Human α-amino-β-carboxymuconate-ε-semialdehyde decarboxylase (ACMSD): A structural and mechanistic unveiling-Reference-Cited by-同舟云学术

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Human α-amino-β-carboxymuconate-ε-semialdehyde decarboxylase (ACMSD): A structural and mechanistic unveiling

Published:2014-11-21 Issue:1 Volume:83 Page:178-187
ISSN:0887-3585
Container-title:Proteins: Structure, Function, and Bioinformatics
language:en
Short-container-title:Proteins

Author:

Huo Lu¹,Liu Fange¹,Iwaki Hiroaki²,Li Tingfeng¹,Hasegawa Yoshie²,Liu Aimin¹

Affiliation:

1. Department of Chemistry and the Center for Diagnostics and Therapeutics; Georgia State University; Atlanta Georgia 30303

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

Funder

National Institute of General Medical Sciences

Georgia Research Alliance

National Science Foundation

Publisher

Wiley

Subject

Molecular Biology,Biochemistry,Structural Biology

Reference38 articles.

1. Kinetic and spectroscopic characterization of ACMSD from Pseudomonas fluorescens reveals a pentacoordinate mononuclear metallocofactor;Li;J Am Chem Soc,2005

2. Detection of transient intermediates in the metal-dependent non-oxidative decarboxylation catalyzed by α-amino-β-carboxymuconic-ε-semialdehyde decarboxylase;Li;J Am Chem Soc,2007

3. The pyridine ring of NAD is formed by a nonenzymatic pericyclic reaction;Colabroy;J Am Chem Soc,2005

4. Uronate isomerase: a nonhydrolytic member of the amidohydrolase superfamily with an ambivalent requirement for a divalent metal ion;Williams;Biochemistry,2006

5. Quinolinic acid: an endogenous metabolite that produces axon-sparing lesions in rat brain;Schwarcz;Science,1983

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