymes I and II at 0.025 mM
swainsonine
-
50% inhibition at 0.00024 mM
swainsonine
O09159
IC50: 0.00015 mM
swainsonine
-
complete inhibition of the Co2+ activated enzyme at 0.01 mM
swainsonine
-
IC50: 0.00011 mM
swainsonine
-
inhibition of both Tris-eluted and unbound isoforms from cobalt-chelating Sepharose, unbound: Ki: 0.028 mM, Tris-eluted: Ki: 0.004 mM
swainsonine
-
83% inhibition at 0.3 mM if 4-methylumbelliferyl-alpha-D-mannopyranoside is used, hydrolysis of p-nitrophenyl-alpha-D-mannopyranoside only slightly diminished at 0.3 mM
swainsonine
-
complete inhibition at 0.008 mM
swainsonine
-
50% inhibition in the range of 0.3-0.6 mM
swainsonine
-
competitive inhibition
swainsonine
-
competitive inhibition, Ki: 0.00036 mM
swainsonine
-
IC50: 10 nM
swainsonine
-
competitive
swainsonine
-
-
swainsonine
-
potent inhibition at 1 mM, 100% inhibition of the activity of the liver lysosomal fraction at pH 4.0, 95% at pH 6.5
swainsonine
-
IC50 is 400 nM
swainsonine
-
20% inhibition of glioblastoma cell growth at 0.25 mM
swainsonine
Q68EM8
concentration of 100 microM
swainsonine
-, Q6L2X5
shows competitive inhibition when p-nitrophenyl-Man is used as a substrate
swainsonine
-
complete inhibition
swainsonine
-
binding of swainsonine to the enzyme is stronger than bionding of 1-deoxymannojirimycin; competitive inhibitor, low binding up to 40C, increased binding at 50C
swainsonine
Q99YP5
binding structure, overview
swainsonine
-
-
swainsonine
-
the enzyme substituted with Zn2+ is considerably less sensitive to swainsonine compared with the Co2+-, Cd2+-, and Mn2+-substituted enzyme
Tris
-
inhibitory for alpha-mannosidases IA and IB
Zn2+
-
complete inhibition of the Co2+ activated enzyme at 0.5 mM
Zn2+
-
complete inhibition at 1 mM
Zn2+
-
strong inhibition at 1 mM
Zn2+
-
moderate inhibition at 1 mM
Zn2+
-
slight inhibition for alpha-mannosidase IA
Zn2+
-
55% inhibition at 10 mM
Zn2+
-
25% inhibition at 20 mM
Zn2+
-
inhibition at 1 mM
ZnCl2
-
92% inhibition by 1 mM, 56% inhibition by 0.01 mM
[[(3S,4S,5R,6R)-3,4,5-trihydroxy-6-(hydroxymethyl)piperidin-2-ylidene]amino] N-(4-chlorophenyl)carbamate
-
-
Mn2+
-
inhibition at 1 mM
additional information
-
no inhibition by 1-deoxymannojirimycin
-
additional information
-
no inhibition by (2R,3R,4S)-2-[(2-hydroxy-1-methyl-2,2-diphenyl-ethylamino)-methyl]-pyrrolidine-3,4-diol, and (2R,3R,4S)-2-(1,2-dihydroxy-ethyl)-pyrrolidine-3,4-diol
-
additional information
-
no inhibition by (2R,3R,4S)-2-[(2-hydroxy-1-methyl-2,2-diphenyl-ethylamino)-methyl]-pyrrolidine-3,4-diol, (2R,3R,4S)-2-(1,2-dihydroxy-ethyl)-pyrrolidine-3,4-diol, and (2R,3R,4S)-2-[2-(phenylamino)ethyl]pyrrolidine-3,4-diol
-
additional information
-
inhibition of growth of glioblastoma and melanoma cells by pyrrolidine-3,4-diol derivatives, overview
-
additional information
Q68EM8
down-regulation of Man2C1 activity by a small interfering RNA drastically change amount and structure of oligosaccharides accumulating in the cytosol, demonstrating that Man2C1 is involved in free oligosaccharide processing in the cytosol
-
additional information
-
inhibitory activity of thiosugar derivatives (thiolevomannosans) is tested against alpha-mannosidase
-
additional information
-, Q6L2X5
1-deoxymannojirimycin has no effect on ManA at concentrations up to 500 microM
-
additional information
-
not inhibitory: 1,5-D-mannoseptanosyl di- and trisaccharide ring-size isomers
-
additional information
-
activity is insensitive to 1-deoxymannojirimycin at concentration up to 2 mM. No change in the enzymatic activity is observed with 0.001-1 mM EDTA
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1-deoxymannojirimycin
-
hydrolysis of p-nitrophenyl-alpha-D-mannopyranoside, slight stimulation for enzyme I at 0.025 mM, enzyme II not affected
2-mercaptoethanol
-
slight activation up to 2.5 mM
2-mercaptoethanol
-
-
ATP
-
25% activation at 1 mM
Bovine serum albumin
-
35% activation at 0.125 mg/ml
-
Bovine serum albumin
-
-
-
CMP
-
25% activation at 1 mM
dithiothreitol
-
nearly 60% activation up to 2.5 mM
dithiothreitol
-
-
L-cysteine
-
slight stimulation at 1 or 10 mM
L-fucose
-
20% activation at 250 mM
lectin
-
Erythrina indica seed lectin (EiSL) 35% increase alpha-mannosidase in its activity, abolished in presence of lactose
-
Mannan
-
from yeast, 80% activation at 10 mg/ml
NaCl
-
increasing activity up to 1.6 M
NaCl
-
50% activation up to 1.5 M
NaN3
-
70% stimulation at 10 mM
phosphatidylcholine
-
10fold stimulation at 0.002%
phosphatidylethanolamine
-
8fold stimulation at 0.002%
swainsonine
-
hydrolysis of p-nitrophenyl-alpha-D-mannopyranoside, slight stimulation for enzyme I at 0.025 mM, enzyme II not affected
Triton X-100
-
increasing activity up to 0.1%
Triton X-100
-
optimal stimulation at 0.02%
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
5
-
2,4-dinitrophenyl alpha-D-mannoside
-
wild-type enzyme
25
-
2,4-dinitrophenyl-alpha-D-mannopyranoside
-
pH 5.0, 50C
0.57
-
2-O-alpha-D-mannopyranosyl-D-mannopyranose
-
-
2
-
2-O-alpha-D-mannopyranosyl-D-mannopyranose
-
-
27
-
3-O-alpha-D-mannopyranosyl-alpha-D-mannopyranose
Q99YP5
pH 6.8, 37C, recombinant enzyme
0.00731
-
4-methylumbelliferyl alpha-D-mannopyranoside
-
pH 6.5, 50C, 15 min, reaction stopped with Na2CO3
3.6
-
4-methylumbelliferyl alpha-D-mannopyranoside
Q99YP5
pH 6.8, 37C, recombinant enzyme
0.0073
-
4-methylumbelliferyl-alpha-D-mannopyranoside
-
pH 6.5, 50C
0.1
-
4-methylumbelliferyl-alpha-D-mannopyranoside
-
-
0.14
-
4-methylumbelliferyl-alpha-D-mannopyranoside
-
-
0.55
-
4-methylumbelliferyl-alpha-D-mannopyranoside
-
pH 5.0, 37C, HCEC cell layer
0.65
-
4-methylumbelliferyl-alpha-D-mannopyranoside
-
pH 5.0, 37C, LNZ-308 cell layer
1.065
-
4-methylumbelliferyl-alpha-D-mannopyranoside
-
pH 5.0, 37C, LN-18 cell layer
1.8
-
4-methylumbelliferyl-alpha-D-mannopyranoside
-
-
2.2
-
4-methylumbelliferyl-alpha-D-mannopyranoside
-
-
5.2
-
4-methylumbelliferyl-alpha-D-mannopyranoside
-
-
1.48
-
4-nitrophenyl alpha-D-mannopyranoside
-
pH 5.0, 37C
3.8
-
4-nitrophenyl alpha-D-mannopyranoside
-
-
0.11
-
4-nitrophenyl alpha-D-mannoside
-
pH 5.0, 70C, enzyme in complex with Co2+
0.39
-
4-nitrophenyl alpha-D-mannoside
-
pH 5.0, 70C, enzyme in complex with Mn2+
0.4
-
4-nitrophenyl alpha-D-mannoside
-
pH 6.5, 65C, recombinant enzyme
0.45
-
4-nitrophenyl alpha-D-mannoside
-
pH 6.5, 65C, native enzyme
0.65
-
4-nitrophenyl alpha-D-mannoside
-
pH 5.0, 70C, enzyme in complex with Zn2+
0.99
-
4-nitrophenyl alpha-D-mannoside
-
pH 5.0, 70C, enzyme in complex with Cd2+
1
-
4-nitrophenyl alpha-D-mannoside
-
pH 5.0, 70C, untreated enzyme which with no externally added metal ion in the incubation assay
0.0826
-
4-nitrophenyl-alpha-D-mannopyranoside
-
pH 6.5, 50C
0.08265
-
4-nitrophenyl-alpha-D-mannopyranoside
-
-
1.8
-
4-nitrophenyl-alpha-D-mannopyranoside
-
pH 5.0
1.6
-
4-nitrophenyl-alpha-D-mannoside
-
pH 6.0, 37C
0.2
-
5-fluoro-beta-L-gulosyl fluoride
-
wild-type enzyme
0.85
-
alpha-D-Man-(1->2)-D-Man
-
pH 5.0, 70C, enzyme in complex with Co2+
2.3
-
alpha-D-Man-(1->2)-D-Man
-
pH 5.0, 70C, enzyme in complex with Mn2+
1.16
-
alpha-D-Man-(1->3)-D-Man
-
pH 5.0, 70C, enzyme in complex with Co2+
-
2
-
alpha-D-Man-(1->4)-D-Man
-
pH 5.0, 70C, enzyme in complex with Mn2+
-
2.5
-
alpha-D-Man-(1->4)-D-Man
-
pH 5.0, 70C, enzyme in complex with Co2+
-
2
-
alpha-D-Man-(1->6)-D-Man
-
pH 5.0, 70C, enzyme in complex with Co2+
0.839
-
Man-alpha(1-3)Man
-
pH 6.5, 50C, 20 min
1.455
-
Man-alpha(1-6)Man
-
pH 6.5, 50C; pH 6.5, 50C, 20 min
1.13
-
Man3GlcNAc2
-
-
0.065
-
Man5GlcNAc
-
-
0.037
-
Man9GlcNAc
-
pH 7.0, 37C, Co2+-treated enzyme
0.11
-
Man9GlcNAc
-
-
0.46
-
Man9GlcNAc
-
pH 7.0, 37C, not treated with Co(II)
1.116
-
Manalpha(1-2)Man
-
pH 6.5, 50C
0.839
-
Manalpha(1-3)Man
-
pH 6.5, 50C
0.67
-
mannobiose
-
-
0.67
-
Mannotetraose
-
-
8.2
-
methyl-4-O-alpha-D-mannopyranosyl-D-mannopyranoside
-
-
0.048
-
p-nitrophenyl-alpha-D-mannopyranoside
-
-
0.05
-
p-nitrophenyl-alpha-D-mannopyranoside
-
-
0.072
-
p-nitrophenyl-alpha-D-mannopyranoside
-
Tris-eluted isoform from cobalt-chelating Sepharose
0.083
-
p-nitrophenyl-alpha-D-mannopyranoside
-
-
0.14
-
p-nitrophenyl-alpha-D-mannopyranoside
-
-
0.17
-
p-nitrophenyl-alpha-D-mannopyranoside
-
-
0.23
-
p-nitrophenyl-alpha-D-mannopyranoside
-
-
0.27
-
p-nitrophenyl-alpha-D-mannopyranoside
-
-
0.63
-
p-nitrophenyl-alpha-D-mannopyranoside
-
unbound isoform from cobalt-chelating Sepharose
0.91
-
p-nitrophenyl-alpha-D-mannopyranoside
-
-
1
-
p-nitrophenyl-alpha-D-mannopyranoside
-
-
1.2
-
p-nitrophenyl-alpha-D-mannopyranoside
-
-
1.4
-
p-nitrophenyl-alpha-D-mannopyranoside
-
-
1.8
-
p-nitrophenyl-alpha-D-mannopyranoside
-
alpha-mannosidase I
1.86
-
p-nitrophenyl-alpha-D-mannopyranoside
-
enzyme II
1.92
-
p-nitrophenyl-alpha-D-mannopyranoside
-
alpha-mannosidase A
2
-
p-nitrophenyl-alpha-D-mannopyranoside
-
fairly constant between pH 4.5-6.0
2
-
p-nitrophenyl-alpha-D-mannopyranoside
-
alpha-mannosidase II
2.04
-
p-nitrophenyl-alpha-D-mannopyranoside
-
enzyme I
2.3
-
p-nitrophenyl-alpha-D-mannopyranoside
-
-
2.3
-
p-nitrophenyl-alpha-D-mannopyranoside
-
-
2.3
-
p-nitrophenyl-alpha-D-mannopyranoside
-
-
2.4
-
p-nitrophenyl-alpha-D-mannopyranoside
-
-
2.7
-
p-nitrophenyl-alpha-D-mannopyranoside
-
isoforms II
2.7
-
p-nitrophenyl-alpha-D-mannopyranoside
-
alpha-mannosidase B
2.8
-
p-nitrophenyl-alpha-D-mannopyranoside
-
-
3.3
-
p-nitrophenyl-alpha-D-mannopyranoside
-
-
3.7
-
p-nitrophenyl-alpha-D-mannopyranoside
-
isoforms I
4.3
-
p-nitrophenyl-alpha-D-mannopyranoside
-
-
6.5
-
p-nitrophenyl-alpha-D-mannopyranoside
-
at pH 7.0
10
-
p-nitrophenyl-alpha-D-mannopyranoside
-
-
10.7
-
p-nitrophenyl-alpha-D-mannopyranoside
-
-
10.9
-
p-nitrophenyl-alpha-D-mannopyranoside
-
at pH 3.5
12.6
-
p-nitrophenyl-alpha-D-mannopyranoside
O09159
-
30
-
p-nitrophenyl-alpha-D-mannopyranoside
-
-
1.04
-
p-nitrophenyl-alpha-D-mannoside
-
-
0.42
-
phenyl-alpha-D-mannopyranoside
-
-
0.44
-
Manalpha(1-6)[Manalpha(1-3)]Manalpha(1-6)[Manalpha(1-)]Manbeta(1-4)GlcNAc
-
-
additional information
-
Mannan
-
value in mg/ml
0.34
-
methyl-alpha-D-mannopyranoside
-
-
additional information
-
additional information
-
the KM-value for 2-deoxy-2-fluoro-alpha-D-mannosyl fluoride is above 25 mM, wild-type enzyme
-
additional information
-
additional information
-
-
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.048
-
2,4-dinitrophenyl alpha-D-mannoside
-
mutant enzyme D341N
8.6
-
2,4-dinitrophenyl alpha-D-mannoside
-
wild-type enzyme
1.7
-
2,4-dinitrophenyl-alpha-D-mannopyranoside
-
pH 5.0, 50C
6.4
-
3-O-alpha-D-mannopyranosyl-alpha-D-mannopyranose
Q99YP5
pH 6.8, 37C, recombinant enzyme
0.03
-
4-methylumbelliferyl alpha-D-mannopyranoside
Q99YP5
pH 6.8, 37C, recombinant enzyme
44
-
4-nitrophenyl alpha-D-mannopyranoside
-
-
4.8
-
4-nitrophenyl alpha-D-mannoside
-
pH 5.0, 70C, enzyme in complex with Mn2+
10.5
-
4-nitrophenyl alpha-D-mannoside
-
pH 5.0, 70C, untreated enzyme which with no externally added metal ion in the incubation assay
12.5
-
4-nitrophenyl alpha-D-mannoside
-
pH 5.0, 70C, enzyme in complex with Co2+
13.6
-
4-nitrophenyl alpha-D-mannoside
-
pH 5.0, 70C, enzyme in complex with Zn2+
16.1
-
4-nitrophenyl alpha-D-mannoside
-
pH 5.0, 70C, enzyme in complex with Cd2+
21
-
4-nitrophenyl alpha-D-mannoside
-
pH 6.5, 65C, recombinant enzyme
158
-
4-nitrophenyl alpha-D-mannoside
-
pH 6.5, 65C, native enzyme
0.0051
-
5-fluoro-beta-L-gulosyl fluoride
-
wild-type enzyme
3.1
-
alpha-D-Man-(1->2)-D-Man
-
pH 5.0, 70C, enzyme in complex with Mn2+
5.5
-
alpha-D-Man-(1->2)-D-Man
-
pH 5.0, 70C, enzyme in complex with Co2+
4.9
-
alpha-D-Man-(1->3)-D-Man
-
pH 5.0, 70C, enzyme in complex with Co2+
-
1.9
-
alpha-D-Man-(1->4)-D-Man
-
pH 5.0, 70C, enzyme in complex with Mn2+
-
10.4
-
alpha-D-Man-(1->4)-D-Man
-
pH 5.0, 70C, enzyme in complex with Co2+
-
2
-
alpha-D-Man-(1->6)-D-Man
-
pH 5.0, 70C, enzyme in complex with Co2+
130
-
p-nitrophenyl-alpha-D-mannopyranoside
-
-
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.00216
-
2,4-dinitrophenyl alpha-D-mannopyranoside
-
pH 7.4, 25C
284164
0.00966
-
2,4-dinitrophenyl alpha-D-mannopyranoside
-
pH 7.4, 25C
284164
0.01
-
2,4-dinitrophenyl alpha-D-mannopyranoside
Q99YP5
pH 6.8, 37C, recombinant enzyme
284164
0.24
-
3-O-alpha-D-mannopyranosyl-alpha-D-mannopyranose
Q99YP5
pH 6.8, 37C, recombinant enzyme
293929
10.5
-
4-nitrophenyl alpha-D-mannoside
-
pH 5.0, 70C, untreated enzyme which with no externally added metal ion in the incubation assay
195542
12
-
4-nitrophenyl alpha-D-mannoside
-
pH 5.0, 70C, enzyme in complex with Mn2+
195542
16
-
4-nitrophenyl alpha-D-mannoside
-
pH 5.0, 70C, enzyme in complex with Cd2+
195542
21
-
4-nitrophenyl alpha-D-mannoside
-
pH 5.0, 70C, enzyme in complex with Zn2+
195542
54
-
4-nitrophenyl alpha-D-mannoside
-
pH 6.5, 65C, recombinant enzyme
195542
120
-
4-nitrophenyl alpha-D-mannoside
-
pH 5.0, 70C, enzyme in complex with Co2+
195542
351
-
4-nitrophenyl alpha-D-mannoside
-
pH 6.5, 65C, native enzyme
195542
0.206
-
alpha-D-Man-(1->2)-D-Man
-
pH 5.0, 70C, enzyme in complex with Zn2+
333434
0.277
-
alpha-D-Man-(1->2)-D-Man
-
pH 5.0, 70C, enzyme in complex with Cd2+
333434
1.3
-
alpha-D-Man-(1->2)-D-Man
-
pH 5.0, 70C, enzyme in complex with Mn2+
333434
6.4
-
alpha-D-Man-(1->2)-D-Man
-
pH 5.0, 70C, enzyme in complex with Co2+
333434
0.102
-
alpha-D-Man-(1->3)-D-Man
-
pH 5.0, 70C, enzyme in complex with Zn2+
0
0.185
-
alpha-D-Man-(1->3)-D-Man
-
pH 5.0, 70C, enzyme in complex with Mn2+
0
0.28
-
alpha-D-Man-(1->3)-D-Man
-
pH 5.0, 70C, enzyme in complex with Cd2+
0
4.2
-
alpha-D-Man-(1->3)-D-Man
-
pH 5.0, 70C, enzyme in complex with Co2+
0
0.106
-
alpha-D-Man-(1->4)-D-Man
-
pH 5.0, 70C, enzyme in complex with Zn2+
0
0.31
-
alpha-D-Man-(1->4)-D-Man
-
pH 5.0, 70C, enzyme in complex with Cd2+
0
0.95
-
alpha-D-Man-(1->4)-D-Man
-
pH 5.0, 70C, enzyme in complex with Mn2+
0
4.2
-
alpha-D-Man-(1->4)-D-Man
-
pH 5.0, 70C, enzyme in complex with Co2+
0
1
-
alpha-D-Man-(1->6)-D-Man
-
pH 5.0, 70C, enzyme in complex with Co2+
333437
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.000155
-
(1S,2R,8R,8aR)-octahydroindolizine-1,2,8-triol
-
37C, pH 5.5
0.053
-
(2R,3R,4S)-2-(aminomethyl)pyrrolidine-3,4-diol
-
35C
0.0023
-
(2R,3R,4S)-2-([(1R)-2,3-dihydro-1H-inden-1-ylamino]methyl)pyrrolidine-3,4-diol
-
37C
0.059
-
(2R,3R,4S)-2-([[(1R)-1-hydroxyethyl]amino]methyl)pyrrolidine-3,4-diol
-
35C
0.000135
-
(2R,3R,4S)-2-([[(1R)-2-hydroxy-1-phenylethyl]amino]methyl)pyrrolidine-3,4-diol
-
37C, pH 5.5
0.12
-
(2R,3R,4S)-2-([[(1S)-1-hydroxyethyl]amino]methyl)pyrrolidine-3,4-diol
-
35C
0.06
-
(2R,3R,4S)-2-phenylaminomethyl-pyrrolidine-3,4-diol
-
35C
0.071
-
(2R,3R,4S)-2-phenylaminomethyl-pyrrolidine-3,4-diol
-
35C
0.17
-
(2R,3R,4S)-2-[(1-phenyl-ethylamino)-methyl]-pyrrolidine-3,4-diol
-
35C
0.0074
-
(2R,3R,4S)-2-[(benzylamino)methyl]pyrrolidine-3,4-diol
-
37C
0.016
-
(2R,3R,4S)-2-[([(1R)-2-benzyloxy-1-phenylethyl]amino)methyl]pyrrolidine-3,4-diol
-
37C
0.000135
-
(2R,3R,4S)-2-[([(1R)-2-hydroxy-1-phenylethyl]amino)methyl]pyrrolidine-3,4-diol
-
37C
0.0074
-
(2R,3R,4S)-2-[[(2H-Imidazol-1-ylmethyl)-amino]-methyl]-pyrrolidine-3,4-diol
-
35C
0.026
-
(2R,3R,4S)-2-[[(thiophen-2-ylmethyl)-amino]-methyl]-pyrrolidine-3,4-diol
-
35C
0.098
-
(2R,3R,4S)-2-[[(thiophen-2-ylmethyl)-amino]-methyl]-pyrrolidine-3,4-diol
-
35C
0.0012
-
(2R,3R,4S,5R)-2-[(benzylamino)methyl]-5-(hydroxymethyl)pyrrolidine-3,4-diol
-
37C
0.00135
-
(2R,3S,4R,5R)-2-(hydroxymethyl)-5-[([(1R)-2-hydroxy-1,2-diphenylethyl]amino)methyl]pyrrolidine-3,4-diol
-
37C
0.024
-
(2S)-2-[([(2R,3S,4S)-3,4-dihydroxypyrrolidin-2-yl]methyl)amino]-2-phenylethyl 2-fluorobenzoate
-
37C
0.019
-
(2S)-2-[([(2R,3S,4S)-3,4-dihydroxypyrrolidin-2-yl]methyl)amino]-2-phenylethyl 4-fluorobenzoate
-
37C
0.000206
-
(3R,4R,5R)-3,4-dihydroxy-5-([[(1R)-2-hydroxy-1-phenylethyl]amino]methyl)-1-methylpyrrolidin-2-one
-
37C, pH 5.5
0.004
-
(3R,4R,5R)-3,4-dihydroxy-5-([[(1R)-2-hydroxy-1-phenylethyl]amino]methyl)pyrrolidin-2-one
-
37C, pH 5.5
0.000385
-
1,6-dideoxy-1,6-episulfinyl-beta-D-mannose
-
-
0.00035
-
1,6-dideoxy-1,6-episulfonyl-beta-D-mannose
-
best inhibitor of alpha-mannosidase
0.00138
-
1,6-dideoxy-1,6-epithio-beta-D-mannose
-
-
0.286
-
1-deoxymannojirimycin
-
low binding up to 40C, increased binding at 50C; pH 6.5, 50C
0.75
-
1-deoxymannojirimycin
-
pH 5.5, liver lysosomal fraction
0.08
-
2-(2,2-dihydroxy-ethyl)-pyrrolidine-3,4-diol
-
35C
2.8
-
2-amino-2-deoxy-D-glucose
-
-
7.5
-
2-deoxy-2-fluoro-alpha-D-mannosyl fluoride
-
-
0.6
-
5-fluoro-beta-L-gulosyl fluoride
-
-
0.02
-
8,8a-di-epi-swainsonine
-
liver lysosomal fraction
0.75
-
8a-epi-swainsonine
-
liver lysosomal fraction
4
-
alpha-1,2-mannopyranosyl-mannopyranose
-
-
-
18
-
alpha-1,3-mannopyranosyl-mannopyranose
-
-
-
100
-
alpha-1,6-mannopyranosyl-mannopyranose
-
-
23.8
-
D-mannono- 1,4 -lactone
-
-
0.13
-
deoxymannojirimycin
-
pH 5.0, 50C
0.4
-
deoxymannojirimycin
-
-
0.046
-
gluco-hydroxyiminolactam
-
pH 5.6
0.07
-
glucoimidazole
-
pH 5.6
0.02
-
mannoimidazole
-
pH 5.6
0.6
-
methyl-alpha-D-lyxopyranosyl-(1'-2)-alpha-D-mannopyranoside
-
pH 5.0, 50C
0.033
-
N-octyl-6-epi-valienamine
-
pH 5.6
0.00024
-
swainsonine
-
-
0.0003
-
swainsonine
-
pH 5.6
0.00068
-
swainsonine
-
-
0.00122
-
swainsonine
-, Q6L2X5
-
0.018
-
swainsonine
Q99YP5
pH 6.8, 37C
0.101
-
swainsonine
-
low binding up to 40C, increased binding at 50C; pH 6.5, 50C
0.3
0.6
swainsonine
-
-
0.15
-
[[(3S,4S,5R,6R)-3,4,5-trihydroxy-6-(hydroxymethyl)piperidin-2-ylidene]amino] N-(4-chlorophenyl)carbamate
-
pH 5.6
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.00001
-
(1S,2R,8R,8aR)-octahydroindolizine-1,2,8-triol
-
pH 5.0, 37C, HCEC cell layer
0.00002
-
(1S,2R,8R,8aR)-octahydroindolizine-1,2,8-triol
-
pH 5.0, 37C, LNZ-308 cell layer
0.00005
-
(1S,2R,8R,8aR)-octahydroindolizine-1,2,8-triol
-
pH 5.0, 37C, LN-18 cell layer
0.017
-
(2R,3R,4S)-2-([(1R)-2,3-dihydro-1H-inden-1-ylamino]methyl)pyrrolidine-3,4-diol
-
IC50 is 0.017 mM
0.025
-
(2R,3R,4S)-2-([[(1R)-2-hydroxy-1-phenylethyl]amino]methyl)pyrrolidine-3,4-diol
-
pH 5.0, 37C, HCEC cell layer
0.05
-
(2R,3R,4S)-2-([[(1R)-2-hydroxy-1-phenylethyl]amino]methyl)pyrrolidine-3,4-diol
-
pH 5.0, 37C, LN-18 cell layer; pH 5.0, 37C, LNZ-308 cell layer
0.06
-
(2R,3R,4S)-2-[(benzylamino)methyl]pyrrolidine-3,4-diol
-
IC50 is 0.06 mM
0.058
-
(2R,3R,4S)-2-[([(1R)-2-benzyloxy-1-phenylethyl]amino)methyl]pyrrolidine-3,4-diol
-
92% inhibition at 1 mM, IC50 is 0.058 mM
0.0007
-
(2R,3R,4S)-2-[([(1R)-2-hydroxy-1-phenylethyl]amino)methyl]pyrrolidine-3,4-diol
-
complete and selective inhibition at 1 mM, IC50 is 700 nM
0.11
-
(2R,3R,4S)-2-[([(1R,2S)-2-hydroxy-1,2-diphenylethyl]amino)methyl]pyrrolidine-3,4-diol
-
88% inhibition at 1 mM, IC50 is 0.11 mM
0.1
-
(2R,3R,4S)-2-[([(1S)-2-hydroxy-1-phenylethyl]amino)methyl]pyrrolidine-3,4-diol
-
92% inhibition at 1 mM, IC50 is 0.1 mM
0.128
-
(2R,3R,4S)-2-[([(1S,2R)-2-hydroxy-1,2-diphenylethyl]amino)methyl]pyrrolidine-3,4-diol
-
84% inhibition at 1 mM, IC50 is 0.128 mM
0.0062
-
(2R,3R,4S,5R)-2-[(benzylamino)methyl]-5-(hydroxymethyl)pyrrolidine-3,4-diol
-
IC50 is 0.0062 mM
0.0042
-
(2R,3S,4R,5R)-2-(hydroxymethyl)-5-[([(1R)-2-hydroxy-1,2-diphenylethyl]amino)methyl]pyrrolidine-3,4-diol
-
98% inhibition at 1 mM, IC50 is 0.0042 mM
0.063
-
(2S)-2-[([(2R,3S,4S)-3,4-dihydroxypyrrolidin-2-yl]methyl)amino]-2-phenylethyl 2-fluorobenzoate
-
83% inhibition at 1 mM, IC50 is 0.063 mM
0.06
-
(2S)-2-[([(2R,3S,4S)-3,4-dihydroxypyrrolidin-2-yl]methyl)amino]-2-phenylethyl 4-fluorobenzoate
-
92% inhibition at 1 mM, IC50 is 0.060 mM
0.0005
-
(3R,4R,5R)-3,4-dihydroxy-5-([[(1R)-2-hydroxy-1-phenylethyl]amino]methyl)-1-methylpyrrolidin-2-one
-
pH 5.0, 37C, HCEC cell layer; pH 5.0, 37C, LNZ-308 cell layer
0.002
-
(3R,4R,5R)-3,4-dihydroxy-5-([[(1R)-2-hydroxy-1-phenylethyl]amino]methyl)-1-methylpyrrolidin-2-one
-
pH 5.0, 37C, LN-18 cell layer
0.05
-
(3R,4R,5R)-3,4-dihydroxy-5-([[(1R)-2-hydroxy-1-phenylethyl]amino]methyl)pyrrolidin-2-one
-
pH 5.0, 37C, LNZ-308 cell layer
0.075
-
(3R,4R,5R)-3,4-dihydroxy-5-([[(1R)-2-hydroxy-1-phenylethyl]amino]methyl)pyrrolidin-2-one
-
pH 5.0, 37C, HCEC cell layer
0.35
-
(3R,4R,5R)-3,4-dihydroxy-5-([[(1R)-2-hydroxy-1-phenylethyl]amino]methyl)pyrrolidin-2-one
-
pH 5.0, 37C, LN-18 cell layer
0.01
-
1-deoxymannojirimicin
-
IC50 = 0.01 mM
0.284
-
1-deoxymannojirimycin
-
low binding up to 40C, increased binding at 50C
0.089
-
3-bromo-N-[(2S)-2-[([(2R,3S,4R)-3,4-dihydroxypyrrolidin-2-yl]methyl)amino]-2-phenylethyl]benzamide
-
95% inhibition at 1 mM, IC50 is 0.089 mM
0.00001
-
swainsonine
-
IC50: 10 nM
0.00011
-
swainsonine
-
IC50: 0.00011 mM
0.00015
-
swainsonine
O09159
IC50: 0.00015 mM
0.0004
-
swainsonine
-
IC50 is 400 nM
0.11
-
swainsonine
-
low binding up to 40C, increased binding at 50C
0.2
-
swainsonine
-
pH 6.5, 65C
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.01
-
-
in leaf and root
0.0175
-
-
-
0.02
-
-
in embryonic axis
0.05
-
-
-
0.057
-
-
-
0.07
-
-
enzyme I with 4-methylumbelliferyl-mannopyranoside as substrate
0.09
-
-
enzyme II with 4-methylumbelliferyl-mannopyranoside as substrate
0.11
-
-
with p-nitrophenyl-alpha-D-mannopyranoside as substrate
0.29
-
-
-
0.36
-
-
-
0.45
-
-
in cotyledon
1.86
-
O09159
-
1.93
-
-
alpha-mannosidase B
2.42
-
-
for Tris-eluted isoform
2.5
-
-
alpha-mannosidase A
4.2
-
-
purified recombinant TM1851
4.6
-
-
alpha-mannosidase B
6.6
-
-, Q6L2X5
ManA is equally active with mannobiose substrates, released mannose is quantified, resulting in a specific activity of approximately 6.6 U/mg
11.9
-
-
-
14.4
-
-
substrate: 4-nitrophenyl alpha-D-mannoside, pH 6.5, 65C
15.94
-
-
alpha-mannosidase A
16.27
-
-
-
20.52
-
-
-
21.1
-
-
-
45
-
-
in the presence of Zn2+
48.5
-
-
-
110.2
-
-
-
129.2
-
-
isoforms III
153
-
-
-
182
-
-
isoforms II
199.9
-
-
isoforms I
2200
-
-
with 4-methylumbelliferyl-alpha-D-mannopyranoside as substrate
additional information
-
-
assay described, enzyme activity measured in homogenates of 10 to 15 male and female flies before and after sucrose meals, monitoring by spectroscopy, values of relative activity shown, enzyme activity of female colonies of the Jordan Valley autumn (arid) differs significantly from those of colonies of Neot Hakikar (oasis) and Kfar Adumim starved (arid)
additional information
-
-
effects of all trans retinoic acid treatment of HL-60 on enzymatic activity of glycohydrolases tested
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4
4.5
-
enzyme from lysosomal fraction
4
4.5
-
lysosomal or acid mannosidases. Neutral optimum pH for endoplasmic reticulum-associated mannosidases
4
-
-
alpha-mannosidase A
4.2
-
O09159
isoforms A and B
4.3
4.5
-
reaction with p-nitrophenyl-alpha-mannoside
4.4
4.6
-
-
4.5
-
O09159
-
4.5
-
-
-
4.5
-
-
assay at
4.6
-
-
-
4.6
-
-
alpha-mannosidase B
4.6
-
-
-
5
-
-
substrate 4-nitrophenyl-alpha-D-mannopyranoside
5
-
-
acetate buffer
5.2
-
-, Q6L2X5
maximum activity of ManA
5.5
5.9
-
-
5.5
6
-
-
5.5
6
-
-
5.5
6
-
enzyme from Golgi compartment
5.5
6
-
Golgi compartment mannosidases. Neutral optimum pH for endoplasmic reticulum-associated mannosidases
5.5
-
-
alpha-mannosidase II with p-nitrophenyl-alpha-D-mannopyranoside as substrate
5.5
-
-
-
5.5
-
-
double-peaked pH profile
5.5
-
-
-
5.7
-
-
assay at, pH-optimum estimated for
5.8
-
-
in acetate buffer
5.8
-
-
alpha-mannosidase II with Man8GlcNAc as substrate
6
6.4
-
-
6
-
-
enzymes I and II
6
-
-
-
6
-
-
alpha-mannosidases IA and IB with Man8GlcNAc as substrate
6
-
-
substrate Man8GlcNAc2-pyridylaminoside
6
-
-
assay at
6.1
6.5
-
-
6.2
6.5
-
-
6.4
6.8
-
both isoforms, unbound and Tris-eluted fractions from cobalt-chelating Sepharose
6.4
6.8
-
double-peaked pH profile
6.5
-
-
-
6.5
-
-
assay at
6.8
-
-
-
6.8
-
Q99YP5
assay at
7
-
-
-
7
-
-
enzyme from endoplasmic reticulum
additional information
-
-
alpha-D-mannosidase exists in multiple forms and can be classified on the basis of their optimum pH, into three groups
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
3
8
-
fluorescence studies over a pH range show tryptophan in highly hydrophobic environment, pH change does not change the tryptophan environment
4.3
6
O09159
-
4.3
6
-
-
5
8
-
pH 5.0: about 80% of maximal activity, pH 8.0: about 50% of maximal activity
5.6
-
-
half maximal activity
5.7
6.7
-
pH 5.7: about 35% of maximal activity, pH 6.5-6.7: optimum
6
6.8
-
activity falls rapid below and above
8
-
-
23% of maximum activity
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
-
-
assay with 2,4-dinitrophenyl alpha-D-mannopyranoside
37
-
-
assay at
37
-
Q99YP5
assay at
37
-
-
assay at
37
-
-
assay at
42
-
-
enzymes I and II
55
-
-
optimal activity
70
-
-, Q6L2X5
maximum activity of ManA
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
50
-
15 min
30
65
-
To determine the energy of activation of alpha-mannosidase (23 kJ/mol), Vmax is determined at various temperatures
60
90
-
60C: about 50% of maximal activity, 80C: optimum, 90C: about 20% of maximal activity
65
-
-
up to, pH 5.0
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
catalytically active soluble domain, released from endogenous proteases
Manually annotated by BRENDA team
-
TAKA diastase, crude enzyme preparation
Manually annotated by BRENDA team
-
Rhozyme HP-150, crude enzyme preparation
Manually annotated by BRENDA team
-
3 isoforms, I, II and III
Manually annotated by BRENDA team
-
alpha-mannosidases A and B
Manually annotated by BRENDA team
-
cauda epididymis
Manually annotated by BRENDA team
O09159
only isoform B present
Manually annotated by BRENDA team
-
cauda epididymis
Manually annotated by BRENDA team
-
highest specific activities of both alpha-and beta-mannosidases
Manually annotated by BRENDA team
-
activity 200fold lower than in white blood cells
Manually annotated by BRENDA team
-
In normal granulocytes, specific enzymatic activities for both glycohydrolases (beta-D-hexosaminidase (EC 3.2.1.52) and alpha-D-mannosidase) are significantly lower in comparison with untreated HL-60 cells
Manually annotated by BRENDA team
-
human promyelocytic leukemia HL-60 cells
Manually annotated by BRENDA team
-
three isoforms I, II and III
Manually annotated by BRENDA team
-
immunological distinct form from enzyme in seed, root, cotyledon and embryonic axis
Manually annotated by BRENDA team
O09159
only isoform B present
Manually annotated by BRENDA team
O09159
cDNA library
Manually annotated by BRENDA team
-
2 isoforms, unbound and Tris-eluted fractions from cobalt-chelating Sepharose
Manually annotated by BRENDA team
-
isolation of the catalytic domain by chymotrypsin digestion
Manually annotated by BRENDA team
-
cDNA library
Manually annotated by BRENDA team
-
lysosomal type
Manually annotated by BRENDA team
-
4 forms of intermediate alpha-mannosidases
Manually annotated by BRENDA team
-
of patients with amyotrophic lateral sclerosis
Manually annotated by BRENDA team
-
maximum induction of enzyme synthesis by culturing in media containing yeast mannan and a nitrogen source
Manually annotated by BRENDA team
-
whole fly homogenates
Manually annotated by BRENDA team
additional information
-
enzymic activities decrease significantly during the postbreeding resting season compared to the breeding season
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
isoforms III present
Manually annotated by BRENDA team
Q68EM8
examination of subcellular localization of Man2C1, using FLAG-tagging at the N-terminus for detection
Manually annotated by BRENDA team
-
ER alpha-mannosidase I
Manually annotated by BRENDA team
-
3 isoforms, alpha-mannosidases IA, IB and II
Manually annotated by BRENDA team
-
Golgi alpha-mannosidase IA
Manually annotated by BRENDA team
-
alpha-D-mannosidase exists in multiple forms, which are detectable in most human tissues
Manually annotated by BRENDA team
-
luminal fluid
Manually annotated by BRENDA team
-
luminal fluid
Manually annotated by BRENDA team
Q99YP5
SpGH38 may be intracellular, absence of any classical signal peptide
Manually annotated by BRENDA team
-
alpha-D-mannosidase exists in multiple forms, which are detectable in most human tissues
Manually annotated by BRENDA team
-
from microsomal membranes
Manually annotated by BRENDA team
-
from microsomal membranes
Manually annotated by BRENDA team
-
bound to vacuolar tonoplast
Manually annotated by BRENDA team
-
from Golgi-enriched membrane fraction
Manually annotated by BRENDA team
-
isoforms I and II present
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30000
32000
-
gel filtration, sedimentation equilibrium centrifugation
42000
-
-
SDS-PAGE, non-denaturating electrophoresis
45000
-
-
SDS-PAGE
49000
-
-
gel filtration
51000
-
-
gel filtration
53000
-
-
SDS-PAGE
54300
-
-
enzyme I, SDS-PAGE
60000
68000
-
gel filtration
70000
-
-
SDS-PAGE
75000
-
-
gel filtration
93300
-
-
enzyme II, SDS-PAGE
113000
-
-
Tris-eluted isoform from cobalt-chelating Sepharose, gel filtration
116000
-
-
predicted from cDNA
120000
-
O00754
LAMAN 120 kDa precursor detected in wild type and mutant constructs. Western blot analysis
120000
-
-, Q6L2X5
small fraction of ManA activity, reflecting single subunits
150000
-
-
gel filtration
185000
200000
-
chymotrypsin-cleaved catalytic subunit, non-reducing SDS-PAGE, gel filtration
188000
197000
-
gel filtration, sucrose density gradient centrifugation
200000
-
-
gel filtration, sucrose density gradient centrifugation
217000
-
-
gel filtration
220000
-
-
gel filtration
220000
-
-
gel filtration
220000
-
-
gel electrophoresis, sedimentation equilibrium analysis
220000
-
-, Q6L2X5
gel filtration
230000
-
-
gel filtration, SDS-PAGE
230000
-
-
gel filtration
230000
-
-
gel filtration
230000
-
-
gel filtration
230000
-
-
gel filtration
240000
-
-
gel filtration
260000
-
-
gel filtration, isoforms I and II
260000
-
-
alpha-mannosidase B
270000
-
O09159
isoform B, gel filtration
270000
-
-
gel filtration
275000
-
-
gel filtration, non-reducing SDS-PAGE
275000
-
-
gel filtration
280000
-
-
gel filtration, alpha-mannosidase A
285000
-
-
gel filtration
290000
-
O09159
isoform A, gel filtration
290000
-
-
gel filtration, discrepancy in molecular mass due to glycoproteic nature
295000
-
-
gel filtration
300000
-
-
gel filtration, alpha-mannosidases A and B
300000
-
-
gel filtration
335000
-
-
gel filtration
359000
-
-
gel filtration
363000
-
-
gel filtration
372000
420000
-
sucrose density gradient centrifugation, gel filtration
412000
-
-
gel filtration
417000
-
-
gel filtration
450000
-
-
gel filtration
460000
-
-
gel filtration
480000
-
-
gel filtration
500000
-
-
non-denaturating PAGE
560000
-
-
gel filtration
670000
-
O09159
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
dimer
-
2 * 100000, reducing SDS-PAGE, catalytic subunit; 2 * 124000, SDS-PAGE
dimer
-
1 * 44000 + 1 * 23000, reducing SDS-PAGE
dimer
-
2 * 110000, reducing and non-reducing SDS-PAGE
dimer
-
denaturating gel electrophoresis, electron microscopy analysis
dimer
-
2 * 110000, SDS-PAGE
dimer
-, Q6L2X5
2 * 111500, gel filtration
dimer
-
2 * 116000, SDS-PAGE
hexamer
-
6 * 69200, SDS-PAGE
hexamer
-
alpha3beta3, 3 * 62000 + 3 * 26000, SDS-PAGE, alpha-mannosidase A
monomer
-
1 * 54300, SDS-PAGE, enzyme I, 1 * 93300, SDS-PAGE, enzyme II
monomer
-
1 * 53000, crystallographic analysis
monomer
-
1 * 113000, gel filtration, SDS-PAGE
monomer
-
1 * 30000-32000, SDS-PAGE
monomer
-
1 * 42000, SDS-PAGE
oligomer
-
composed of one to six 107, 73 and 31 kDa subunits
oligomer
-
composed of 60 and 31 kDa subunits
oligomer
-
composed of equal amounts of 62, 58 and 26 kDa subunits
oligomer
-
-
tetramer
-
alpha2, 2 * 63000, beta2, 2 * 51000, reducing SDS-PAGE
tetramer
-
heterotetramer composed of 57000 + 46000 subunits, SDS-PAGE, endo H deglycosylation
tetramer
-
4 * 110000, SDS-PAGE
tetramer
-
4 * 115000, SDS-PAGE
tetramer
-
4 * 58000, SDS-PAGE
tetramer
-
alpha2, 2 * 44000, beta2, 2 * 66000, SDS-PAGE
tetramer
-
4 * 70000, SDS-PAGE
tetramer
-
1 * 75000 + 1 * 60000 + 1 * 50000 + 1 * 45000, SDS-PAGE
tetramer
-
4 * 75000, denaturating electrophoresis
tetramer
-
2 * 66000 + 2 * 44000, SDS-PAGE
tetramer
-
4 * 110000, SDS-PAGE
tetramer
-
2 * 70000, L-subunit, + 2 * 47000, S-subunit, SDS-PAGE
trimer
-
3 * 110000, SDS-PAGE
trimer
-
3 * 110000, SDS-PAGE
-
monomer
-
1 * 43000, SDS-PAGE
additional information
-
SDS-PAGE reveals a major protein of 150000 Da and a minor protein with a MW of 130000 Da
additional information
-
structure analysis, the enzyme has an (alphaalpha)7 barrel structure with a coordinating Ca2+ ion, overview
additional information
Q99YP5
structure comparisons, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
glycoprotein
-
3.8% neutral sugar content
glycoprotein
-
the enzyme contains 8 N-glycosylation sites, e.g. at residues 133, 367, 497, 692, 766, and 930, site-specific glycosylation analysis, high mannose and complex type N-glycans, overview, the N497 glycosylation is very important for maintenance of lysosomal stability of the enzyme
glycoprotein
-
6% carbohydrate content for the 66 kDa subunit, smaller subunit not glycosylated
glycoprotein
-
-
glycoprotein
-
-
glycoprotein
-
-
glycoprotein
-
-
glycoprotein
-
partial site-specific glycosylation analysis, paucimannosidic type N-glycan
glycoprotein
O09159
isoforms A and B different in sialic acid content
glycoprotein
-
alpha-mannosidaseI contains mannose and glucose, alpha-mannosidase II mannose, galactose and glucose
glycoprotein
-
-
glycoprotein
-
contains mainly N-linked oligosaccharides, small amounts of fucose, galactose, glucose
glycoprotein
-
15% carbohydrate content, mannose, glucose, galactose major components
glycoprotein
-
8% mannose, 3.3% glucosamine
glycoprotein
-
sugar content, w/w: 20.1% glucose, 3.09% mannose, 1.7% galactose, less than 1%N-acetyl-D-glucosamine, minor component: sialic acid
glycoprotein
-
presence of N-glycans
glycoprotein
-
only N-linked high-mannose-type oligosaccharides
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
crystal structure at 2.7 A resolution
Q29451
X-ray crystal structures obtained in apo-, inhibitor-bound, and substrate-bound forms provide both mechanistic and molecular insight into how the proteins, which adopts an (alpha/alpha)6fold, recognizes and hydrolyzes the alpha1,6-mannosidic bond by an inverting, metal-independent catalytic mechanism
-
hanging drop vapour diffusion method, crystallization of wild-type enzyme in complex with 5-fluoro-beta-L-gulosyl fluoride, mutant enzyme D341N in complex with 2-deoxy-2-fluoro-alpgha-D-mannosyl fluoride and mutant enzyme D341N in complex with 5-fluoro-beta-L-gulosyl fluoride
-
in complex with inhibitors mannoimidazole, glucoimidazole, N-octyl-6-epi-valienamine, gluco-hydroxyiminolactam, and [[(3S,4S,5R,6R)-3,4,5-trihydroxy-6-(hydroxymethyl)piperidin-2-ylidene]amino] N-(4-chlorophenyl)carbamate
-
vapor diffusion and micro-batch crystallization techniques, crystal structure in absence and presence of the anti-cancer agent swainsonine and the inhibitor deoxymannojirimycin
-
structual 3D analysis
O00754
30 mg/ml purified recombinant Golgi alpha-mannosidase IA in 20 mM MES, pH 6.5, 150 mM NaCl, 5 mM CaCl2, and 0.75 M NDSB-201, crystallization of free enzyme by microbatch method using a precipitation solution containing 15-20% PEG 4000 at pH 4.5-6.5, cocrystallization of 1-deoxymannojirimycin bound to the enzyme by hanging drop vapour diffusion method at 37C, 0.001 ml of a solution containing 200 mM 1-deoxymannojirimycin is mixed with an equal volume of crystallization solution containing 100 mM MES and 100 mM Tris-HCl, pH 6.0, and 25-35% PEG 4000, 2 days at 18C, X-ray diffraction structure determination and analysis at 1.5 A resolution, structure modelling
-
crystal structure at 2.8 A resolution
-
purified recombinent enzyme free or in complex with the inhibitor swainsonine, sitting drop vapour diffusion method, mixing of 12 mg/ml protein in 100 mM Tris, pH 8.5, 1.5 M (NH4)2SO4 and 12% v/v glycerol, with reservoir solution, containing 3% v/v glycerol, 54% v/v Tacsimate, pH 7.0, and 2% v/v PEG 6000, also acting as the cryo-protectant, crystals of the swainsonine complex form are obtained by soaking SpGH38 crystals for ,16 h in mother liquor supplemented with 2 mM swainsonine, X-ray diffraction structure determination and analysis at 1.9 A and 2.6 A resolution, respectively
Q99YP5
purified recombinant TM1851, sitting drop vapour diffusion method, optimal conditions: 0.001 ml of protein solution containing 5.3 mg/ml protein in 5 mM sodium phosphate and 150 mM NaCl, pH 6.8, mixed with an equal volume of reservoir solution containing 4% w/v PEG 6000, 50 mM sodium phosphate, pH 6.0, and 0.5 M NaCl, 1 day at 25C, X-ray diffraction structure determination and preliminary analysis at 2.9 A resolution
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
3
-
-
40% remaining activity
3.3
5.5
-
50% activity at pH 3.3 and pH 5.5
3.8
5.5
-
50% activity at pH 3.8 and pH 5.5
4.5
6
-
stable for 6 months at 4C
4.5
6.5
-
completely stable at 75C for 24 h, slightly less stable in buffers at pH 4.5
4.5
-
-
45% remaining activity
4.8
8
-
stable for 5 h at 20C
5
7
-
stable within
5
8
-
stable within
5.5
-
-
activity lowered by 22%
6
-
-
stable for 1 h, 40% and 20% loss of activity at pH 4.0 and pH 8.0
6
-
-
90% activity after 60 min at 37C
6
-
-
unstable below
6
-
-
activity is abolished above pH 6.0
6.3
6.8
-
most stable within
6.5
10
-
stable within at 5C
6.8
-
-
activity lowered by 27%
7
7.5
-
30-64% remaining activity
7
9
-
stable within
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
-20
-
-
no loss of activity within 3 months
0
4
-
60-70% loss of activity within 24 h
10
45
-
stable within
24
-
-
activity constant for 1 h
25
-
-
stable for 16 h
30
50
-
fully stable, no inactivation, no denaturation
35
-
-
half maximal activity
37
-
-
10% loss of activity after 2.5 h
40
-
-
increasing activity up to
44
-
-
stable for 5 min
50
-
-
stable for 30 min at pH 6.0
50
-
-
10% loss of activity after 1 h
50
-
-
complete loss of activity after 15 min
55
-
-
half maximal activity
60
-
O09159
stable up to 1 h
60
-
-
stable for 24 h in 0% mannose, stability at 20C higher in 85% mannose
60
-
-
fully inactivated in 5 min
60
-
-
thermal activation up to
60
-
-
10-20% loss of activity for acid alpha-mannosidase, 60-80% inhibition for neutral alpha-mannosidases
60
-
-
40% loss of activity after 5 min
60
-
-
stable within 15 min
60
-
-
stable for 1 h
75
-
-
continual increase of activity up to
80
-
-, Q6L2X5
resistance of ManA to heat inactivation (at 80C)
80
-
-
half-life: 1.5 min
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
25-30% of activity remains in 6 M urea
-
albumin protects activity
-
stable in the presence of Co2+ at 37C
-
stable in the presence of Co2+ at 37C
-
albumin protects activity
-
extremely labile, stabilized by the presence of 20% glycerol, v/v, 5 mM CoCl2, protease inhibitors
-
stable in the presence of Co2+ at 37C
-
increasing thermostability in the presence of 0.1-1 mM CaCl2
-
presence of CHAPS necessary for maximum activity
-
glutathione S-transferase/mannosidase III fusion protein is inactivated by freezing
-
addition of Zn2+ stabilizes activity
-
very stable if solution is kept frozen
-
quite stable in buffer containing 10% glycerol, v/v
-
OXIDATION STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
2-mercaptoethanol required during purification
-
136007
dithiothreitol stabilizes
-
136017
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-10C, several weeks
-
4C or -20C, 4 months
-
4C, 25 mM sodium phosphate, pH 7.0, 9 months
-
0-4C, pH 6.0, several weeks
-
4C, 10 mM sodium acetate, pH 6.0, high protein concentration, 1 month
-
-20C, 0.2 mg protein/ml, 1 year
-
5C, 50% loss of activity after 3 weeks
-
4C, glutathione S-transferase/mannosidase III fusion protein is stable for at least 1 week
-
-20C, pH 6.0, 50% glycerol, 3 months
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
to homogeneity, chromatography steps
-
further purification of TAKA-diastase, to homogeneity
-
to homogeneity, one step affinity chromatography
-
to homogeneity, chromatography steps
-
to homogeneity, preparative PAGE
-
to homogeneity, chromatography steps
-
to homogeneity, chromatography steps, isoelectric focusing
-
purification procedure consists of ammonium sulfate precipitation, anion exchange, ConA lectin affinity and gel filtration chromatography
-
to homogeneity, chromatography steps
-
using Ni-NTA chromatography
-
from Erythrina indica seeds by gel filtration and affinity chromatography
-
to homogeneity, chromatography steps
-
to homogeneity, chromatography steps, chromatofocusing
-
FLAGtagged Man2C1 from cytosolic fraction of HEK-293 cells, analysed by silver staining
Q68EM8
recombinant protein, to homogeneity
-
to homogeneity, chromatography steps
-
ammonium sulfate precipitation, anion exchange, galactose Sepharose, phenyl Sepharose, gel permeation and Con A Sepharose chromatography
-
to homogeneity, chromatography steps
-
near homogeneity, preincubation with Co2+, metal chelating affinity chromatography
-
separation of neutral mannosidase from acid mannosidase by 1step Co-chelate affinity chromatography
-
to homogeneity, chromatography steps, preparative electrophoresis
-
recombinant protein, immobilized on IgG Sepharose
-
recombinant protein, to homogeneity
-
recombinant yeast alpha-factor signal sequence-fusion enzyme from Pichia pastoris strain GS115 by ion exchange and hydrophobic interaction chromatography, eluent is ammonium sulfate, and gel filtration
-
to homogeneity, chromatography steps
O09159
near homogeneity, chromatography steps
-
to homogeneity, immunoabsorbent chromatography
-
SDS-PAGE, anion-exchange, size exclusion chromatography
-, Q6L2X5
catalytic subunit, to homogeneity
-
near homogeneitiy
-
near homogeneity, doesn't bind to ConA-Sepharose
-
to homogeneity, chromatography steps
-
to homogeneity, chromatography steps, cobalt-chelating Sepharose
-
to homogeneity, chromatography steps, isoelectric focusing
-
to homogeneity, chromatography steps
-
from amture red fruit
-
using Ni-NTA chromatography
-
glutathione S-transferase/mannosidase III fusion protein
-
using Ni-NTA chromatography
-
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
Q99YP5
to homogeneity, chromatography steps
-
to homogeneity, chromatography steps
-
recombinant TM1851 from Escherichia coli by ion exchange and hydroxyapatite chromatography, and gel filtration
-
to homogeneity, chromatography steps, affinity chromatography
-
recombinant protein, to homogeneity
-
to homogeneity, chromatography steps
-
near homogeneity, chromatography steps
-
partial, affinity chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expressed in Escherichia coli as a His-tagged fusion protein
-
expression in CHO cells. The enzyme is secreted as an active homodimer of a 130000 Da precursor that is proteolyzed into two polypeptides of 55000 Da and 72000 Da during the subsequent purification of the enzyme
-
expression in Pichia pastoris
-
expression in COS cells
-
expression in Pichia pastoris
-
expression of Golgi alpha-mannosidase IA in fusion with the yeast alpha-factor signal sequence in Pichia pastoris strain GS115
-
overexpressed in Escherichia coli
-, Q6L2X5
expression in COS cells
-
expressed in Escherichia coli as a His-tagged fusion protein
-
expressed in Escherichia coli as a His-tagged fusion protein
-
gene M1 GAS SF370, DNA and amino acid sequence determination and analysis, cloning of the coding sequence for SpGH38 residues 1-901, overexpression as 3C protease cleavable N-terminal His6-tagged enzyme in Escherichia coli strain BL21(DE3)
Q99YP5
expressed as a fusion of the glutathione S-transferase of Schistosoma japonicum in Escherichia coli
-
overexpression in Sulfolobus solfataricus mutant PBL2025, that misses 50 genes (SSO3004-3050), including genes coding for a multitude of enzymes possibly involved in sugar degradation or metabolism
-
expression in Escherichia coli
-
TM1851, expression in Escherichia coli
-
expression in Pichia pastoris
-
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
alpha-Man transcripts as well as enzyme activity increase with the ripening and/or softening of capsicum
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
DELTAT887
O00754
T887SfsX45, c.2660delC causes a frameshift introducing a premature stop codon (p.T887SfsX45)
H200N
O00754
missense mutantion c.597 C>A. Equal deleterious effect missense mutations indicating disease-causing mutations
L518P
O00754
missense mutantion c.1553 T
R916S
O00754
missense mutantion c.2746 C>A, spatially close to the oldest known inherited alpha mannosidosis mutation p.R750W. Equal deleterious effect missense mutations indicating disease-causing mutations
D338G
-
inactive mutant enzyme. In presence of the external nucleophil (1 M) sodium formate the activity is partially rescued
D338G
-
inactive mutant enzyme. In presence of the external nucleophil (1 M) sodium formate the activity is partially rescued
-
D341N
-
the turnover numberis lower by roughly 200fold compared with that of wild-type enzyme
additional information
-
N-bromosuccinimide added to determine Trp-residues involved in enzyme activity. N-bromosuccinimide modified inactivation is monitored spectrophotometerically
Renatured/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
66% remaining activity after urea is removed from a Sepharose-immobilized enzyme
-
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
analysis
-
characterization of asparagine-linked oligosaccharides
medicine
-
the key enzyme in N-glycan processing is a target in the development of anticanver therapies
diagnostics
-
detection of enzymatic changes might relate to the pathogenesis of leukemia disease but also represent a potential peripheral diagnostic marker
medicine
-
determination of the activity of alpha-mannosidase, beta-mannosidase, beta-glucocerebrosidase, beta-galactosidase and beta-hexosaminidase in cerebrospinal fluid of patients suffering from dementia with Lewis bodies, Alzheimer's disease, fronto-temporal dementia and controls. alpha-Mannosidase activity shows a marked decrease across all the pathological groups as compared to controls
medicine
-
inhibition of N-glycan processing in the endoplasmic reticulum attenuates endoplasmic reticulum stressinduced cell death by increasing high-mannose type oligosaccharides that reduce protein aggregation, such as amyloidogenesis
analysis
-
comparison of glycolytic and chitinolytic enzyme activities between desert and oasis flies of Phlebotomus papatasi to evaluate potential differences in susceptibility to infection with Leishmania major
medicine
-
inhibition of N-glycan processing in the endoplasmic reticulum attenuates endoplasmic reticulum stress-induced cell death by increasing high-mannose type oligosaccharides that reduce protein aggregation, such as amyloidogenesis