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Literature summary for 3.4.21.12 extracted from

  • Kudryakova, I.V.; Gabdulkhakov, A.G.; Tishchenko, S.V.; Lysanskaya, V.Y.; Suzina, N.E.; Tsfasman, I.M.; Afoshin, A.S.; Vasilyeva, N.V.
    Structural and functional properties of antimicrobial protein L5 of Lysobacter sp. XL1 (2018), Appl. Microbiol. Biotechnol., 102, 10043-10053 .
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21(DE3) cells Lysobacter sp. XL1

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging drop vapor diffusion method, using 2.7 M sodium formate and 0.01 M PIPES, at pH 7.0 Lysobacter sp. XL1

Localization

Localization Comment Organism GeneOntology No. Textmining
vesicle
-
Lysobacter sp. XL1 31982
-

Organism

Organism UniProt Comment Textmining
Lysobacter sp. XL1 D2K8B4 VKM B-1576
-

Purification (Commentary)

Purification (Comment) Organism
His Trap column chromatography and Enrich S column chromatography Lysobacter sp. XL1

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Abz-Ala-Ala-Phe-4-nitroanilide + H2O
-
Lysobacter sp. XL1 Abz-Ala-Ala-Phe + 4-nitroaniline
-
?
Staphylococcus aureus peptidoglycan + H2O the enzyme possesses a Gly-Gly endopeptidase activity with respect to staphylococcal peptidoglycan and an amidase that manifests an N-acetylmuramoyl-L-Ala amidase activity with respect to this substrate Lysobacter sp. XL1 ?
-
?

Synonyms

Synonyms Comment Organism
alpha-lytic protease
-
Lysobacter sp. XL1
bacteriolytic protease L5
-
Lysobacter sp. XL1
protein L5
-
Lysobacter sp. XL1