Purification, characterization, and genetic analysis of a leucine aminopeptidase from Aspergillus sojae-Reference-Cited by-同舟云学术

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Purification, characterization, and genetic analysis of a leucine aminopeptidase from Aspergillus sojae

Published:2002-06 Issue:1-2 Volume:1576 Page:119-126
ISSN:0167-4781
Container-title:Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression
language:en
Short-container-title:Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression

Author:

Chien Hung-Chien Roger,Lin Long-Liu,Chao Shiou-Huei,Chen Chun-Chang,Wang Wen-Ching,Shaw Chin-Ying,Tsai Ying-Chie,Hu Hui-Yu,Hsu Wen-Hwei

Publisher

Elsevier BV

Subject

Genetics,Biochemistry,Biophysics,Structural Biology

Reference52 articles.

1. Two-Metal Ion Mechanism of Bovine Lens Leucine Aminopeptidase: Active Site Solvent Structure and Binding Mode of L-Leucinal, a gem-Diolate Transition State Analog, by X-ray Crystallography

2. Transition State Analog L-Leucinephosphonic Acid Bound to Bovine Lens Leucine Aminopeptidase: X-ray Structure at 1.65 .ANG. Resolution in a New Crystal Form

3. Identification and quantification of leucine aminopeptidase in aged normal and cataractous human lenses and ability of bovine lens LAP to cleave bovine crystallins

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3. The role of propeptide-mediated autoinhibition and intermolecular chaperone in the maturation of cognate catalytic domain in leucine aminopeptidase;Journal of Structural Biology;2021-09

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