scholarly journals Structure and function of yeast alcohol dehydrogenase

2000 ◽  
Vol 65 (4) ◽  
pp. 207-227 ◽  
Author(s):  
Svetlana Trivic ◽  
Vladimir Leskovac

1. Introduction 2. Isoenzymes of YADH 3. Substrate specificity 4. Kinetic mechanism 5. Primary structure 6. The active site 7. Mutations in the yeast enzyme 8. Chemical mechanism 9. Binding of coenzymes 10. Hydride transfer <br><br><font color="red"><b> This article has been corrected. Link to the correction <u><a href="http://dx.doi.org/10.2298/JSC0008609E">10.2298/JSC0008609E</a><u></b></font>

2000 ◽  
Vol 65 (8) ◽  
pp. 609-609
Author(s):  
E Editorial

Erratum In the paper entitled "Structure and Function of Yeast Alcohol Dehydrogenase" by Svetlana Trivic and Vladimir Leskovac published in J. Serb. Chem. Soc. Vol. 65. No. 4 (2000) Table 5 on page 213 should be replaced with: TABLE V. Primary structure of the three isoenzymes of yeast alcohol dehydrogenase. <br><br><font color="red"><b> Link to the corrected article <u><a href="http://dx.doi.org/10.2298/JSC0004207T">10.2298/JSC0004207T</a></b></u>


Author(s):  
Xavier Parés ◽  
Jaume Farrés ◽  
Alberto Moreno ◽  
Narcís Saubi ◽  
M. Dolors Boleda ◽  
...  

2015 ◽  
Vol 5 (1) ◽  
Author(s):  
A.E. Naas ◽  
A.K. MacKenzie ◽  
B. Dalhus ◽  
V.G.H. Eijsink ◽  
P.B. Pope

Abstract Previous gene-centric analysis of a cow rumen metagenome revealed the first potentially cellulolytic polysaccharide utilization locus, of which the main catalytic enzyme (AC2aCel5A) was identified as a glycoside hydrolase (GH) family 5 endo-cellulase. Here we present the 1.8 Å three-dimensional structure of AC2aCel5A and characterization of its enzymatic activities. The enzyme possesses the archetypical (β/α)8-barrel found throughout the GH5 family and contains the two strictly conserved catalytic glutamates located at the C-terminal ends of β-strands 4 and 7. The enzyme is active on insoluble cellulose and acts exclusively on linear β-(1,4)-linked glucans. Co-crystallization of a catalytically inactive mutant with substrate yielded a 2.4 Å structure showing cellotriose bound in the −3 to −1 subsites. Additional electron density was observed between Trp178 and Trp254, two residues that form a hydrophobic “clamp”, potentially interacting with sugars at the +1 and +2 subsites. The enzyme’s active-site cleft was narrower compared to the closest structural relatives, which in contrast to AC2aCel5A, are also active on xylans, mannans and/or xyloglucans. Interestingly, the structure and function of this enzyme seem adapted to less-substituted substrates such as cellulose, presumably due to the insufficient space to accommodate the side-chains of branched glucans in the active-site cleft.


Author(s):  
Brian M. Hoffman ◽  
Victoria J. DeRose ◽  
Peter E. Doan ◽  
Ryszard J. Gurbiel ◽  
Andrew L. P. Houseman ◽  
...  

2008 ◽  
Vol 281 (1) ◽  
pp. 10-16 ◽  
Author(s):  
Hitoshi Tsugawa ◽  
Asako Ogawa ◽  
Satomi Takehara ◽  
Mayumi Kimura ◽  
Yoshio Okawa

Biochemistry ◽  
1992 ◽  
Vol 31 (8) ◽  
pp. 2294-2298 ◽  
Author(s):  
Verena Steiner ◽  
Rene Knecht ◽  
K. Olaf Boernsen ◽  
Ernst Gassmann ◽  
Stuart R. Stone ◽  
...  

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