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Information on EC 3.2.1.18 - exo-alpha-sialidase and Organism(s) Micromonospora viridifaciens and UniProt Accession Q02834

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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:
Micromonospora viridifaciens
UNIPROT: Q02834
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Word Map
The taxonomic range for the selected organisms is: Micromonospora viridifaciens
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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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-acetylneuraminosyl glycohydrolase
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N-acylneuraminate glycohydrolase
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NANase
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neuraminidase
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
exo-glycosidase, active center contains essential cysteine residues
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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
phenyl alpha-sialoside + H2O
?
show the reaction diagram
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?
phenyl beta-sialoside + H2O
phenol + alpha-sialic acid
show the reaction diagram
mutant enzymes Y370G, Y370A, Y370N and Y370T catalyze the hydrolysis of phenyl beta-sialoside with an inversion of the anomeric configuration. Mutant enzyme Y370A shows 4% of the activity of Y370G, mutant enzymes Y370N and Y370T show 9% of the activity of Y370G
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?
phenyl beta-sialoside + lactose
phenol + sialyllactose
show the reaction diagram
the Y370G mutant can transfer the sialic acid moiety from phenyl beta-sialoside to lactose in yields of up to 13%13%. Greater than 90% of the sialyllactose product formed in the coupling reactions is the alpha-2,6-isomer.
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?
2-(4-methylumbelliferyl)-alpha-D-N-acetylneuraminic acid + H2O
4-methylumbelliferol + alpha-D-N-acetylneuraminic acid
show the reaction diagram
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?
2-(4-nitrophenyl)-alpha-D-N-acetylneuraminic acid + H2O
4-nitrophenol + alpha-D-N-acetylneuraminic acid
show the reaction diagram
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?
phenyl beta-sialoside + lactose
phenol + sialyllactose
show the reaction diagram
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?
additional information
?
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essential enzyme, bacterial enzymes may serve as a colonization and virulence factor or as an important tool for nutrification
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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
additional information
?
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essential enzyme, bacterial enzymes may serve as a colonization and virulence factor or as an important tool for nutrification
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?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
N-bromosuccimide
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000045
phenyl alpha-sialoside
pH 5.25, 37°C, mutant enzyme Y370G
0.000023
phenyl beta-sialoside
pH 5.25, 37°C, mutant enzyme Y370G
2.1
alpha-sialyllactose
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.82
phenyl alpha-sialoside
pH 5.25, 37°C, mutant enzyme Y370G
13.3
phenyl beta-sialoside
pH 5.25, 37°C, mutant enzyme Y370G
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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?
NANH_MICVI
647
0
68830
Swiss-Prot
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Y370A
catalyzes the hydrolysis of phenyl beta-sialoside with an inversion of the anomeric configuration, 4% of the activity with Y370G
Y370G
Y370N
catalyzes the hydrolysis of phenyl beta-sialoside with an inversion of the anomeric configuration, 9% of the activity with Y370N
Y370T
catalyzes the hydrolysis of phenyl beta-sialoside with an inversion of the anomeric configuration, 9% of the activity with Y370T
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Abrashev, I.; Dulguerova, G.
Neuraminidases (sialidases) from bacterial origin
Exp. Pathol. Parasitol.
4
35-40
2000
Glutamicibacter nicotianae, Arthrobacter sp., Paenarthrobacter ureafaciens, Clostridium chauvoei, Clostridium perfringens, Paeniclostridium sordellii, Corynebacterium diphtheriae, Corynebacterium ulcerans, Pasteurella multocida, Streptococcus sp., Trichomonas vaginalis, Micromonospora viridifaciens, Erysipelothrix rhusiopathiae, Vibrio cholerae serotype O1, Paeniclostridium sordellii G12
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Manually annotated by BRENDA team
Watson, J.N.; Indurugalla, D.; Cheng, L.L.; Narine, A.A.; Bennet, A.J.
The hydrolase and transferase activity of an inverting mutant sialidase using non-natural beta-sialoside substrates
Biochemistry
45
13264-13275
2006
Micromonospora viridifaciens (Q02834), Micromonospora viridifaciens
Manually annotated by BRENDA team
Cheng, L.L.; Shidmoossavee, F.S.; Bennet, A.J.
Neuraminidase substrate promiscuity permits a mutant Micromonospora viridifaciens enzyme to synthesize artificial carbohydrates
Biochemistry
53
3982-3989
2014
Micromonospora viridifaciens (Q02834), Micromonospora viridifaciens
Manually annotated by BRENDA team