Literature summary for 3.2.1.129 extracted from

Schwarzer, D.; Stummeyer, K.; Gerardy-Schahn, R.; Muehlenhoff, M.
Characterization of a Novel Intramolecular Chaperone Domain Conserved in Endosialidases and Other Bacteriophage Tail Spike and Fiber Proteins (2007), J. Biol. Chem., 282, 2821-2831.

Search for more literature for 3.2.1.129

Application

Application	Comment	Organism
additional information	the C-terminal domain plays a crucial role in folding and assembling not only the C-terminal domain of endosialidases but also of other, unrelated phage proteins	Escherichia phage K1F

Cloned(Commentary)

Cloned (Comment)	Organism
subcloned into the NdeI and XhoI restriction sites of pET22b, resulting in a construct encoding the C-terminal domain of endoNF with a C-terminal His6 tag, expressed in Escherichia coli BL21-Gold(DE3)	Escherichia phage K1F

Protein Variants

Protein Variants	Comment	Organism
G956A	completely loses enzymatic activity	Escherichia phage K1F
H954A	completely loses enzymatic activity	Escherichia phage K1F
additional information	mutant deltaN-endoNF lacking the capsid binding domain, forms trimeric complexes	Escherichia phage K1F
N912A	completely loses enzymatic activity	Escherichia phage K1F
R1035A	completely loses enzymatic activity	Escherichia phage K1F
S911A	mutant deltaN-endoNF lacking the capsid binding domain but retaining the C-terminal domain, prevents cleavage but not assembly into active trimers	Escherichia phage K1F

Organism

Organism	UniProt	Comment	Textmining
Escherichia phage K1F	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
by gel filtration, affinity chromatography and a Ni2+-chelating column	Escherichia phage K1F

Subunits

Subunits	Comment	Organism
trimer	gel filtration	Escherichia phage K1F

Synonyms

Synonyms	Comment	Organism
endo-N-acetylneuraminidase	-	Escherichia phage K1F
endoNF	-	Escherichia phage K1F
endosialidase	-	Escherichia phage K1F

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Release 2023.1 (January 2023)