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

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EC Tree
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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This record set is specific for:
Homo sapiens
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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, alpha1,2-mannosidase, golgi alpha-mannosidase ii, alpha-1,2-mannosidase, alpha-man, man2c1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
-
-
-
-
ER-mannosidase II
-
exo-alpha-mannosidase
-
-
-
-
Laman
Lysosomal acid alpha-mannosidase
-
-
-
-
lysosomal alpha-mannosidase
-
Man2C1 alpha-mannosidase
-
neutral alpha-mannosidase
-
-
neutral/cytosol 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-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
-
-
-
?
4-nitrophenyl-alpha-D-mannoside + H2O
4-nitrophenol + alpha-D-mannose
show the reaction diagram
pNP-alpha-Man, used for enzyme activity test
-
-
?
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
?
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+
-
-
?
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
Zn2+
activates
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
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,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
-
potent and selective inhibition
(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
EDTA
-
complete inhibition at 20 mM, activity recovered in the presence of Ca2+
kifunensine
methyl-alpha-D-mannopyranoside
-
40-50% inhibition of acid alpha-mannosidase, neutral alpha-mannosidase not affected
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
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
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?
MA2B1_HUMAN
1011
0
113744
Swiss-Prot
Mitochondrion (Reliability: 4)
MA2B2_HUMAN
1009
0
113979
Swiss-Prot
Secretory Pathway (Reliability: 1)
MA2C1_HUMAN
1040
0
115835
Swiss-Prot
other Location (Reliability: 5)
A0A140VJN9_HUMAN
1040
0
115835
TrEMBL
other Location (Reliability: 5)
Q93093_HUMAN
323
0
37152
TrEMBL
Secretory Pathway (Reliability: 1)
MA1B1_HUMAN
699
1
79580
Swiss-Prot
-
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
DEAE-cellulose column chromatography
FLAG–tagged Man2C1 from cytosolic fraction of HEK-293 cells, analysed by silver staining
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