scholarly journals Enhanced thermal stability ofClostridium beijerinckiialcohol dehydrogenase after strategic substitution of amino acid residues with prolines from the homologous thermophilicThermoanaerobacter brockiialcohol dehydrogenase

1998 ◽  
Vol 7 (5) ◽  
pp. 1156-1163 ◽  
Author(s):  
Oren Bogin ◽  
Moshe Peretz ◽  
Yael Hacham ◽  
Yigal Burstein ◽  
Yakov Korkhin ◽  
...  
Keyword(s):  
Thermal Stability ◽  
Amino Acid ◽  
Amino Acid Residues

scholarly journals Intrinsic contributions of polar amino acid residues toward thermal stability of an ABC-ATPase of mesophilic origin

2003 ◽  
Vol 12 (9) ◽  
pp. 2118-2120 ◽  
Author(s):  
Jyoti Sarin ◽  
Gajendra P.S. Raghava ◽  
Pradip K. Chakraborti
Keyword(s):  
Thermal Stability ◽  
Amino Acid ◽  
Amino Acid Residues ◽  
Polar Amino Acid ◽  
Thermal Stability Of

scholarly journals Molecular Dynamics Analysis of Glucose Oxidase Stability against Temperature

2021 ◽  
Vol 12 (3) ◽  
pp. 4062-4073
Keyword(s):  
Molecular Dynamics ◽  
Thermal Stability ◽  
Amino Acid ◽  
Glucose Oxidase ◽  
Dynamics Simulation ◽  
Amino Acid Residues ◽  
Widespread Application ◽  
Important Amino Acid ◽  
Ribose Sugar ◽  
Fad Binding

Glucose oxidase (GOD) from local isolated Aspergillus niger IPBCC.08.610 shows a widespread application, specifically as a bioanode in glucose-based biofuel cells. Enzymes with adequate thermal stability are necessary for enhancing product efficiency. Also, evaluating the structural dynamics to improve temperature helps to determine the residue. The molecular dynamics simulation of GOD_IPBCC_1CF3 at temperatures of 300, 400, and 500 K was carried out to analyze important amino acid residues for thermal stability. The results showed that the amino acid residues responsible for thermal stability were dispersed into several essential regions, including D576 at the C terminal, E266-R250, and E38-R237 in the FAD-binding domain E485-R470 in the substrate-binding antiparallel beta system. However, the FAD molecular flexibility against temperature depends on conserve E48 by stabilizing the ribose sugar moiety.

Substrate Recognition by Vitamin K-Dependent Carboxylase

1987 ◽  
Vol 57 (01) ◽  
pp. 017-019 ◽  
Author(s):  
Magda M W Ulrich ◽  
Berry A M Soute ◽  
L Johan M van Haarlem ◽  
Cees Vermeer
Keyword(s):  
Amino Acid ◽  
Vitamin K ◽  
Substrate Recognition ◽  
Bovine Liver ◽  
Amino Acid Residues

SummaryDecarboxylated osteocalcins were prepared and purified from bovine, chicken, human and monkey bones and assayed for their ability to serve as a substrate for vitamin K-dependent carboxylase from bovine liver. Substantial differences were observed, especially between bovine and monkey d-osteocalcin. Since these substrates differ only in their amino acid residues 3 and 4, it seems that these residues play a role in the recognition of a substrate by hepatic carboxylase.

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