Mechanisms of peptide hydrolysis by aspartyl and metalloproteases
Peptide hydrolysis has been involved in a wide range of biological, biotechnological, and industrial applications. In this perspective, the mechanisms of three distinct peptide bond cleaving enzymes, beta secretase (BACE1), insulin degrading enzyme (IDE), and bovine lens leucine aminopeptidase (BILA...
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| Veröffentlicht in: | Physical chemistry chemical physics : PCCP 2016-09, Vol.18 (36), p.2479-2481 |
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| container_title | Physical chemistry chemical physics : PCCP |
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| creator | Paul, Thomas J Barman, Arghya Ozbil, Mehmet Bora, Ram Prasad Zhang, Tingting Sharma, Gaurav Hoffmann, Zachary Prabhakar, Rajeev |
| description | Peptide hydrolysis has been involved in a wide range of biological, biotechnological, and industrial applications. In this perspective, the mechanisms of three distinct peptide bond cleaving enzymes, beta secretase (BACE1), insulin degrading enzyme (IDE), and bovine lens leucine aminopeptidase (BILAP), have been discussed. BACE1 is a catalytic Asp dyad [Asp, Asp
−
] containing aspartyl protease, while IDE and BILAP are mononuclear [Zn(His, His, Glu)] and binuclear [Zn1(Asp, Glu, Asp)-Zn2(Lys, Glu, Asp, Asp)] core possessing metallopeptidases, respectively. Specifically, enzyme-substrate interactions and the roles of metal ion(s), the ligand environment, second coordination shell residues, and the protein environment in the functioning of these enzymes have been elucidated. This information will be useful to design small inhibitors, activators, and synthetic analogues of these enzymes for biomedical, biotechnological, and industrial applications.
Peptide hydrolysis has been involved in a wide range of biological, biotechnological, and industrial applications. |
| doi_str_mv | 10.1039/c6cp02097f |
| format | Article |
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−
] containing aspartyl protease, while IDE and BILAP are mononuclear [Zn(His, His, Glu)] and binuclear [Zn1(Asp, Glu, Asp)-Zn2(Lys, Glu, Asp, Asp)] core possessing metallopeptidases, respectively. Specifically, enzyme-substrate interactions and the roles of metal ion(s), the ligand environment, second coordination shell residues, and the protein environment in the functioning of these enzymes have been elucidated. This information will be useful to design small inhibitors, activators, and synthetic analogues of these enzymes for biomedical, biotechnological, and industrial applications.
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−
] containing aspartyl protease, while IDE and BILAP are mononuclear [Zn(His, His, Glu)] and binuclear [Zn1(Asp, Glu, Asp)-Zn2(Lys, Glu, Asp, Asp)] core possessing metallopeptidases, respectively. Specifically, enzyme-substrate interactions and the roles of metal ion(s), the ligand environment, second coordination shell residues, and the protein environment in the functioning of these enzymes have been elucidated. This information will be useful to design small inhibitors, activators, and synthetic analogues of these enzymes for biomedical, biotechnological, and industrial applications.
Peptide hydrolysis has been involved in a wide range of biological, biotechnological, and industrial applications.</description><subject>Amyloid Precursor Protein Secretases - chemistry</subject><subject>Amyloid Precursor Protein Secretases - metabolism</subject><subject>Animals</subject><subject>Biocatalysis</subject><subject>Catalytic Domain</subject><subject>Cattle</subject><subject>Enzymes</subject><subject>Hydrolysis</subject><subject>Industrial applications</subject><subject>Insulysin - chemistry</subject><subject>Insulysin - metabolism</subject><subject>Leucine</subject><subject>Leucyl Aminopeptidase - chemistry</subject><subject>Leucyl Aminopeptidase - metabolism</subject><subject>Ligands</subject><subject>Peptides</subject><subject>Peptides - chemistry</subject><subject>Peptides - metabolism</subject><subject>Physical chemistry</subject><subject>Protein Structure, Tertiary</subject><subject>Residues</subject><subject>Thermodynamics</subject><subject>Zinc - chemistry</subject><issn>1463-9076</issn><issn>1463-9084</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2016</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqF0cFLwzAUBvAgipvTi3elRxGqL03TNMdRnAoTPei5pOkLq7RrzesO_e9X3ZxHTwnkx_d4Xxi75HDHQeh7m9gOItDKHbEpjxMRakjj48NdJRN2RvQJAFxyccomkVKcCyWmbP6CdmXWFTUUtC7osOurEoPVUPq2HqiioBgCQ53x_VAHZl0GDfamrtvOtz0aQjpnJ87UhBf7c8Y-Fg_v2VO4fH18zubL0Aql-5BLAzwxSkKkjFFlHGkLUuoiKmJuY7TSOZk6V1hwBddYaif0aJwUSRyhEzN2s8sdJ39tkPq8qchiXZs1thvKuYY44um44P80FWMqKJAjvd1R61sijy7vfNUYP-Qc8u928yzJ3n7aXYz4ep-7KRosD_S3zhFc7YAne3j9-x6xBbkofrI</recordid><startdate>20160914</startdate><enddate>20160914</enddate><creator>Paul, Thomas J</creator><creator>Barman, Arghya</creator><creator>Ozbil, Mehmet</creator><creator>Bora, Ram Prasad</creator><creator>Zhang, Tingting</creator><creator>Sharma, Gaurav</creator><creator>Hoffmann, Zachary</creator><creator>Prabhakar, Rajeev</creator><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><scope>7SR</scope><scope>7U5</scope><scope>8BQ</scope><scope>8FD</scope><scope>JG9</scope><scope>L7M</scope></search><sort><creationdate>20160914</creationdate><title>Mechanisms of peptide hydrolysis by aspartyl and metalloproteases</title><author>Paul, Thomas J ; 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In this perspective, the mechanisms of three distinct peptide bond cleaving enzymes, beta secretase (BACE1), insulin degrading enzyme (IDE), and bovine lens leucine aminopeptidase (BILAP), have been discussed. BACE1 is a catalytic Asp dyad [Asp, Asp
−
] containing aspartyl protease, while IDE and BILAP are mononuclear [Zn(His, His, Glu)] and binuclear [Zn1(Asp, Glu, Asp)-Zn2(Lys, Glu, Asp, Asp)] core possessing metallopeptidases, respectively. Specifically, enzyme-substrate interactions and the roles of metal ion(s), the ligand environment, second coordination shell residues, and the protein environment in the functioning of these enzymes have been elucidated. This information will be useful to design small inhibitors, activators, and synthetic analogues of these enzymes for biomedical, biotechnological, and industrial applications.
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| ispartof | Physical chemistry chemical physics : PCCP, 2016-09, Vol.18 (36), p.2479-2481 |
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| source | MEDLINE; Royal Society Of Chemistry Journals 2008-; Alma/SFX Local Collection |
| subjects | Amyloid Precursor Protein Secretases - chemistry Amyloid Precursor Protein Secretases - metabolism Animals Biocatalysis Catalytic Domain Cattle Enzymes Hydrolysis Industrial applications Insulysin - chemistry Insulysin - metabolism Leucine Leucyl Aminopeptidase - chemistry Leucyl Aminopeptidase - metabolism Ligands Peptides Peptides - chemistry Peptides - metabolism Physical chemistry Protein Structure, Tertiary Residues Thermodynamics Zinc - chemistry |
| title | Mechanisms of peptide hydrolysis by aspartyl and metalloproteases |
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