Protocatechuate 3,4-Dioxygenase: A Wide Substrate Specificity Enzyme Isolated from Stenotrophomonas maltophilia KB2 as a Useful Tool in Aromatic Acid Biodegradation

2014 ◽  
Vol 24 (3) ◽  
pp. 150-160 ◽  
Author(s):  
Urszula Guzik ◽  
Katarzyna Hupert-Kocurek ◽  
Małgorzata Sitnik ◽  
Danuta Wojcieszyńska
Keyword(s):  
Substrate Specificity ◽  
Stenotrophomonas Maltophilia ◽  
Aromatic Acid ◽  
Wide Substrate Specificity

scholarly journals Analysis of Sequence Divergence in Mammalian ABCGs Predicts a Structural Network of Residues That Underlies Functional Divergence

2021 ◽  
Vol 22 (6) ◽  
pp. 3012
Author(s):  
James I. Mitchell-White ◽  
Thomas Stockner ◽  
Nicholas Holliday ◽  
Stephen J. Briddon ◽  
Ian D. Kerr
Keyword(s):  
Substrate Specificity ◽  
Functional Divergence ◽  
3D Structure ◽  
Sequence Divergence ◽  
Conformational Flexibility ◽  
Substrate Selectivity ◽  
Multiple Sequence ◽  
Atp Binding Cassette Transporters ◽  
Structural Network ◽  
Wide Substrate Specificity

The five members of the mammalian G subfamily of ATP-binding cassette transporters differ greatly in their substrate specificity. Four members of the subfamily are important in lipid transport and the wide substrate specificity of one of the members, ABCG2, is of significance due to its role in multidrug resistance. To explore the origin of substrate selectivity in members 1, 2, 4, 5 and 8 of this subfamily, we have analysed the differences in conservation between members in a multiple sequence alignment of ABCG sequences from mammals. Mapping sets of residues with similar patterns of conservation onto the resolved 3D structure of ABCG2 reveals possible explanations for differences in function, via a connected network of residues from the cytoplasmic to transmembrane domains. In ABCG2, this network of residues may confer extra conformational flexibility, enabling it to transport a wider array of substrates.

Reshaping the Active Pocket of Esterase Est816 for Resolution of Economically Important Racemates

2021 ◽  
Author(s):  
Xiaolong Liu ◽  
Meng Zhao ◽  
Xinjiong Fan ◽  
Yao Fu
Keyword(s):  
Substrate Specificity ◽  
Industrial Applications ◽  
Pure Compounds ◽  
Optically Pure ◽  
Wide Substrate Specificity

One of the most important industrial applications of bacterial esterases is the production of optically pure compounds. However, the contradiction between the wide substrate specificity and high enantioselectivity of natural...

scholarly journals Earthworm Protease

2010 ◽  
Vol 2010 ◽  
pp. 1-13 ◽  
Author(s):  
Rong Pan ◽  
Zi-Jian Zhang ◽  
Rong-Qiao He
Keyword(s):  
Substrate Specificity ◽  
Protein Function ◽  
Eisenia Fetida ◽  
Alimentary Tract ◽  
Protein Crystal ◽  
Lumbricus Rubellus ◽  
Earthworm Species ◽  
Tumor Study ◽  
New Applications ◽  
Wide Substrate Specificity

The alimentary tract of earthworm secretes a group of proteases with a relative wide substrate specificity. In 1983, six isozymes were isolated from earthworm with fibrinolytic activities and called fibriniolytic enzymes. So far, more isozymes have been found from different earthworm species such asLumbricus rubellusandEisenia fetida. For convenience, the proteases are named on the basis of the earthworm species and the protein function, for instance,Eisenia fetidaprotease (EfP). The proteases have the abilities not only to hydrolyze fibrin and other protein, but also activate proenzymes such as plasminogen and prothrombin. In the light of recent studies, eight of theEfPs contain oligosaccharides chains which are thought to support the enzyme structure. Interestingly,EfP-II has a broader substrate specificity presenting alkaline trypsin, chymotrypsin and elastase activities, butEfP-III-1 has a stricter specificity. The protein crystal structures show the characteristics in their specificities. Earthworm proteases have been applied in several areas such as clinical treatment of clotting diseases, anti-tumor study, environmental protection and nutritional production. The current clinical utilizations and some potential new applications of the earthworm protease will be discussed in this paper.

scholarly journals The Pseudomonas cellulosa glycoside hydrolase family 51 arabinofuranosidase exhibits wide substrate specificity

2001 ◽  
Vol 358 (3) ◽  
pp. 607 ◽  
Author(s):  
Marie-Helene BEYLOT ◽  
Vincent A. McKIE ◽  
Alphons G.J. VORAGEN ◽  
Chantal H.L. DOESWIJK-VORAGEN ◽  
Harry J. GILBERT
Keyword(s):  
Substrate Specificity ◽  
Glycoside Hydrolase ◽  
Glycoside Hydrolase Family ◽  
Hydrolase Family ◽  
Glycoside Hydrolase Family 51 ◽  
Wide Substrate Specificity

scholarly journals Unexpected wide substrate specificity of C. perfringens α-toxin phospholipase C

2011 ◽  
Vol 1808 (10) ◽  
pp. 2618-2627 ◽  
Author(s):  
Patricia Urbina ◽  
M. Isabel Collado ◽  
Alicia Alonso ◽  
Félix M. Goñi ◽  
Marietta Flores-Díaz ◽  
...  
Keyword(s):  
Substrate Specificity ◽  
Phospholipase C ◽  
Wide Substrate Specificity
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