M17 aminopeptidases diversify function by moderating their macromolecular assemblies and active site environment.

Drinkwater, Nyssa; Malcolm, Tess R; McGowan, Sheena

Drinkwater, Nyssa; Malcolm, Tess R; McGowan, Sheena.

Afiliación

Drinkwater N; Biomedicine Discovery Institute, Department of Microbiology, Monash University, Melbourne, VIC, 3800, Australia.
Malcolm TR; Biomedicine Discovery Institute, Department of Microbiology, Monash University, Melbourne, VIC, 3800, Australia.
McGowan S; Biomedicine Discovery Institute, Department of Microbiology, Monash University, Melbourne, VIC, 3800, Australia. Electronic address: sheena.mcgowan@monash.edu.

Biochimie ; 166: 38-51, 2019 Nov.

Article en En | MEDLINE | ID: mdl-30654132

Asunto(s)

Bacterias/enzimología; Eucariontes/enzimología; Leucil Aminopeptidasa/química; Leucil Aminopeptidasa/fisiología; Animales; Dominio Catalítico; Humanos; Metales/metabolismo; Modelos Moleculares; Especificidad por Sustrato

Palabras clave

Cysteinylglycinase; Cytosol aminopeptidase; Leucine aminopeptidase; Leucyl aminopeptidase; M17; Metalloenzyme

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Texto completo: 1 Bases de datos: MEDLINE Asunto principal: Bacterias / Eucariontes / Leucil Aminopeptidasa Tipo de estudio: Prognostic_studies Límite: Animals / Humans Idioma: En Revista: Biochimie Año: 2019 Tipo del documento: Article País de afiliación: Australia

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