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Information on EC 3.2.1.18 - exo-alpha-sialidase and Organism(s) Trypanosoma rangeli and UniProt Accession O44049

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EC Tree
IUBMB Comments
The enzyme does not act on 4-O-acetylated sialic acids. endo-alpha-Sialidase activity is listed as EC 3.2.1.129, endo-alpha-sialidase. See also EC 4.2.2.15 anhydrosialidase.
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This record set is specific for:
Trypanosoma rangeli
UNIPROT: O44049
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Word Map
The taxonomic range for the selected organisms is: Trypanosoma rangeli
The enzyme appears in selected viruses and cellular organisms
Synonyms
neuraminidase, sialidase, glycosyl hydrolase, trans-sialidase, hemagglutinin-neuraminidase, major surface antigen, alpha2,6-sialyltransferase, cytosolic sialidase, endosialidase, neuraminidase 1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
acetylneuraminidase
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Acetylneuraminyl hydrolase
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acylneuraminyl glycohydrolase
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alpha-neuraminidase
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Cytosolic sialidase
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-
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G9 sialidase
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Ganglioside sialidase
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Lysosomal sialidase
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Major 85 kDa surface antigen
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Major surface antigen
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Membrane sialidase
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Mouse skeletal muscle sialidase
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MSS
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MTS
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mucopolysaccharide N-acetylneuraminylhydrolase
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Murine thymic sialidase
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N-acylneuraminate glycohydrolase
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NANase
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neuraminidase
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SA85-1.1 protein
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SA85-1.2 protein
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SA85-1.3 protein
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sialidase
STNA
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-(2->8)- glycosidic linkages of terminal sialic acid residues in oligosaccharides, glycoproteins, glycolipids, colominic acid and synthetic substrates
show the reaction diagram
catalytic chemistry involves the formation of a covalent intermediate with an active site tyrosine nucleophile
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of O-glycosyl bond
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PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
acetylneuraminyl hydrolase
The enzyme does not act on 4-O-acetylated sialic acids. endo-alpha-Sialidase activity is listed as EC 3.2.1.129, endo-alpha-sialidase. See also EC 4.2.2.15 anhydrosialidase.
CAS REGISTRY NUMBER
COMMENTARY hide
9001-67-6
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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
3'-sialyllactose + H2O
sialic acid + lactose
show the reaction diagram
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?
casein glycomacropeptide + H2O
sialic acid + ?
show the reaction diagram
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?
casein glycomacropeptide + lactose
3'-sialyllactose + ?
show the reaction diagram
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?
fetuin + H2O
?
show the reaction diagram
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?
additional information
?
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the strict hydrolase of Trypanosoma rangeli shows no trans-sialidase activity
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?
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
fetuin + H2O
?
show the reaction diagram
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?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-Deoxy-2,3-didehydro-N-acetylneuraminic acid
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
O44049_TRYRA
660
0
71965
TrEMBL
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
72700
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x * 72700, calculated from amino acid sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 72700, calculated from amino acid sequence
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
comparison of the catalytic cleft plasticity of free and ligand-bound forms of Trypanosoma rangeli sialidase and Trypanosoma cruzi trans-sialidase using molecular dynamics simulations. The Trypanosoma cruzi enzyme has a very flexible, widely open catalytic cleft, mostly due to resiude W312 loop motion, in apo form. In ligan-bound form, the flexibility and solvent exposure is significantly reduced. The Trypanosoma rangeli sialidase maintains a more open catalytic cleft in both apo and holo forms
three-dimensional structures of the covalent glycosyl-enzyme complexes formed by Trypanosoma rangeli sialidase with two different mechanism-based inactivators at 1.9 A and at 1.7 A resolution
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 65
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engineered free sialidase Tr6 is stable at 25°C for at least 24 h. At 45°C the enzyme is stable for at least 100 min. 2% of the initial trans-sialidase activity is retained after 5 min of incubation at 65°C
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni2+ affinity column chromatography, and gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Pichia pastoris
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Watts, A.G.; Oppezzo, P.; Withers, S.G.; Alzari, P.M.; Buschiazzo, A.
Structural and kinetic analysis of two covalent sialosyl-enzyme intermediates on Trypanosoma rangeli sialidase
J. Biol. Chem.
281
4149-4155
2006
Trypanosoma rangeli (O44049), Trypanosoma rangeli
Manually annotated by BRENDA team
Demir, O.; Roitberg, A.
Modulation of catalytic function by differential plasticity of an active site: case study of Trypanosoma cruzi trans-sialidase and Trypanosoma rangeli sialidase
Biochemistry
48
3398-3406
2009
Trypanosoma cruzi, Trypanosoma rangeli (O44049), Trypanosoma rangeli
Manually annotated by BRENDA team
Zeuner, B.; Luo, J.; Nyffenegger, C.; Aumala, V.; Mikkelsen, J.D.; Meyer, A.S.
Optimizing the biocatalytic productivity of an engineered sialidase from Trypanosoma rangeli for 3-sialyllactose production
Enzyme Microb. Technol.
55
85-93
2014
Trypanosoma rangeli
Manually annotated by BRENDA team
Bueren-Calabuig, J.A.; Pierdominici-Sottile, G.; Roitberg, A.E.
Unraveling the differences of the hydrolytic activity of Trypanosoma cruzi trans-sialidase and Trypanosoma rangeli sialidase: a quantum mechanics-molecular mechanics modeling study
J. Phys. Chem. B
118
5807-5816
2014
Trypanosoma rangeli
Manually annotated by BRENDA team