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Literature summary for 3.2.1.17 extracted from

  • Sugahara, K.; Yokoi, K.J.; Nakamura, Y.; Nishino, T.; Yamakawa, A.; Taketo, A.; Kodaira, K.
    Mutational and biochemical analyses of the endolysin Lys(gaY) encoded by the Lactobacillus gasseri JCM 1131T phage phi gaY (2007), Gene, 404, 41-52.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
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Lactobacillus phage phigaY

Protein Variants

Protein Variants Comment Organism
D12A cell-lytic activity is strongly reduced Lactobacillus phage phigaY
D12A/E33A no cell-lytic activity Lactobacillus phage phigaY
D12G cell-lytic activity isstrongly reduced Lactobacillus phage phigaY
D198A cell-lytic activity is slightly reduced Lactobacillus phage phigaY
D36A cell-lytic activity is similar to wild-type enzyme Lactobacillus phage phigaY
D96A cell-lytic activity is strongly reduced Lactobacillus phage phigaY
E237A cell-lytic activity is similar to wild-type enzyme Lactobacillus phage phigaY
E238A cell-lytic activity is similar to wild-type enzyme Lactobacillus phage phigaY
E33A cell-lytic activity isstrongly reduced Lactobacillus phage phigaY
E88D cell-lytic activity is similar to wild-type enzyme Lactobacillus phage phigaY
E98A no cell-lytic activity Lactobacillus phage phigaY
G10S cell-lytic activity is strongly reduced Lactobacillus phage phigaY
G253A cell-lytic activity is similar to wild-type enzyme Lactobacillus phage phigaY
G267A cell-lytic activity is similar to wild-type enzyme Lactobacillus phage phigaY
G281A cell-lytic activity is similar to wild-type enzyme Lactobacillus phage phigaY
G292A cell-lytic activity is similar to wild-type enzyme Lactobacillus phage phigaY
H60R cell-lytic activity is strongly reduced Lactobacillus phage phigaY
K142E cell-lytic activity is similar to wild-type enzyme Lactobacillus phage phigaY
K142R cell-lytic activity is similar to wild-type enzyme Lactobacillus phage phigaY
K207A cell-lytic activity is similar to wild-type enzyme Lactobacillus phage phigaY
K211A cell-lytic activity is similar to wild-type enzyme Lactobacillus phage phigaY
K25T cell-lytic activity is similar to wild-type enzyme Lactobacillus phage phigaY
L132P cell-lytic activity is strongly reduced Lactobacillus phage phigaY
L264A cell-lytic activity is slightly reduced Lactobacillus phage phigaY
M1I cell-lytic activity is reduced Lactobacillus phage phigaY
M1K cell-lytic activity is reduced Lactobacillus phage phigaY
additional information deletion analysis demonstrates that the beta/alphagaY domain of N-terminal 216 residues is the core enzyme portion, although the cell-lytic ability is lower than that of LysgaY. These mutational experiments suggest that beta/alphagaY (in which two acidic residues of D12 and E98 likely act as catalytic residues) is responsible for cell-lytic activity, and SH3bgaY promotes beta/alphagaY possibly through cell-wall binding function Lactobacillus phage phigaY
N67K cell-lytic activity is similar to wild-type enzyme Lactobacillus phage phigaY
P212A cell-lytic activity is similar to wild-type enzyme Lactobacillus phage phigaY
P216A cell-lytic activity is similar to wild-type enzyme Lactobacillus phage phigaY
R109L cell-lytic activity is similar to wild-type enzyme Lactobacillus phage phigaY
R251A cell-lytic activity is slightly reduced Lactobacillus phage phigaY
V124M cell-lytic activity is slightly reduced Lactobacillus phage phigaY
V79F cell-lytic activity is similar to wild-type enzyme Lactobacillus phage phigaY
W284A cell-lytic activity is strongly reduced Lactobacillus phage phigaY
W284G cell-lytic activity is strongly reduced Lactobacillus phage phigaY
Y272A cell-lytic activity is strongly reduced Lactobacillus phage phigaY
Y61H cell-lytic activity is stronly reduced Lactobacillus phage phigaY

Inhibitors

Inhibitors Comment Organism Structure
Co(NO3)2 10 mM Lactobacillus phage phigaY
CoCl2 10 mM Lactobacillus phage phigaY
CuSO4 10 mM Lactobacillus phage phigaY
NiSO4 10 mM Lactobacillus phage phigaY
Zn(NO3)2 10 mM Lactobacillus phage phigaY
ZnCl2 10 mM Lactobacillus phage phigaY

Organism

Organism UniProt Comment Textmining
Lactobacillus phage phigaY
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-
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
peptidoglycan + H2O LysgaY lysed over 20 heated Gram-positive bacterial species as the substrates, including lactobacilli, lactococci, enterococci, micrococci, and staphylococci Lactobacillus phage phigaY ?
-
?

Synonyms

Synonyms Comment Organism
endolysin
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Lactobacillus phage phigaY
LysgaY
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Lactobacillus phage phigaY

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
-
Lactobacillus phage phigaY

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.5
-
-
Lactobacillus phage phigaY