Analysis of Mammalian Histidine Decarboxylase Dimerization Interface Reveals an Electrostatic Hotspot Important for Catalytic Site Topology and Function-Reference-Cited by-同舟云学术

Analysis of Mammalian Histidine Decarboxylase Dimerization Interface Reveals an Electrostatic Hotspot Important for Catalytic Site Topology and Function

Published:2011-05-13 Issue:6 Volume:7 Page:1935-1942
ISSN:1549-9618
Container-title:Journal of Chemical Theory and Computation
language:en
Short-container-title:J. Chem. Theory Comput.

Author:

Moya-García Aurelio A.¹²,Rodríguez-Agudo Daniel¹,Hayashi Hideyuki³,Medina Miguel Angel¹²,Urdiales José Luis¹²,Sánchez-Jiménez Francisca¹²

Affiliation:

1. Departamento de Biología Molecular y Bioquímica, Facultad de Ciencias, Campus de Teatinos, Universidad de Málaga, Málaga, Spain

2. CIBER de Enfermedades Raras (CIBERER), Málaga, Spain

3. Department of Biochemistry, Osaka Medical College, Takatsuki, Osaka 569-8686, Japan

Publisher

American Chemical Society (ACS)

Subject

Physical and Theoretical Chemistry,Computer Science Applications

Link

https://pubs.acs.org/doi/pdf/10.1021/ct100690p

Reference38 articles.

1. Purification and Characterization of L-Histidine Decarboxylase from Mouse Mastocytoma P-815 Cells

2. Purification of histidine decarboxylase from the liver of fetal rats and its immunochemical and immunohistochemical characterization.

3. The Production of 53–55-kDa Isoforms Is Not Required for Ratl-Histidine Decarboxylase Activity

4. Spectroscopic Analysis of Recombinant Rat Histidine Decarboxylase

5. Analysis of the Decarboxylation Step in Mammalian Histidine Decarboxylase

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