Evidence for a Dual Role of an Active Site Histidine in α-Amino-β-carboxymuconate-ε-semialdehyde Decarboxylase-Reference-Cited by-同舟云学术

Evidence for a Dual Role of an Active Site Histidine in α-Amino-β-carboxymuconate-ε-semialdehyde Decarboxylase

Published:2012-07-12 Issue:29 Volume:51 Page:5811-5821
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Huo Lu¹,Fielding Andrew J.²,Chen Yan¹,Li Tingfeng³,Iwaki Hiroaki⁴,Hosler Jonathan P.³,Chen Lirong¹,Hasegawa Yoshie⁴,Que Lawrence²,Liu Aimin¹³

Affiliation:

1. Department of Chemistry and Center for Diagnostics and Therapeutics, Georgia State University, P.O. Box 4098, Atlanta, Georgia 30303, United States

2. Department of Chemistry and Center for Metals in Biocatalysis, University of Minnesota, 207 Pleasant Street, Minneapolis, Minnesota 55455, United States

3. Department of Biochemistry, University of Mississippi Medical Center, Jackson, Mississippi 39216, United States

4. Department of Life Science and Biotechnology and ORDIST, Kansai University, Suita, Osaka 564-8680, Japan

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi300635b

Reference74 articles.

1. On the structure of histidine and its role in enzyme active sites

2. Structural and Catalytic Diversity within the Amidohydrolase Superfamily

3. Kinetic and Spectroscopic Characterization of ACMSD from Pseudomonas fluorescens Reveals a Pentacoordinate Mononuclear Metallocofactor

4. α-Amino-β-carboxymuconic-ε-semialdehyde Decarboxylase (ACMSD) Is a New Member of the Amidohydrolase Superfamily

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