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Information on EC 3.2.1.24 - alpha-mannosidase and Organism(s) Homo sapiens and UniProt Accession Q9NTJ4

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IUBMB Comments
Also hydrolyses alpha-D-lyxosides and heptopyranosides with the same configuration at C-2, C-3 and C-4 as mannose.
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Select one or more organisms in this record: ?
This record set is specific for:
Homo sapiens
UNIPROT: Q9NTJ4
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
alpha-mannosidase, mannanase, alpha-d-mannosidase, lysosomal alpha-mannosidase, alpha-mannosidase ii, golgi alpha-mannosidase ii, alpha1,2-mannosidase, alpha-1,2-mannosidase, alpha-man, man2c1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
alpha-mannosidase
-
ER-mannosidase II
-
Man2C1 alpha-mannosidase
-
neutral/cytosol mannosidase
-
1,2-alpha-D-mannosidase
-
-
-
-
1,2-alpha-mannosidase
-
-
-
-
acid alpha-mannosidase
-
-
alpha 1,2-mannosidase
-
-
Alpha mannosidase 6A8B
-
-
-
-
alpha-D-mannopyranosidase
-
-
-
-
alpha-D-mannosidase
Alpha-D-mannoside mannohydrolase
-
-
-
-
alpha-mann
-
-
alpha-mannosidase
alpha-mannosidase C
-
-
AMAN
-
-
-
-
exo-alpha-mannosidase
-
-
-
-
Laman
Lysosomal acid alpha-mannosidase
-
-
-
-
lysosomal alpha-mannosidase
-
neutral alpha-mannosidase
-
-
p-nitrophenyl-alpha-mannosidase
-
-
-
-
velmanase alfa
-
commercial preparation
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of O-glycosyl bond
-
-
-
-
PATHWAY SOURCE
PATHWAYS
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.
CAS REGISTRY NUMBER
COMMENTARY hide
9025-42-7
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-nitrophenyl-alpha-D-mannoside + H2O
4-nitrophenol + alpha-D-mannose
show the reaction diagram
pNP-alpha-Man, used for enzyme activity test
-
-
?
mannosyl(5)-N-acetyl-glucosamine-pyridylamino + H2O
mannosyl(4)-N-acetyl-glucosamine-pyridylamino + mannosyl(3)-N-acetyl-glucosamine-pyridylamino
show the reaction diagram
-
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 + 4 H2O
mannosyl(5)-N-acetyl-glucosamine + 4 alpha-D-mannose
show the reaction diagram
in presence of Co2+
-
-
?
mannosyl(9)-N-acetyl-glucosamine + H2O
mannosyl(8)-N-acetyl-glucosamine + alpha-D-mannose
show the reaction diagram
absence of Co2+
-
-
?
4-methylumbelliferyl alpha-D-mannopyranoside + H2O
4-methylumbelliferol + alpha-D-mannopyranose
show the reaction diagram
-
-
-
?
4-methylumbelliferyl-alpha-D-mannopyranoside
?
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
-
-
-
?
6 pyridylamino-Man9GlcNAc2 + H2O
pyridylamino-Man8GlcNAc2 + pyridylamino-Man7GlcNAc2 + pyridylamino-Man6GlcNAc2 + pyridylamino-Man5GlcNAc2 + pyridylamino-Man4GlcNAc2 + pyridylamino-Man3GlcNAc2 + 21 alpha-D-mannopyranose
show the reaction diagram
-
-
-
?
alpha-D-mannosidosis fibroblasts + H2O
Man7-2GlcNAc + ?
show the reaction diagram
-
-
-
?
Man9GlcNAc2 + H2O
Man5GlcNAc2 + Man6GlcNAc2 + Man7GlcNAc2 + Man8GlcNAc2 + 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
?
methyl-alpha-D-mannopyranoside + H2O
alpha-D-mannopyranose + methanol
show the reaction diagram
-
-
-
?
p-nitrophenyl-alpha-D-mannopyranoside + H2O
p-nitrophenol + alpha-D-mannopyranose
show the reaction diagram
-
-
-
?
pyridylamino-Man5GlcNAc + 3 H2O
pyridylamino-Man2GlcNA + alpha-D-mannopyranose
show the reaction diagram
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
alpha-D-mannosidosis fibroblasts + H2O
Man7-2GlcNAc + ?
show the reaction diagram
-
-
-
?
Man9GlcNAc2 + H2O
Man5GlcNAc2 + Man6GlcNAc2 + Man7GlcNAc2 + Man8GlcNAc2 + 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
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
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+
-
2-3fold increase of activity for neutral alpha-mannosidases
Zn2+
activates
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
deoxymannojirimycin
less effective compared with swainsonine, concentration of 100 microM
kifunensine
little inhibitory effect, concentration of 10 microM
small interfering RNA
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
-
swainsonine
concentration of 100 microM
(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,8R,8aR)-octahydroindolizine-1,2,8-triol
-
-
(2R,3R,4S)-2-([[(1R)-2-hydroxy-1-phenylethyl]amino]methyl)pyrrolidine-3,4-diol
-
-
(2R,3R,4S)-2-[([(1R)-2-hydroxy-1-phenylethyl]amino)methyl]pyrrolidine-3,4-diol
(2R,3R,4S)-2-[([(1S)-2-hydroxy-1-phenylethyl]amino)methyl]pyrrolidine-3,4-diol
-
-
(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
-
-
(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
-
-
(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
-
-
1,4-Dideoxy-1,4-imino-D-mannitol
-
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-deoxymannojirimicin
-
complete inhibition at 1 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
3-bromo-N-[(2S)-2-[([(2R,3S,4R)-3,4-dihydroxypyrrolidin-2-yl]methyl)amino]-2-phenylethyl]benzamide
-
-
8,8a-di-epi-swainsonine
-
-
8a-epi-swainsonine
-
-
Co2+
-
10-30% inhibition for acid alpha-mannosidase
deoxymannojirimycin
-
DMJ 3
EDTA
-
complete inhibition at 20 mM, activity recovered in the presence of Ca2+
kifunensine
-
Kif 2, docking studies with the crystal structure of human alpha-1,2-mannosidase complexed with kifunensine (PDB: 1FO3) as a template
methyl-alpha-D-mannopyranoside
-
40-50% inhibition of acid alpha-mannosidase, neutral alpha-mannosidase not affected
swainsonine
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.55 - 1.065
4-methylumbelliferyl-alpha-D-mannopyranoside
2.4
p-nitrophenyl-alpha-D-mannopyranoside
-
-
additional information
additional information
-
-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
-
-
0.75
1-deoxymannojirimycin
-
pH 5.5, liver lysosomal fraction
0.02
8,8a-di-epi-swainsonine
-
liver lysosomal fraction
0.75
8a-epi-swainsonine
-
liver lysosomal fraction
0.4
deoxymannojirimycin
-
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00001 - 0.00005
(1S,2R,8R,8aR)-octahydroindolizine-1,2,8-triol
0.025 - 0.05
(2R,3R,4S)-2-([[(1R)-2-hydroxy-1-phenylethyl]amino]methyl)pyrrolidine-3,4-diol
0.0005 - 0.002
(3R,4R,5R)-3,4-dihydroxy-5-([[(1R)-2-hydroxy-1-phenylethyl]amino]methyl)-1-methylpyrrolidin-2-one
0.05 - 0.35
(3R,4R,5R)-3,4-dihydroxy-5-([[(1R)-2-hydroxy-1-phenylethyl]amino]methyl)pyrrolidin-2-one
0.00011
swainsonine
Homo sapiens
-
IC50: 0.00011 mM
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.29
-
-
2.5
-
alpha-mannosidase A
4.6
-
alpha-mannosidase B
additional information
-
effects of all trans retinoic acid treatment of HL-60 on enzymatic activity of glycohydrolases tested
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 4.5
5.5 - 6
6 - 6.4
-
-
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
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.3 - 6
-
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
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
-
4 forms of intermediate alpha-mannosidases
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
examination of subcellular localization of Man2C1, using FLAG-tagging at the N-terminus for detection
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
MA2C1_HUMAN
1040
0
115835
Swiss-Prot
other Location (Reliability: 5)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
120000
LAMAN 120 kDa precursor detected in wild type and mutant constructs. Western blot analysis
26000
-
alpha3beta3, 3 * 62000 + 3 * 26000, SDS-PAGE, alpha-mannosidase A
260000
280000
62000
-
alpha3beta3, 3 * 62000 + 3 * 26000, SDS-PAGE, alpha-mannosidase A
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
heterodimer
1 * 62000 + 1 * 26000, liver isoform A, SDS-PAGE
heterotrimer
1 * 62000 + 1 * 58000 + 1 * 26000, liver isoform B, SDS-PAGE
hexamer
-
alpha3beta3, 3 * 62000 + 3 * 26000, SDS-PAGE, alpha-mannosidase A
oligomer
-
composed of equal amounts of 62, 58 and 26 kDa subunits
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
-
-
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
structual 3D analysis
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A95P
inactive
C501S
more than 30% of wild type activity
C501S/R950P
inactive
C55F
inactive
D149N
inactive
D74E
inactive
DELTAT887
T887SfsX45, c.2660delC causes a frameshift introducing a premature stop codon (p.T887SfsX45)
F1000S
inactive
G390C
inactive
G420V
inactive
G451C
20-30% of wild type activity
G800R
inactive
G800W
inactive
G891R
inactive
H200L
more than 30% of wild type activity
H200N
H445Y
inactive
L352P
inactive
L518P
missense mutantion c.1553 T
L565P
inactive
L809P
the mutation is associated with alpha-mannosidosis
L892P
inactive
L956R
inactive
P197R
inactive
P263L
inactive
P379L
20-30% of wild type activity
R202P
20-30% of wild type activity
R229W
20-30% of wild type activity
R750W
the mutation is associated with alpha-mannosidosis
R916C
inactive
R916H
inactive
R916S
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
R950P
inactive
S318L
more than 30% of wild type activity
S453F
20-30% of wild type activity
S453Y
inactive
T745R
inactive
V457E
more than 30% of wild type activity
Y99H
inactive
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 7.5
-
30-64% remaining activity
135958
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
-
10-20% loss of activity for acid alpha-mannosidase, 60-80% inhibition for neutral alpha-mannosidases
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
FLAG–tagged Man2C1 from cytosolic fraction of HEK-293 cells, analysed by silver staining
DEAE-cellulose column chromatography
recombinant protein, to homogeneity
-
to homogeneity, chromatography steps
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Porwoll, S.; Fuchs, H.; Tauber, R.
Characterization of a soluble class I alpha-mannosidase in human serum
FEBS Lett.
449
175-178
1999
Homo sapiens
Manually annotated by BRENDA team
Liao, Y.F.; Lal, A.; Moremen, K.W.
Cloning, expression, purification, and characterization of the human broad specificity lysosomal acid alpha-mannosidase
J. Biol. Chem.
271
28348-28358
1996
Homo sapiens
Manually annotated by BRENDA team
Cheng, S.H.; Malcolm, S.; Pemble, S.; Winchester, B.
Purification and comparison of the structures of human liver acidic alpha-D-mannosidases A and B
Biochem. J.
233
65-72
1986
Homo sapiens
Manually annotated by BRENDA team
Poenaru, L.; Dreyfus, J.C.
alpha-Mannosidase in human red cells
Biochim. Biophys. Acta
566
67-71
1979
Homo sapiens
Manually annotated by BRENDA team
Hirani, S.; Winchester, B.
The multiple forms of alpha-D-mannosidase in human plasma
Biochem. J.
179
583-592
1979
Homo sapiens
Manually annotated by BRENDA team
Hultberg, B.; Masson, P.K.; Sjbald, S.
Neutral alpha-mannosidase activity in human serum
Biochim. Biophys. Acta
445
398-405
1976
Homo sapiens
Manually annotated by BRENDA team
Orlacchio, A.; Bernardi, G.; Orlacchio, A.; Emiliani, C.
alpha-D-Mannosidase properties in serum of patients with amyotrophic lateral sclerosis
J. Neurol.
248
1090-1092
2001
Homo sapiens
Manually annotated by BRENDA team
Berg, T.; King, B.; Meikle, P.J.; Nilssen, O.; Tollersrud, O.K.; Hopwood, J.J.
Purification and characterization of recombinant human lysosomal alpha-mannosidase
Mol. Genet. Metab.
73
18-29
2001
Homo sapiens
Manually annotated by BRENDA team
Siriwardena, A.; Strachan, H.; El-Daher, S.; Way, G.; Winchester, B.; Glushka, J.; Moremen, K.; Boons, G.
Potent and selective inhibition of class II alpha-D-mannosidase activity by a bicyclic sulfonium salt
ChemBioChem
6
845-848
2005
Homo sapiens
Manually annotated by BRENDA team
Fiaux, H.; Popowycz, F.; Favre, S.; Schuetz, C.; Vogel, P.; Gerber-Lemaire, S.; Juillerat-Jeanneret, L.
Functionalized pyrrolidines inhibit alpha-mannosidase activity and growth of human glioblastoma and melanoma cells
J. Med. Chem.
48
4237-4246
2005
Canavalia ensiformis, Homo sapiens
Manually annotated by BRENDA team
Suzuki, T.; Hara, I.; Nakano, M.; Shigeta, M.; Nakagawa, T.; Kondo, A.; Funakoshi, Y.; Taniguchi, N.
Man2C1, an alpha-mannosidase, is involved in the trimming of free oligosaccharides in the cytosol
Biochem. J.
400
33-41
2006
Homo sapiens (Q9NTJ4), Homo sapiens
Manually annotated by BRENDA team
Sivapriya, K.; Hariharaputran, S.; Suhas, V.L.; Chandra, N.; Chandrasekaran, S.
Conformationally locked thiosugars as potent alpha-mannosidase inhibitors: synthesis, biochemical and docking studies
Bioorg. Med. Chem.
15
5659-5665
2007
Homo sapiens
Manually annotated by BRENDA team
Pittis, M.G.; Montalvo, A.L.; Heikinheimo, P.; Sbaragli, M.; Balducci, C.; Persichetti, E.; Van Maldergem, L.; Filocamo, M.; Bembi, B.; Beccari, T.
Funtional characterization of four novel MAN2B1 mutations causing juvenile onset alpha-mannosidosis
Clin. Chim. Acta
375
136-139
2007
Homo sapiens (O00754), Homo sapiens
Manually annotated by BRENDA team
Racanicchi, L.; Montanucci, P.; Basta, G.P.; Pensato, A.; Conti, V.; Calafiore, R.
Effect of all trans retinoic acid on lysosomal alpha-D-mannosidase activity in Hl-60 cell: correlation with Hl-60 cells differentiation
Mol. Cell. Biochem.
308
17-24
2008
Homo sapiens
Manually annotated by BRENDA team
Fiaux, H.; Kuntz, D.A.; Hoffman, D.; Janzer, R.C.; Gerber-Lemaire, S.; Rose, D.R.; Juillerat-Jeanneret, L.
Functionalized pyrrolidine inhibitors of human type II alpha-mannosidases as anti-cancer agents: optimizing the fit to the active site
Bioorg. Med. Chem.
16
7337-7346
2008
Homo sapiens, Canavalia sp.
Manually annotated by BRENDA team
Parnetti, L.; Balducci, C.; Pierguidi, L.; De Carlo, C.; Peducci, M.; DAmore, C.; Padiglioni, C.; Mastrocola, S.; Persichetti, E.; Paciotti, S.; Bellomo, G.; Tambasco, N.; Rossi, A.; Beccari, T.; Calabresi, P.
Cerebrospinal fluid beta-glucocerebrosidase activity is reduced in dementia with Lewy Bodies
Neurobiol. Dis.
34
484-486
2009
Homo sapiens
Manually annotated by BRENDA team
Riise Stensland, H.; Klenow, H.; Nguyen, L.; Hansen, G.; Malm, D.; Nilssen, .
Identification of 83 novel alpha-mannosidosis-associated sequence variants: Functional analysis of MAN2B1 missense mutations
Hum. Mutat.
33
511-520
2012
Homo sapiens (O00754), Homo sapiens
Manually annotated by BRENDA team
Borgwardt, L.; Dali, C.I.; Fogh, J.; Mansson, J.E.; Olsen, K.J.; Beck, H.C.; Nielsen, K.G.; Nielsen, L.H.; Olsen, S.O.; Riise Stensland, H.M.; Nilssen, O.; Wibrand, F.; Thuesen, A.M.; Pearl, T.; Haugsted, U.; Saftig, P.; Blanz, J.; Jones, S.A.; Tylki-Szymanska, A.; Guffon-Fouiloux, N.; Beck, M.; Lund, A.M.
Enzyme replacement therapy for alpha-mannosidosis: 12 months follow-up of a single centre, randomised, multiple dose study
J. Inherit. Metab. Dis.
36
1015-1024
2013
Homo sapiens
Manually annotated by BRENDA team
Paciotti, S.; Codini, M.; Tasegian, A.; Ceccarini, M.R.; Cataldi, S.; Arcuri, C.; Fioretti, B.; Albi, E.; Beccari, T.
Lysosomal alpha-mannosidase and alpha-mannosidosis
Front. Biosci.
22
157-167
2017
Homo sapiens (O00754), Homo sapiens
Manually annotated by BRENDA team
Lund, A.M.; Borgwardt, L.; Cattaneo, F.; Ardigo, D.; Geraci, S.; Gil-Campos, M.; De Meirleir, L.; Laroche, C.; Dolhem, P.; Cole, D.; Tylki-Szymanska, A.; Lopez-Rodriguez, M.; Guillen-Navarro, E.; Dali, C.I.; Heron, B.; Fogh, J.; Muschol, N.; Phillips, D.; Van den Hout, J.M.H.; Jones, S.A.; Amraoui, Y.
Comprehensive long-term efficacy and safety of recombinant human alpha-mannosidase (velmanase alfa) treatment in patients with alpha-mannosidosis
J. Inherit. Metab. Dis.
41
1225-1233
2018
Homo sapiens
Manually annotated by BRENDA team
Harmatz, P.; Cattaneo, F.; Ardigo, D.; Geraci, S.; Hennermann, J.B.; Guffon, N.; Lund, A.; Hendriksz, C.J.; Borgwardt, L.
Enzyme replacement therapy with velmanase alfa (human recombinant alpha-mannosidase) Novel global treatment response model and outcomes in patients with alpha-mannosidosis
Mol. Genet. Metab.
124
152-160
2018
Homo sapiens
Manually annotated by BRENDA team