The Experts below are selected from a list of 165 Experts worldwide ranked by ideXlab platform
Nancy A. Thornberry - One of the best experts on this subject based on the ideXlab platform.
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Catalytic properties and inhibition of proline-specific dipeptidyl peptidases II, IV and VII
2015Co-Authors: Jonathan A. Ellman, Richard T. Cummings, Nancy A. ThornberryAbstract:There is currently intense interest in the emerging group of proline-specific Dipeptidases, and their roles in the regulation of biological processes. Dipeptidyl peptidase IV (DPP-IV) is involved in glucose metabolism by contributing to the regulation of glucagon family peptides and has emerged as a potential target for the treatment of metabolic diseases. Two other proline-specific Dipeptidases, DPP-VII (also known as quiescent cell proline Dipeptidase) and DPP-II, have unknown functions and have recently been suggested to be identical proteases based on a sequence comparison of human DPP-VII and rat DPP-II (78
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Catalytic properties and inhibition of proline-specific dipeptidyl peptidases II, IV and VII
Biochemical Journal, 2003Co-Authors: Barbara Leiting, Jonathan A. Ellman, Richard T. Cummings, Kellyann D. Pryor, Joseph K. Wu, Frank Marsilio, Reshma A. Patel, Charles S. Craik, Nancy A. ThornberryAbstract:There is currently intense interest in the emerging group of proline-specific Dipeptidases, and their roles in the regulation of biological processes. Dipeptidyl peptidase IV (DPP-IV) is involved in glucose metabolism by contributing to the regulation of glucagon family peptides and has emerged as a potential target for the treatment of metabolic diseases. Two other prolinespecific Dipeptidases, DPP-VII (also known as quiescent cell proline Dipeptidase) and DPP-II, have unknown functions and have recently been suggested to be identical proteases based on a sequence comparison of human DPP-VII and rat DPP-II (78% identity) [Araki, Li, Yamamoto, Haneda, Nishi, Kikkawa and Ohkubo (2001) J. Biochem. 129, 279‐288; Fukasawa, Fukasawa, Higaki, Shiina, Ohno, Ito, Otogoto and Ota (2001) Biochem. J. 353, 283‐290]. To facilitate the identification of selective sub
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Catalytic properties and inhibition of proline-specific dipeptidyl peptidases II, IV and VII.
The Biochemical journal, 2003Co-Authors: Barbara Leiting, Jonathan A. Ellman, Richard T. Cummings, Kellyann D. Pryor, Joseph K. Wu, Frank Marsilio, Reshma A. Patel, Charles S. Craik, Nancy A. ThornberryAbstract:There is currently intense interest in the emerging group of proline-specific Dipeptidases, and their roles in the regulation of biological processes. Dipeptidyl peptidase IV (DPP-IV) is involved in glucose metabolism by contributing to the regulation of glucagon family peptides and has emerged as a potential target for the treatment of metabolic diseases. Two other proline-specific Dipeptidases, DPP-VII (also known as quiescent cell proline Dipeptidase) and DPP-II, have unknown functions and have recently been suggested to be identical proteases based on a sequence comparison of human DPP-VII and rat DPP-II (78% identity) [Araki, Li, Yamamoto, Haneda, Nishi, Kikkawa and Ohkubo (2001) J. Biochem. 129, 279-288; Fukasawa, Fukasawa, Higaki, Shiina, Ohno, Ito, Otogoto and Ota (2001) Biochem. J. 353, 283-290]. To facilitate the identification of selective substrates and inhibitors for these enzymes, a complete biochemical profile of these enzymes was obtained. The pH profiles, substrate specificities as determined by positional scanning, Michaelis-Menten constants and inhibition profiles for DPP-VII and DPP-II were shown to be virtually identical, strongly supporting the hypothesis that they are the same protease. In addition, substrate specificities, catalytic constants and IC(50) values were shown to be markedly different from those of DPP-IV. Selective DPP-IV and DPP-VII substrates were identified and they can be used to design selective inhibitors and probe further into the biology of these enzymes.
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Catalytic properties and inhibition of proline-specific dipeptidyl peptidases II, IV and VII - eScholarship
2003Co-Authors: Barbara Leiting, Jonathan A. Ellman, Richard T. Cummings, Kellyann D. Pryor, Joseph K. Wu, Frank Marsilio, Reshma A. Patel, Charles S. Craik, Nancy A. ThornberryAbstract:There is currently intense interest in the emerging group of proline-specific Dipeptidases, and their roles in the regulation of biological processes. Dipeptidyl peptidase IV (DPP-IV) is involved in glucose metabolism by contributing to the regulation of glucagon family peptides and has emerged as a potential target for the treatment of metabolic diseases. Two other proline-specific Dipeptidases, DPP-VII (also known as quiescent cell proline Dipeptidase) and DPP-II, have unknown functions and have recently been suggested to be identical proteases based on a sequence comparison of human DPP-VII and rat DPP-II (78% identity) [Araki, Li, Yamamoto, Haneda, Nishi, Kikkawa and Ohkubo (2001) J. Biochem. 129,279-288; Fukasawa, Fukasawa, Higaki, Shiina, Ohno, Ito, Otogoto and Ota (2001) Biochem. J. 353, 283-290]. To facilitate the identification of selective substrates and inhibitors for these enzymes, a complete biochemical profile of these enzymes was obtained. The pH profiles, substrate specificities as determined by positional scanning, Michaelis-Menten constants and inhibition profiles for DPP-VII and DPP-II were shown to be virtually identical, strongly supporting the hypothesis that they are the same protease. In addition, substrate specificities, catalytic constants and IC50 values were shown to be markedly different from those of DPP-IV. Selective DPP-IV and DPP-VII substrates were identified and they can be used to design selective inhibitors and probe further into the biology of these enzymes.
Anand K Bachhawat - One of the best experts on this subject based on the ideXlab platform.
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dug1p is a cys gly peptidase of the γ glutamyl cycle of saccharomyces cerevisiae and represents a novel family of cys gly peptidases
Journal of Biological Chemistry, 2009Co-Authors: Hardeep Kaur, Chitranshu Kumar, Christophe Junot, Michel B Toledano, Anand K BachhawatAbstract:GSH metabolism in yeast is carried out by the gamma-glutamyl cycle as well as by the DUG complex. One of the last steps in the gamma-glutamyl cycle is the cleavage of Cys-Gly by a peptidase to the constitutent amino acids. Saccharomyces cerevisiae extracts carry Cys-Gly Dipeptidase activity, but the corresponding gene has not yet been identified. We describe the isolation and characterization of a novel Cys-Gly Dipeptidase, encoded by the DUG1 gene. Dug1p had previously been identified as part of the Dug1p-Dug2p-Dug3p complex that operates as an alternate GSH degradation pathway and has also been suggested to function as a possible di- or tripeptidase based on genetic studies. We show here that Dug1p is a homodimer that can also function in a Dug2-Dug3-independent manner as a Dipeptidase with high specificity for Cys-Gly and no activity toward tri- or tetrapeptides in vitro. This activity requires zinc or manganese ions. Yeast cells lacking Dug1p (dug1Delta) accumulate Cys-Gly. Unlike all other Cys-Gly peptidases, which are members of the metallopeptidase M17, M19, or M1 families, Dug1p is the first to belong to the M20A family. We also show that the Dug1p Schizosaccharomyces pombe orthologue functions as the exclusive Cys-Gly peptidase in this organism. The human orthologue CNDP2 also displays Cys-Gly peptidase activity, as seen by complementation of the dug1Delta mutant and by biochemical characterization, which revealed a high substrate specificity and affinity for Cys-Gly. The results indicate that the Dug1p family represents a novel class of Cys-Gly Dipeptidases.
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dug1p is a cys gly peptidase of the γ glutamyl cycle of saccharomyces cerevisiae and represents a novel family of cys gly peptidases
Journal of Biological Chemistry, 2009Co-Authors: Hardeep Kaur, Chitranshu Kumar, Christophe Junot, Michel B Toledano, Anand K BachhawatAbstract:GSH metabolism in yeast is carried out by the γ-glutamyl cycle as well as by the DUG complex. One of the last steps in the γ-glutamyl cycle is the cleavage of Cys-Gly by a peptidase to the constitutent amino acids. Saccharomyces cerevisiae extracts carry Cys-Gly Dipeptidase activity, but the corresponding gene has not yet been identified. We describe the isolation and characterization of a novel Cys-Gly Dipeptidase, encoded by the DUG1 gene. Dug1p had previously been identified as part of the Dug1p-Dug2p-Dug3p complex that operates as an alternate GSH degradation pathway and has also been suggested to function as a possible di- or tripeptidase based on genetic studies. We show here that Dug1p is a homodimer that can also function in a Dug2-Dug3-independent manner as a Dipeptidase with high specificity for Cys-Gly and no activity toward tri- or tetrapeptides in vitro. This activity requires zinc or manganese ions. Yeast cells lacking Dug1p (dug1Δ) accumulate Cys-Gly. Unlike all other Cys-Gly peptidases, which are members of the metallopeptidase M17, M19, or M1 families, Dug1p is the first to belong to the M20A family. We also show that the Dug1p Schizosaccharomyces pombe orthologue functions as the exclusive Cys-Gly peptidase in this organism. The human orthologue CNDP2 also displays Cys-Gly peptidase activity, as seen by complementation of the dug1Δ mutant and by biochemical characterization, which revealed a high substrate specificity and affinity for Cys-Gly. The results indicate that the Dug1p family represents a novel class of Cys-Gly Dipeptidases.
Barbara Leiting - One of the best experts on this subject based on the ideXlab platform.
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Catalytic properties and inhibition of proline-specific dipeptidyl peptidases II, IV and VII
Biochemical Journal, 2003Co-Authors: Barbara Leiting, Jonathan A. Ellman, Richard T. Cummings, Kellyann D. Pryor, Joseph K. Wu, Frank Marsilio, Reshma A. Patel, Charles S. Craik, Nancy A. ThornberryAbstract:There is currently intense interest in the emerging group of proline-specific Dipeptidases, and their roles in the regulation of biological processes. Dipeptidyl peptidase IV (DPP-IV) is involved in glucose metabolism by contributing to the regulation of glucagon family peptides and has emerged as a potential target for the treatment of metabolic diseases. Two other prolinespecific Dipeptidases, DPP-VII (also known as quiescent cell proline Dipeptidase) and DPP-II, have unknown functions and have recently been suggested to be identical proteases based on a sequence comparison of human DPP-VII and rat DPP-II (78% identity) [Araki, Li, Yamamoto, Haneda, Nishi, Kikkawa and Ohkubo (2001) J. Biochem. 129, 279‐288; Fukasawa, Fukasawa, Higaki, Shiina, Ohno, Ito, Otogoto and Ota (2001) Biochem. J. 353, 283‐290]. To facilitate the identification of selective sub
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Catalytic properties and inhibition of proline-specific dipeptidyl peptidases II, IV and VII.
The Biochemical journal, 2003Co-Authors: Barbara Leiting, Jonathan A. Ellman, Richard T. Cummings, Kellyann D. Pryor, Joseph K. Wu, Frank Marsilio, Reshma A. Patel, Charles S. Craik, Nancy A. ThornberryAbstract:There is currently intense interest in the emerging group of proline-specific Dipeptidases, and their roles in the regulation of biological processes. Dipeptidyl peptidase IV (DPP-IV) is involved in glucose metabolism by contributing to the regulation of glucagon family peptides and has emerged as a potential target for the treatment of metabolic diseases. Two other proline-specific Dipeptidases, DPP-VII (also known as quiescent cell proline Dipeptidase) and DPP-II, have unknown functions and have recently been suggested to be identical proteases based on a sequence comparison of human DPP-VII and rat DPP-II (78% identity) [Araki, Li, Yamamoto, Haneda, Nishi, Kikkawa and Ohkubo (2001) J. Biochem. 129, 279-288; Fukasawa, Fukasawa, Higaki, Shiina, Ohno, Ito, Otogoto and Ota (2001) Biochem. J. 353, 283-290]. To facilitate the identification of selective substrates and inhibitors for these enzymes, a complete biochemical profile of these enzymes was obtained. The pH profiles, substrate specificities as determined by positional scanning, Michaelis-Menten constants and inhibition profiles for DPP-VII and DPP-II were shown to be virtually identical, strongly supporting the hypothesis that they are the same protease. In addition, substrate specificities, catalytic constants and IC(50) values were shown to be markedly different from those of DPP-IV. Selective DPP-IV and DPP-VII substrates were identified and they can be used to design selective inhibitors and probe further into the biology of these enzymes.
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Catalytic properties and inhibition of proline-specific dipeptidyl peptidases II, IV and VII - eScholarship
2003Co-Authors: Barbara Leiting, Jonathan A. Ellman, Richard T. Cummings, Kellyann D. Pryor, Joseph K. Wu, Frank Marsilio, Reshma A. Patel, Charles S. Craik, Nancy A. ThornberryAbstract:There is currently intense interest in the emerging group of proline-specific Dipeptidases, and their roles in the regulation of biological processes. Dipeptidyl peptidase IV (DPP-IV) is involved in glucose metabolism by contributing to the regulation of glucagon family peptides and has emerged as a potential target for the treatment of metabolic diseases. Two other proline-specific Dipeptidases, DPP-VII (also known as quiescent cell proline Dipeptidase) and DPP-II, have unknown functions and have recently been suggested to be identical proteases based on a sequence comparison of human DPP-VII and rat DPP-II (78% identity) [Araki, Li, Yamamoto, Haneda, Nishi, Kikkawa and Ohkubo (2001) J. Biochem. 129,279-288; Fukasawa, Fukasawa, Higaki, Shiina, Ohno, Ito, Otogoto and Ota (2001) Biochem. J. 353, 283-290]. To facilitate the identification of selective substrates and inhibitors for these enzymes, a complete biochemical profile of these enzymes was obtained. The pH profiles, substrate specificities as determined by positional scanning, Michaelis-Menten constants and inhibition profiles for DPP-VII and DPP-II were shown to be virtually identical, strongly supporting the hypothesis that they are the same protease. In addition, substrate specificities, catalytic constants and IC50 values were shown to be markedly different from those of DPP-IV. Selective DPP-IV and DPP-VII substrates were identified and they can be used to design selective inhibitors and probe further into the biology of these enzymes.
Jonathan A. Ellman - One of the best experts on this subject based on the ideXlab platform.
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Catalytic properties and inhibition of proline-specific dipeptidyl peptidases II, IV and VII
2015Co-Authors: Jonathan A. Ellman, Richard T. Cummings, Nancy A. ThornberryAbstract:There is currently intense interest in the emerging group of proline-specific Dipeptidases, and their roles in the regulation of biological processes. Dipeptidyl peptidase IV (DPP-IV) is involved in glucose metabolism by contributing to the regulation of glucagon family peptides and has emerged as a potential target for the treatment of metabolic diseases. Two other proline-specific Dipeptidases, DPP-VII (also known as quiescent cell proline Dipeptidase) and DPP-II, have unknown functions and have recently been suggested to be identical proteases based on a sequence comparison of human DPP-VII and rat DPP-II (78
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Catalytic properties and inhibition of proline-specific dipeptidyl peptidases II, IV and VII
Biochemical Journal, 2003Co-Authors: Barbara Leiting, Jonathan A. Ellman, Richard T. Cummings, Kellyann D. Pryor, Joseph K. Wu, Frank Marsilio, Reshma A. Patel, Charles S. Craik, Nancy A. ThornberryAbstract:There is currently intense interest in the emerging group of proline-specific Dipeptidases, and their roles in the regulation of biological processes. Dipeptidyl peptidase IV (DPP-IV) is involved in glucose metabolism by contributing to the regulation of glucagon family peptides and has emerged as a potential target for the treatment of metabolic diseases. Two other prolinespecific Dipeptidases, DPP-VII (also known as quiescent cell proline Dipeptidase) and DPP-II, have unknown functions and have recently been suggested to be identical proteases based on a sequence comparison of human DPP-VII and rat DPP-II (78% identity) [Araki, Li, Yamamoto, Haneda, Nishi, Kikkawa and Ohkubo (2001) J. Biochem. 129, 279‐288; Fukasawa, Fukasawa, Higaki, Shiina, Ohno, Ito, Otogoto and Ota (2001) Biochem. J. 353, 283‐290]. To facilitate the identification of selective sub
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Catalytic properties and inhibition of proline-specific dipeptidyl peptidases II, IV and VII.
The Biochemical journal, 2003Co-Authors: Barbara Leiting, Jonathan A. Ellman, Richard T. Cummings, Kellyann D. Pryor, Joseph K. Wu, Frank Marsilio, Reshma A. Patel, Charles S. Craik, Nancy A. ThornberryAbstract:There is currently intense interest in the emerging group of proline-specific Dipeptidases, and their roles in the regulation of biological processes. Dipeptidyl peptidase IV (DPP-IV) is involved in glucose metabolism by contributing to the regulation of glucagon family peptides and has emerged as a potential target for the treatment of metabolic diseases. Two other proline-specific Dipeptidases, DPP-VII (also known as quiescent cell proline Dipeptidase) and DPP-II, have unknown functions and have recently been suggested to be identical proteases based on a sequence comparison of human DPP-VII and rat DPP-II (78% identity) [Araki, Li, Yamamoto, Haneda, Nishi, Kikkawa and Ohkubo (2001) J. Biochem. 129, 279-288; Fukasawa, Fukasawa, Higaki, Shiina, Ohno, Ito, Otogoto and Ota (2001) Biochem. J. 353, 283-290]. To facilitate the identification of selective substrates and inhibitors for these enzymes, a complete biochemical profile of these enzymes was obtained. The pH profiles, substrate specificities as determined by positional scanning, Michaelis-Menten constants and inhibition profiles for DPP-VII and DPP-II were shown to be virtually identical, strongly supporting the hypothesis that they are the same protease. In addition, substrate specificities, catalytic constants and IC(50) values were shown to be markedly different from those of DPP-IV. Selective DPP-IV and DPP-VII substrates were identified and they can be used to design selective inhibitors and probe further into the biology of these enzymes.
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Catalytic properties and inhibition of proline-specific dipeptidyl peptidases II, IV and VII - eScholarship
2003Co-Authors: Barbara Leiting, Jonathan A. Ellman, Richard T. Cummings, Kellyann D. Pryor, Joseph K. Wu, Frank Marsilio, Reshma A. Patel, Charles S. Craik, Nancy A. ThornberryAbstract:There is currently intense interest in the emerging group of proline-specific Dipeptidases, and their roles in the regulation of biological processes. Dipeptidyl peptidase IV (DPP-IV) is involved in glucose metabolism by contributing to the regulation of glucagon family peptides and has emerged as a potential target for the treatment of metabolic diseases. Two other proline-specific Dipeptidases, DPP-VII (also known as quiescent cell proline Dipeptidase) and DPP-II, have unknown functions and have recently been suggested to be identical proteases based on a sequence comparison of human DPP-VII and rat DPP-II (78% identity) [Araki, Li, Yamamoto, Haneda, Nishi, Kikkawa and Ohkubo (2001) J. Biochem. 129,279-288; Fukasawa, Fukasawa, Higaki, Shiina, Ohno, Ito, Otogoto and Ota (2001) Biochem. J. 353, 283-290]. To facilitate the identification of selective substrates and inhibitors for these enzymes, a complete biochemical profile of these enzymes was obtained. The pH profiles, substrate specificities as determined by positional scanning, Michaelis-Menten constants and inhibition profiles for DPP-VII and DPP-II were shown to be virtually identical, strongly supporting the hypothesis that they are the same protease. In addition, substrate specificities, catalytic constants and IC50 values were shown to be markedly different from those of DPP-IV. Selective DPP-IV and DPP-VII substrates were identified and they can be used to design selective inhibitors and probe further into the biology of these enzymes.
Richard T. Cummings - One of the best experts on this subject based on the ideXlab platform.
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Catalytic properties and inhibition of proline-specific dipeptidyl peptidases II, IV and VII
2015Co-Authors: Jonathan A. Ellman, Richard T. Cummings, Nancy A. ThornberryAbstract:There is currently intense interest in the emerging group of proline-specific Dipeptidases, and their roles in the regulation of biological processes. Dipeptidyl peptidase IV (DPP-IV) is involved in glucose metabolism by contributing to the regulation of glucagon family peptides and has emerged as a potential target for the treatment of metabolic diseases. Two other proline-specific Dipeptidases, DPP-VII (also known as quiescent cell proline Dipeptidase) and DPP-II, have unknown functions and have recently been suggested to be identical proteases based on a sequence comparison of human DPP-VII and rat DPP-II (78
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Catalytic properties and inhibition of proline-specific dipeptidyl peptidases II, IV and VII
Biochemical Journal, 2003Co-Authors: Barbara Leiting, Jonathan A. Ellman, Richard T. Cummings, Kellyann D. Pryor, Joseph K. Wu, Frank Marsilio, Reshma A. Patel, Charles S. Craik, Nancy A. ThornberryAbstract:There is currently intense interest in the emerging group of proline-specific Dipeptidases, and their roles in the regulation of biological processes. Dipeptidyl peptidase IV (DPP-IV) is involved in glucose metabolism by contributing to the regulation of glucagon family peptides and has emerged as a potential target for the treatment of metabolic diseases. Two other prolinespecific Dipeptidases, DPP-VII (also known as quiescent cell proline Dipeptidase) and DPP-II, have unknown functions and have recently been suggested to be identical proteases based on a sequence comparison of human DPP-VII and rat DPP-II (78% identity) [Araki, Li, Yamamoto, Haneda, Nishi, Kikkawa and Ohkubo (2001) J. Biochem. 129, 279‐288; Fukasawa, Fukasawa, Higaki, Shiina, Ohno, Ito, Otogoto and Ota (2001) Biochem. J. 353, 283‐290]. To facilitate the identification of selective sub
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Catalytic properties and inhibition of proline-specific dipeptidyl peptidases II, IV and VII.
The Biochemical journal, 2003Co-Authors: Barbara Leiting, Jonathan A. Ellman, Richard T. Cummings, Kellyann D. Pryor, Joseph K. Wu, Frank Marsilio, Reshma A. Patel, Charles S. Craik, Nancy A. ThornberryAbstract:There is currently intense interest in the emerging group of proline-specific Dipeptidases, and their roles in the regulation of biological processes. Dipeptidyl peptidase IV (DPP-IV) is involved in glucose metabolism by contributing to the regulation of glucagon family peptides and has emerged as a potential target for the treatment of metabolic diseases. Two other proline-specific Dipeptidases, DPP-VII (also known as quiescent cell proline Dipeptidase) and DPP-II, have unknown functions and have recently been suggested to be identical proteases based on a sequence comparison of human DPP-VII and rat DPP-II (78% identity) [Araki, Li, Yamamoto, Haneda, Nishi, Kikkawa and Ohkubo (2001) J. Biochem. 129, 279-288; Fukasawa, Fukasawa, Higaki, Shiina, Ohno, Ito, Otogoto and Ota (2001) Biochem. J. 353, 283-290]. To facilitate the identification of selective substrates and inhibitors for these enzymes, a complete biochemical profile of these enzymes was obtained. The pH profiles, substrate specificities as determined by positional scanning, Michaelis-Menten constants and inhibition profiles for DPP-VII and DPP-II were shown to be virtually identical, strongly supporting the hypothesis that they are the same protease. In addition, substrate specificities, catalytic constants and IC(50) values were shown to be markedly different from those of DPP-IV. Selective DPP-IV and DPP-VII substrates were identified and they can be used to design selective inhibitors and probe further into the biology of these enzymes.
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Catalytic properties and inhibition of proline-specific dipeptidyl peptidases II, IV and VII - eScholarship
2003Co-Authors: Barbara Leiting, Jonathan A. Ellman, Richard T. Cummings, Kellyann D. Pryor, Joseph K. Wu, Frank Marsilio, Reshma A. Patel, Charles S. Craik, Nancy A. ThornberryAbstract:There is currently intense interest in the emerging group of proline-specific Dipeptidases, and their roles in the regulation of biological processes. Dipeptidyl peptidase IV (DPP-IV) is involved in glucose metabolism by contributing to the regulation of glucagon family peptides and has emerged as a potential target for the treatment of metabolic diseases. Two other proline-specific Dipeptidases, DPP-VII (also known as quiescent cell proline Dipeptidase) and DPP-II, have unknown functions and have recently been suggested to be identical proteases based on a sequence comparison of human DPP-VII and rat DPP-II (78% identity) [Araki, Li, Yamamoto, Haneda, Nishi, Kikkawa and Ohkubo (2001) J. Biochem. 129,279-288; Fukasawa, Fukasawa, Higaki, Shiina, Ohno, Ito, Otogoto and Ota (2001) Biochem. J. 353, 283-290]. To facilitate the identification of selective substrates and inhibitors for these enzymes, a complete biochemical profile of these enzymes was obtained. The pH profiles, substrate specificities as determined by positional scanning, Michaelis-Menten constants and inhibition profiles for DPP-VII and DPP-II were shown to be virtually identical, strongly supporting the hypothesis that they are the same protease. In addition, substrate specificities, catalytic constants and IC50 values were shown to be markedly different from those of DPP-IV. Selective DPP-IV and DPP-VII substrates were identified and they can be used to design selective inhibitors and probe further into the biology of these enzymes.