The crystal structure of l-lactate oxidase from Aerococcus viridans at 2.1Å resolution reveals the mechanism of strict substrate recognition

2006 ◽  
Vol 350 (2) ◽  
pp. 249-256 ◽  
Author(s):  
Yasufumi Umena ◽  
Kazuko Yorita ◽  
Takeshi Matsuoka ◽  
Akiko Kita ◽  
Kiyoshi Fukui ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Substrate Recognition ◽  
Lactate Oxidase ◽  
Aerococcus Viridans

scholarly journals Crystal structure of ribonuclease A.d(ApTpApApG) complex. Direct evidence for extended substrate recognition.

1994 ◽  
Vol 269 (34) ◽  
pp. 21526-21531 ◽  
Author(s):  
J.C. Fontecilla-Camps ◽  
R. de Llorens ◽  
M.H. le Du ◽  
C.M. Cuchillo
Keyword(s):  
Crystal Structure ◽  
Direct Evidence ◽  
Substrate Recognition

Crystal structure of a family 16 endoglucanase from the hyperthermophile Pyrococcus furiosus- structural basis of substrate recognition

FEBS Journal ◽  
2009 ◽  
Vol 276 (4) ◽  
pp. 1048-1058 ◽  
Author(s):  
Andrea Ilari ◽  
Annarita Fiorillo ◽  
Sebastiana Angelaccio ◽  
Rita Florio ◽  
Roberta Chiaraluce ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Pyrococcus Furiosus ◽  
Substrate Recognition ◽  
Structural Basis

X-ray Structures of Aerococcus viridans Lactate Oxidase and Its Complex with d-Lactate at pH 4.5 Show an α-Hydroxyacid Oxidation Mechanism

2008 ◽  
Vol 378 (2) ◽  
pp. 436-446 ◽  
Author(s):  
Makio Furuichi ◽  
Nobuhiro Suzuki ◽  
Balasundaresan Dhakshnamoorhty ◽  
Hirotaka Minagawa ◽  
Ryosuke Yamagishi ◽  
...  
Keyword(s):  
Oxidation Mechanism ◽  
Lactate Oxidase ◽  
X Ray ◽  
Aerococcus Viridans

scholarly journals Crystal Structure of YaeT: Conformational Flexibility and Substrate Recognition

Structure ◽  
2008 ◽  
Vol 16 (12) ◽  
pp. 1873-1881 ◽  
Author(s):  
Petia Z. Gatzeva-Topalova ◽  
Troy A. Walton ◽  
Marcelo C. Sousa
Keyword(s):  
Crystal Structure ◽  
Substrate Recognition ◽  
Conformational Flexibility

scholarly journals FMN-dependent oligomerization of putative lactate oxidase from Pediococcus acidilactici

2019 ◽  
Author(s):  
Yashwanth Ashok ◽  
Mirko M. Maksimainen ◽  
Tuija Kallio ◽  
Pekka Kilpeläinen ◽  
Lari Lehtiö
Keyword(s):  
Hydrogen Peroxide ◽  
Active Site ◽  
Pediococcus Acidilactici ◽  
Active Site Residues ◽  
Lactate Oxidase ◽  
Monooxygenase Activity ◽  
Aerococcus Viridans ◽  
Lactate Levels

AbstractLactate oxidases belong to a group of FMN-dependent enzymes and they catalyze a conversion of lactate to pyruvate with a release of hydrogen peroxide. Hydrogen peroxide is also utilized as a read out in biosensors to quantitate lactate levels in biological samples. Aerococcus viridans lactate oxidase is the best characterized lactate oxidase and our knowledge of lactate oxidases relies largely to studies conducted with that particular enzyme. Pediococcus acidilactici lactate oxidase is also commercially available for e.g. lactate measurements, but this enzyme has not been characterized before in detail. Here we report structural characterization of the recombinant enzyme and its co-factor dependent oligomerization. The crystal structures revealed two distinct conformations in the loop closing the active site, consistent with previous biochemical studies implicating the role of loop in catalysis. Despite the structural conservation of active site residues when compared to Aerococcus viridans lactate oxidase we were not able to detect either oxidase or monooxygenase activity when L-lactate or other potential alpha hydroxyl acids were used as a substrate. Pediococcus acidilactici lactate oxidase is therefore an example of a misannotation of an FMN-dependent enzyme, which catalyzes likely a so far unknown oxidation reaction.

Crystal structure and substrate recognition mechanism of Aspergillus oryzae isoprimeverose-producing enzyme

2019 ◽  
Vol 205 (1) ◽  
pp. 84-90 ◽  
Author(s):  
Tomohiko Matsuzawa ◽  
Masahiro Watanabe ◽  
Yusuke Nakamichi ◽  
Zui Fujimoto ◽  
Katsuro Yaoi
Keyword(s):  
Crystal Structure ◽  
Aspergillus Oryzae ◽  
Substrate Recognition ◽  
Recognition Mechanism

scholarly journals The first crystal structure of human RNase 6 reveals a novel substrate-binding and cleavage site arrangement

2016 ◽  
Vol 473 (11) ◽  
pp. 1523-1536 ◽  
Author(s):  
Guillem Prats-Ejarque ◽  
Javier Arranz-Trullén ◽  
Jose A. Blanco ◽  
David Pulido ◽  
M. Victòria Nogués ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Molecular Dynamics ◽  
Kinetic Analysis ◽  
Cleavage Site ◽  
Substrate Recognition ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Cleavage Sites ◽  
Human Rnase ◽  
Dynamics Simulations

We describe the first human RNase 6 crystal structure in complex with sulfate anions. Kinetic analysis, site-directed mutagenesis and molecular dynamics simulations identified novel substrate recognition and cleavage sites.

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