Role of a propeller loop in the quaternary structure and enzymatic activity of prolyl dipeptidases DPP-IV and DPP9

Hung Kuan Tang; Ku Chuan Chen; Gan Guang Liou; Shu Chun Cheng; Chia Hui Chien; Hsiang Yun Tang; Li Hao Huang; Hui Ping Chang; Chi Yuan Chou; Xin Chen

doi:10.1016/j.febslet.2011.10.009

Role of a propeller loop in the quaternary structure and enzymatic activity of prolyl dipeptidases DPP-IV and DPP9

Hung Kuan Tang, Ku Chuan Chen, Gan Guang Liou, Shu Chun Cheng, Chia Hui Chien, Hsiang Yun Tang, Li Hao Huang, Hui Ping Chang, Chi Yuan Chou, Xin Chen

Research output: Contribution to journal › Article › peer-review

11 Scopus citations

Abstract

The dipeptidyl peptidase (DPP) family members, including DPP-IV, DPP8, DPP9 and others, cleave the peptide bond after the penultimate proline residue and are drug target rich. The dimerization of DPP-IV is required for its activity. A propeller loop located at the dimer interface is highly conserved within the family. Here we carried out site-directed mutagenesis on the loop of DPPIV and identified several residues important for dimer formation and enzymatic activity. Interestingly, the corresponding residues on DPP9 have a different impact whereby the mutations decrease activity without changing dimerization. Thus the propeller loop seems to play a varying role in different DPPs.

Original language	English
Pages (from-to)	3409-3414
Number of pages	6
Journal	FEBS Letters
Volume	585
Issue number	21
DOIs	https://doi.org/10.1016/j.febslet.2011.10.009
State	Published - Nov 4 2011
Externally published	Yes

Keywords

Analytical ultracentrifugation
Dimerization
Dipeptidyl peptidase 9
Dipeptidyl peptidase-IV
Propeller loop

Access to Document

10.1016/j.febslet.2011.10.009

Cite this

@article{832621a494994e47a10abccbbb4d5522,

title = "Role of a propeller loop in the quaternary structure and enzymatic activity of prolyl dipeptidases DPP-IV and DPP9",

abstract = "The dipeptidyl peptidase (DPP) family members, including DPP-IV, DPP8, DPP9 and others, cleave the peptide bond after the penultimate proline residue and are drug target rich. The dimerization of DPP-IV is required for its activity. A propeller loop located at the dimer interface is highly conserved within the family. Here we carried out site-directed mutagenesis on the loop of DPPIV and identified several residues important for dimer formation and enzymatic activity. Interestingly, the corresponding residues on DPP9 have a different impact whereby the mutations decrease activity without changing dimerization. Thus the propeller loop seems to play a varying role in different DPPs.",

keywords = "Analytical ultracentrifugation, Dimerization, Dipeptidyl peptidase 9, Dipeptidyl peptidase-IV, Propeller loop",

author = "Tang, {Hung Kuan} and Chen, {Ku Chuan} and Liou, {Gan Guang} and Cheng, {Shu Chun} and Chien, {Chia Hui} and Tang, {Hsiang Yun} and Huang, {Li Hao} and Chang, {Hui Ping} and Chou, {Chi Yuan} and Xin Chen",

note = "Funding Information: We thank Dr. Wei-Hau Chang for the electron microscopy and Gu-Gang Chang, Peter Rubenstein, Ann Marie Stanley and Wang Chung for helpful suggestions. The study was financially supported by NRPGM (to X.C.) and an individual grant (to C.Y.C.) from National Science Council and National Health Research Institutes, Taiwan, ROC (to X.C.). ",

year = "2011",

month = nov,

day = "4",

doi = "10.1016/j.febslet.2011.10.009",

language = "English",

volume = "585",

pages = "3409--3414",

journal = "FEBS Letters",

issn = "0014-5793",

number = "21",

}

TY - JOUR

T1 - Role of a propeller loop in the quaternary structure and enzymatic activity of prolyl dipeptidases DPP-IV and DPP9

AU - Tang, Hung Kuan

AU - Chen, Ku Chuan

AU - Liou, Gan Guang

AU - Cheng, Shu Chun

AU - Chien, Chia Hui

AU - Tang, Hsiang Yun

AU - Huang, Li Hao

AU - Chang, Hui Ping

AU - Chou, Chi Yuan

AU - Chen, Xin

N1 - Funding Information: We thank Dr. Wei-Hau Chang for the electron microscopy and Gu-Gang Chang, Peter Rubenstein, Ann Marie Stanley and Wang Chung for helpful suggestions. The study was financially supported by NRPGM (to X.C.) and an individual grant (to C.Y.C.) from National Science Council and National Health Research Institutes, Taiwan, ROC (to X.C.).

PY - 2011/11/4

Y1 - 2011/11/4

N2 - The dipeptidyl peptidase (DPP) family members, including DPP-IV, DPP8, DPP9 and others, cleave the peptide bond after the penultimate proline residue and are drug target rich. The dimerization of DPP-IV is required for its activity. A propeller loop located at the dimer interface is highly conserved within the family. Here we carried out site-directed mutagenesis on the loop of DPPIV and identified several residues important for dimer formation and enzymatic activity. Interestingly, the corresponding residues on DPP9 have a different impact whereby the mutations decrease activity without changing dimerization. Thus the propeller loop seems to play a varying role in different DPPs.

AB - The dipeptidyl peptidase (DPP) family members, including DPP-IV, DPP8, DPP9 and others, cleave the peptide bond after the penultimate proline residue and are drug target rich. The dimerization of DPP-IV is required for its activity. A propeller loop located at the dimer interface is highly conserved within the family. Here we carried out site-directed mutagenesis on the loop of DPPIV and identified several residues important for dimer formation and enzymatic activity. Interestingly, the corresponding residues on DPP9 have a different impact whereby the mutations decrease activity without changing dimerization. Thus the propeller loop seems to play a varying role in different DPPs.

KW - Analytical ultracentrifugation

KW - Dimerization

KW - Dipeptidyl peptidase 9

KW - Dipeptidyl peptidase-IV

KW - Propeller loop

UR - http://www.scopus.com/inward/record.url?scp=80255122763&partnerID=8YFLogxK

U2 - 10.1016/j.febslet.2011.10.009

DO - 10.1016/j.febslet.2011.10.009

M3 - Article

C2 - 22001206

AN - SCOPUS:80255122763

SN - 0014-5793

VL - 585

SP - 3409

EP - 3414

JO - FEBS Letters

JF - FEBS Letters

IS - 21

ER -

Role of a propeller loop in the quaternary structure and enzymatic activity of prolyl dipeptidases DPP-IV and DPP9

Abstract

Keywords

Access to Document

Other files and links

Fingerprint

Cite this