scholarly journals Ligand-binding specificity and promiscuity of the main lignocellulolytic enzyme families as revealed by active-site architecture analysis

2016 ◽  
Vol 6 (1) ◽  
Author(s):  
Li Tian ◽  
Shijia Liu ◽  
Shuai Wang ◽  
Lushan Wang
Keyword(s):  
Ligand Binding ◽  
Active Site ◽  
Binding Specificity ◽  
Enzyme Families ◽  
Architecture Analysis

Substrate-binding specificity of chitinase and chitosanase as revealed by active-site architecture analysis

2015 ◽  
Vol 418 ◽  
pp. 50-56 ◽  
Author(s):  
Shijia Liu ◽  
Shangjin Shao ◽  
Linlin Li ◽  
Zhi Cheng ◽  
Li Tian ◽  
...  
Keyword(s):  
Active Site ◽  
Substrate Binding ◽  
Binding Specificity ◽  
Architecture Analysis

scholarly journals Crystal Structure, Exogenous Ligand Binding, and Redox Properties of an Engineered Diiron Active Site in a Bacterial Hemerythrin

2013 ◽  
Vol 52 (22) ◽  
pp. 13014-13020 ◽  
Author(s):  
Yasunori Okamoto ◽  
Akira Onoda ◽  
Hiroshi Sugimoto ◽  
Yu Takano ◽  
Shun Hirota ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Ligand Binding ◽  
Active Site ◽  
Redox Properties ◽  
Exogenous Ligand

scholarly journals Myelin 2′,3′-Cyclic Nucleotide 3′-Phosphodiesterase: Active-Site Ligand Binding and Molecular Conformation

PLoS ONE ◽  
2012 ◽  
Vol 7 (2) ◽  
pp. e32336 ◽  
Author(s):  
Matti Myllykoski ◽  
Arne Raasakka ◽  
Huijong Han ◽  
Petri Kursula
Keyword(s):  
Ligand Binding ◽  
Active Site ◽  
Cyclic Nucleotide ◽  
Molecular Conformation

scholarly journals Structural comparisons lead to the definition of a new superfamily of NAD(P)(H)-accepting oxidoreductases: the single-domain reductases/epimerases/dehydrogenases (the ‘RED’ family)

1994 ◽  
Vol 304 (1) ◽  
pp. 95-99 ◽  
Author(s):  
G Labesse ◽  
A Vidal-Cros ◽  
J Chomilier ◽  
M Gaudry ◽  
J P Mornon
Keyword(s):  
Amino Acids ◽  
Sequence Alignment ◽  
Active Site ◽  
Tertiary Structure ◽  
Binding Specificity ◽  
Single Domain ◽  
Divergent Evolution ◽  
Cofactor Binding ◽  
Sequence Identity ◽  
Definition Of

Using both primary- and tertiary-structure comparisons, we have established new structural similarities shared by reductases, epimerases and dehydrogenases not previously known to be related. Despite the low sequence identity (down to 10%), short consensus segments are identified. We show that the sequence, the active site and the supersecondary structure are well conserved in these proteins. New homologues (the protochlorophyllide reductases) are detected, and we define a new superfamily composed of single-domain dinucleotide-binding enzymes. Rules for the cofactor-binding specificity are deduced from our sequence alignment. The involvement of some amino acids in catalysis is discussed. Comparison with two-domain dehydrogenases allows us to distinguish two general mechanisms of divergent evolution.

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