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Literature summary 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)

EC Number Cloned (Comment) Organism
3.2.1.17
-
 Lactobacillus phage phigaY

Protein Variants

EC Number Protein Variants Comment Organism
3.2.1.17 D12A cell-lytic activity is strongly reduced Lactobacillus phage phigaY
3.2.1.17 D12A/E33A no cell-lytic activity Lactobacillus phage phigaY
3.2.1.17 D12G cell-lytic activity isstrongly reduced Lactobacillus phage phigaY
3.2.1.17 D198A cell-lytic activity is slightly reduced Lactobacillus phage phigaY
3.2.1.17 D36A cell-lytic activity is similar to wild-type enzyme Lactobacillus phage phigaY
3.2.1.17 D96A cell-lytic activity is strongly reduced Lactobacillus phage phigaY
3.2.1.17 E237A cell-lytic activity is similar to wild-type enzyme Lactobacillus phage phigaY
3.2.1.17 E238A cell-lytic activity is similar to wild-type enzyme Lactobacillus phage phigaY
3.2.1.17 E33A cell-lytic activity isstrongly reduced Lactobacillus phage phigaY
3.2.1.17 E88D cell-lytic activity is similar to wild-type enzyme Lactobacillus phage phigaY
3.2.1.17 E98A no cell-lytic activity Lactobacillus phage phigaY
3.2.1.17 G10S cell-lytic activity is strongly reduced Lactobacillus phage phigaY
3.2.1.17 G253A cell-lytic activity is similar to wild-type enzyme Lactobacillus phage phigaY
3.2.1.17 G267A cell-lytic activity is similar to wild-type enzyme Lactobacillus phage phigaY
3.2.1.17 G281A cell-lytic activity is similar to wild-type enzyme Lactobacillus phage phigaY
3.2.1.17 G292A cell-lytic activity is similar to wild-type enzyme Lactobacillus phage phigaY
3.2.1.17 H60R cell-lytic activity is strongly reduced Lactobacillus phage phigaY
3.2.1.17 K142E cell-lytic activity is similar to wild-type enzyme Lactobacillus phage phigaY
3.2.1.17 K142R cell-lytic activity is similar to wild-type enzyme Lactobacillus phage phigaY
3.2.1.17 K207A cell-lytic activity is similar to wild-type enzyme Lactobacillus phage phigaY
3.2.1.17 K211A cell-lytic activity is similar to wild-type enzyme Lactobacillus phage phigaY
3.2.1.17 K25T cell-lytic activity is similar to wild-type enzyme Lactobacillus phage phigaY
3.2.1.17 L132P cell-lytic activity is strongly reduced Lactobacillus phage phigaY
3.2.1.17 L264A cell-lytic activity is slightly reduced Lactobacillus phage phigaY
3.2.1.17 M1I cell-lytic activity is reduced Lactobacillus phage phigaY
3.2.1.17 M1K cell-lytic activity is reduced Lactobacillus phage phigaY
3.2.1.17 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
3.2.1.17 N67K cell-lytic activity is similar to wild-type enzyme Lactobacillus phage phigaY
3.2.1.17 P212A cell-lytic activity is similar to wild-type enzyme Lactobacillus phage phigaY
3.2.1.17 P216A cell-lytic activity is similar to wild-type enzyme Lactobacillus phage phigaY
3.2.1.17 R109L cell-lytic activity is similar to wild-type enzyme Lactobacillus phage phigaY
3.2.1.17 R251A cell-lytic activity is slightly reduced Lactobacillus phage phigaY
3.2.1.17 V124M cell-lytic activity is slightly reduced Lactobacillus phage phigaY
3.2.1.17 V79F cell-lytic activity is similar to wild-type enzyme Lactobacillus phage phigaY
3.2.1.17 W284A cell-lytic activity is strongly reduced Lactobacillus phage phigaY
3.2.1.17 W284G cell-lytic activity is strongly reduced Lactobacillus phage phigaY
3.2.1.17 Y272A cell-lytic activity is strongly reduced Lactobacillus phage phigaY
3.2.1.17 Y61H cell-lytic activity is stronly reduced Lactobacillus phage phigaY

Inhibitors

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

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.17 Lactobacillus phage phigaY
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.17 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

EC Number Synonyms Comment Organism
3.2.1.17 endolysin
-
 Lactobacillus phage phigaY
3.2.1.17 LysgaY
-
 Lactobacillus phage phigaY

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.17 37
-
-
 Lactobacillus phage phigaY

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.17 6.5
-
-
 Lactobacillus phage phigaY