Literature summary for 3.2.1.18 extracted from

Wu, J.; Zhang, F.; Wang, M.; Xu, C.; Song, J.; Zhou, J.; Lin, X.; Zhang, Y.; Wu, X.; Tan, W.; Lu, J.; Zhao, H.; Gao, J.; Zhao, P.; Lu, J.; Wang, Y.
Characterization of neuraminidases from the highly pathogenic avian H5N1 and 2009 pandemic H1N1 influenza A viruses (2010), PLoS ONE, 5, e15825.

Search for more literature for 3.2.1.18

Protein Variants

Protein Variants	Comment	Organism
additional information	construction of insertion mutant enzyme by deleting the 20-aa segment, residues 49-68, from the stalk region of 2009H1N1 neuraminidase, and inserting this segment, designated 09s60, into the stalk region of H5N1 neuraminidase	influenza A virus

Inhibitors

Inhibitors	Comment	Organism	Structure
oseltamivir	the robust neuraminidase activity of the 2009H1N1 virus is responsible for the high sensitivity of the virus to oseltamivir	influenza A virus

Organism

Organism	UniProt	Comment	Textmining
influenza A virus	-	-	-
influenza A virus A/California/05/2009/H1N1	-	-	-
influenza A virus A/Hong Kong/156/97/H5N1	-	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
glycoprotein	-	influenza A virus
glycoprotein	glycosylation pattern of insertion mutant 09N1	influenza A virus

Source Tissue

Source Tissue	Comment	Organism	Textmining

Subunits

Subunits	Comment	Organism
oligomer	the wild-type neuraminidase from this virus occurs primarily as a 120 kDa dimer but also as a tetramer and, in lesser amounts, as a 60 kDa monomer. The molecular masses of AH N1 and AH N1+09s60 expressed in pseudoparticle-infected 293T cells are 50 kDa and 60 kDa, respectively	influenza A virus

Synonyms

Synonyms	Comment	Organism
neuraminidase	-	influenza A virus

General Information

General Information	Comment	Organism
malfunction	neuraminidase insertion mutant virus shows increased particles formation, in pseudotyped particles system, activity compared to the wild-type virus. Compared with the wild-type AH N1, from A/California/05/2009/H1N1, the wild-type 09N1 exhibits higher neuraminidase activity and releases more pseudoparticles. Deletion/insertion of the 09s60 segment does not alter this relationship. The infectivity of pseudoparticles harboring neuraminidase in combination with the hemagglutinin from HPAI H5N1 (AH H5) is decreased by insertion of 09s60 into AH N1 and is increased by deletion of 09s60 from 09N1, the mutation also alters the oligomeric structure, overview	influenza A virus
malfunction	neuraminidase insertion mutant virus shows increased particles formation, in pseudotyped particles system, activity compared to the wild-type virus. Compared with the wild-type AH N1, the wild-type 09N1 exhibits higher neuraminidase activity and releases more pseudoparticles. Deletion/insertion of the 09s60 segment does not alter this relationship. The infectivity of pseudoparticles harboring neuraminidase in combination with the hemagglutinin from HPAI H5N1 (AH H5, from A/Hong Kong/156/97/H5N1) is decreased by insertion of 09s60 into AH N1 and is increased by deletion of 09s60 from 09N1, the mutation also alters the oligomeric structure, overview	influenza A virus

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)