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Information on EC 3.2.1.24 - alpha-mannosidase and Organism(s) Bos taurus and UniProt Accession Q29451

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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:
Bos taurus
UNIPROT: Q29451
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Word Map
The taxonomic range for the selected organisms is: Bos taurus
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
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-
-
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1,2-alpha-mannosidase
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-
-
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Alpha mannosidase 6A8B
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-
-
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alpha-D-mannopyranosidase
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-
-
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alpha-D-mannosidase
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-
-
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Alpha-D-mannoside mannohydrolase
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-
-
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AMAN
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-
-
-
exo-alpha-mannosidase
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-
-
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Laman
-
-
-
-
Lysosomal acid alpha-mannosidase
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-
-
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p-nitrophenyl-alpha-mannosidase
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of O-glycosyl bond
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-
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-
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
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
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
additional information
?
-
-
the enzyme is involved in ordered degradation of glycoproteins, inborn enzyme-deficiency results in lysosomal storage disorder alpha-mannosidosis
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-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
Uniprot
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
MA2B1_BOVIN
999
0
112919
Swiss-Prot
Mitochondrion (Reliability: 5)
PDB
SCOP
CATH
UNIPROT
ORGANISM
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
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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
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure at 2.7 A resolution
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Heikinheimo, P.; Helland, R.; Leiros, H.K.; Leiros, I.; Karlsen, S.; Evjen, G.; Ravelli, R.; Schoehn, G.; Ruigrok, R.; Tollersrud, O.K.; McSweeney, S.; Hough, E.
The structure of bovine lysosomal alpha-mannosidase suggests a novel mechanism for low-pH activation
J. Mol. Biol.
327
631-644
2003
Bos taurus (Q29451), Bos taurus
Manually annotated by BRENDA team
Faid, V.; Evjen, G.; Tollersrud, O.K.; Michalski, J.C.; Morelle, W.
Site-specific glycosylation analysis of the bovine lysosomal alpha-mannosidase
Glycobiology
16
440-461
2006
Bos taurus
Manually annotated by BRENDA team