scholarly journals Protein engineering of the aldoxime dehydratase from Bacillus sp. OxB-1 based on a rational sequence alignment approach

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Keiko Oike ◽  
Jens Sproß ◽  
Daisuke Matsui ◽  
Yasuhisa Asano ◽  
Harald Gröger
Keyword(s):  
Amino Acid ◽  
Secondary Structure ◽  
Amino Acid Sequence ◽  
Enzymatic Activity ◽  
Structure Data ◽  
Single Mutation ◽  
Bacillus Sp ◽  
Activity Increase ◽  
Aldoxime Dehydratase ◽  
Rational Sequence

AbstractRecently, the program INTMSAlign_HiSol for identifying aggregation hotspots in proteins only requiring secondary structure data was introduced. We explored the utility of this program further and applied it for engineering of the aldoxime dehydratase from Bacillus sp. OxB-1. Towards this end, the effect of inverting the hydropathy at selected positions of the amino acid sequence on the enzymatic activity was studied leading to 60% of our constructed variants, which showed improved activity. In part, this activity increase can be rationalised by an improved heme incorporation of the variants. For example, a single mutation gave a 1.8 fold increased enzymatic activity and 30% improved absolute heme incorporation.

Shark Myelin Basic Protein: Amino Acid Sequence, Secondary Structure, and Self-Association

1990 ◽  
Vol 55 (3) ◽  
pp. 950-955 ◽  
Author(s):  
Trudy J. Milne ◽  
Annette R. Atkins ◽  
Juanita A. Warren ◽  
Wendy P. Auton ◽  
Ross Smith
Keyword(s):  
Amino Acid ◽  
Secondary Structure ◽  
Amino Acid Sequence ◽  
Myelin Basic Protein ◽  
Basic Protein ◽  
Protein Amino Acid ◽  
Protein Amino Acid Sequence ◽  
Self Association

scholarly journals Partial amino acid sequence of protease I produced by Bacillus sp. 11-4 isolated from Vietnamese fish sauces

2003 ◽  
Vol 29 (1) ◽  
pp. 25-31 ◽  
Author(s):  
Yoshitaka NISHIYAMA ◽  
Haruko MAEDA ◽  
Toshio NAGASHIMA ◽  
Toshihiro WATANABE ◽  
Kiyoshi MURA
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Bacillus Sp ◽  
Partial Amino Acid Sequence

Amino acid sequence restriction in relation to proteolysis

1983 ◽  
Vol 3 (3) ◽  
pp. 225-232 ◽  
Author(s):  
Hans Jórnvall ◽  
Bengt Persson
Keyword(s):  
Amino Acid ◽  
Secondary Structure ◽  
Amino Acid Sequence ◽  
Distribution Patterns ◽  
Amino Acid Residues ◽  
Individual Protein ◽  
Proteolytic Cleavages ◽  
N Proteins

Distributions of amino acid residues in proteins show that proline is overrepresented in sequence positions following two basic residues ({LysArg}−{LysArg}), i.e. at sites similar to those susceptible to proteolytic cleavages of hormonal pro-forms. Conformational correlations further show that {LysArg}−{LysArg}-Pro sequences are often (8/11) not adiacent to elements of secondary structure, whereas the opposite applies to {LysArg}−{LysArg}-nonPro sequences (82/103 adjacent to elements of secondary structure). These distribution patterns from proteins in general also seem applicable in individual protein groups as demonstrated for some dehydrogenases. It appears possible that {LysArg}−{LysArg}-nonPro constitutes a restricted sequence, n proteins, and that proline, in addition to elements of secondary structure, contributes a means of avoiding unacceptable proteolytic processings of proteins in general.

Highly alkaline pectate lyase Pel-4A from alkaliphilic Bacillus sp. strain P-4-N: its catalytic properties and deduced amino acid sequence

Extremophiles ◽  
2000 ◽  
Vol 4 (6) ◽  
pp. 377-383 ◽  
Author(s):  
Tohru Kobayashi ◽  
Yuji Hatada ◽  
Atsushi Suzumatsu ◽  
Katsuhisa Saeki ◽  
Yoshihiro Hakamada ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Catalytic Properties ◽  
Pectate Lyase ◽  
Bacillus Sp ◽  
Alkaliphilic Bacillus ◽  
Alkaline Pectate Lyase

scholarly journals Human cardiac troponin I: precise identification of antigenic epitopes and prediction of secondary structure

1998 ◽  
Vol 44 (3) ◽  
pp. 487-493 ◽  
Author(s):  
Gaelle Ferrieres ◽  
Charles Calzolari ◽  
Jean-Claude Mani ◽  
Daniel Laune ◽  
Sylvie Trinquier ◽  
...  
Keyword(s):  
Myocardial Infarction ◽  
Monoclonal Antibodies ◽  
Amino Acid ◽  
Secondary Structure ◽  
Amino Acid Sequence ◽  
Cardiac Troponin ◽  
Troponin I ◽  
Cardiac Troponin I ◽  
Peptide Epitope ◽  
Antigenic Properties

Abstract The presence of human cardiac troponin I (hcTnI) in serum is considered to be a highly specific biochemical marker of acute myocardial infarction. To better understand the antigenic properties of hcTnI, a set of 68 overlapping peptides covering the complete amino acid sequence of hcTnI was prepared and used in epitope mapping experiments. All 16 anti-hcTnI monoclonal antibodies tested were found to recognize a peptide epitope, indicating that recognition by anti-hcTnI monoclonal antibodies was not dependent on the tertiary structure of the protein. Furthermore, the peptide reactivity with anti-hcTnI polyclonal antibodies indicated that most of the sequence of the protein was antigenic; in particular, the N- and C-terminal extremities were found to be the strongest antigenic regions. By using accurate secondary structure prediction methods, hcTnI was found to be an all-alpha type protein, with five regions predicted as helices. Matching the results of the epitope analysis with the structural prediction led us to the view that hcTnI is not a globular protein but probably adopts an extended conformation, allowing a large part of the amino acid sequence of this molecule to be recognized by the immune system. This improved knowledge of the antigenic and structural properties of hcTnI may help in developing new antibodies and immunoassays for use in diagnosing myocardial infarction.

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