Amidase Activity of AmiC Controls Cell Separation and Stem Peptide Release and Is Enhanced by NlpD in Neisseria gonorrhoeae.

Lenz, Jonathan D; Stohl, Elizabeth A; Robertson, Rosanna M; Hackett, Kathleen T; Fisher, Kathryn; Xiong, Kalia; Lee, Mijoon; Hesek, Dusan; Mobashery, Shahriar; Seifert, H Steven; Davies, Christopher; Dillard, Joseph P

Lenz, Jonathan D; Stohl, Elizabeth A; Robertson, Rosanna M; Hackett, Kathleen T; Fisher, Kathryn; Xiong, Kalia; Lee, Mijoon; Hesek, Dusan; Mobashery, Shahriar; Seifert, H Steven; Davies, Christopher; Dillard, Joseph P.

Afiliação

Lenz JD; From the Department of Medical Microbiology and Immunology, University of Wisconsin-Madison, Madison, Wisconsin 53706.
Stohl EA; the Department of Microbiology-Immunology, Northwestern University Feinberg School of Medicine, Chicago, Illinois 60611.
Robertson RM; the Department of Biochemistry and Molecular Biology, Medical University of South Carolina, Charleston, South Carolina 29425, and.
Hackett KT; From the Department of Medical Microbiology and Immunology, University of Wisconsin-Madison, Madison, Wisconsin 53706.
Fisher K; From the Department of Medical Microbiology and Immunology, University of Wisconsin-Madison, Madison, Wisconsin 53706.
Xiong K; From the Department of Medical Microbiology and Immunology, University of Wisconsin-Madison, Madison, Wisconsin 53706.
Lee M; the Department of Chemistry and Biochemistry, University of Notre Dame, South Bend, Indiana 46556.
Hesek D; the Department of Chemistry and Biochemistry, University of Notre Dame, South Bend, Indiana 46556.
Mobashery S; the Department of Chemistry and Biochemistry, University of Notre Dame, South Bend, Indiana 46556.
Seifert HS; the Department of Microbiology-Immunology, Northwestern University Feinberg School of Medicine, Chicago, Illinois 60611.
Davies C; the Department of Biochemistry and Molecular Biology, Medical University of South Carolina, Charleston, South Carolina 29425, and.
Dillard JP; From the Department of Medical Microbiology and Immunology, University of Wisconsin-Madison, Madison, Wisconsin 53706, jpdillard@wisc.edu.

J Biol Chem ; 291(20): 10916-33, 2016 May 13.

Article em En | MEDLINE | ID: mdl-26984407

Assuntos

Proteínas de Bactérias/metabolismo; N-Acetil-Muramil-L-Alanina Amidase/metabolismo; Neisseria gonorrhoeae/metabolismo; Substituição de Aminoácidos; Proteínas de Bactérias/química; Proteínas de Bactérias/genética; Domínio Catalítico/genética; Cátions Bivalentes/metabolismo; Ativação Enzimática; Humanos; N-Acetil-Muramil-L-Alanina Amidase/química; N-Acetil-Muramil-L-Alanina Amidase/genética; Neisseria gonorrhoeae/genética; Neisseria gonorrhoeae/patogenicidade; Peptidoglicano/química; Peptidoglicano/metabolismo; Domínios e Motivos de Interação entre Proteínas; Especificidade por Substrato

Palavras-chave

Gram-negative bacteria; NOD-like receptor (NLR); Neisseria gonorrhoeae; amidase; cell separation; cell wall; infectious disease; pathogen-associated molecular pattern (PAMP); peptidoglycan

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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Proteínas de Bactérias / N-Acetil-Muramil-L-Alanina Amidase / Neisseria gonorrhoeae Limite: Humans Idioma: En Ano de publicação: 2016 Tipo de documento: Article

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