Last update 01 Nov 2024

enteropeptidase

Last update 01 Nov 2024

Basic Info

Synonyms

Enterokinase, Enteropeptidase, Enteropeptidase catalytic light chain

+ [11]

Introduction

Responsible for initiating activation of pancreatic proteolytic proenzymes (trypsin, chymotrypsin and carboxypeptidase A). It catalyzes the conversion of trypsinogen to trypsin which in turn activates other proenzymes including chymotrypsinogen, procarboxypeptidases, and proelastases.

Drugs associated with enteropeptidase

Sucunamostat

Target

enteropeptidase

Mechanism

enteropeptidase inhibitors

Active Org.

SCOHIA PHARMA, Inc.Startup

Originator Org.

Takeda Pharmaceutical Co., Ltd.

Active Indication

Homocystinuria [+2]

Inactive Indication

Diabetes Mellitus, Type 2 [+2]

Drug Highest PhasePhase 1

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

WO2023141744

Patent Mining

Target

ADHs x ALDH2 x enteropeptidase

Mechanism-

Active Org.

Institute of Zoology Chinese Academy of Science

Originator Org.

Institute of Zoology Chinese Academy of Science

Active Indication

Substance Abuse

Inactive Indication-

Drug Highest PhaseDiscovery

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

OBE-2001

Target

enteropeptidase

Mechanism

enteropeptidase inhibitors

Active Org.-

Originator Org.

Obe Therapy Biotechnology SAS

Active Indication-

Inactive Indication

Diabetes Mellitus, Type 2 [+1]

Drug Highest PhasePending

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

Clinical Trials associated with enteropeptidase

JPRN-JapicCTI-205109 / CompletedPhase 2

A Randomized, Multi-center, Double-blind, Placebo-controlled, Parallel-group Comparison, Phase 2a Study to Evaluate the Safety, Tolerability and Efficacy of SCO-792 in Subjects with Type 2 Diabetes and Albuminuria.

Start Date11 Jun 2020

Sponsor / Collaborator

SCOHIA PHARMA, Inc.Startup

JPRN-jRCT1080225017 / CompletedPhase 2

Start Date11 Jun 2020

Sponsor / Collaborator

SCOHIA PHARMA, Inc.Startup

JPRN-JapicCTI-194848 / CompletedPhase 2

Start Date28 Nov 2019

Sponsor / Collaborator

SCOHIA PHARMA, Inc.Startup

100 Clinical Results associated with enteropeptidase

100 Translational Medicine associated with enteropeptidase

0 Patents (Medical) associated with enteropeptidase

727

Literatures (Medical) associated with enteropeptidase

01 Nov 2024·Protein Expression and Purification

Preparation of recombinant neuritin protein

Article

Author: Sun, Jiawei ; Meng, Pingping ; Li, Yuanyuan ; Wei, Yu ; Guo, Jiatong ; Zhu, Liyan ; Zhu, Jingling

Neuritin plays an important role in promoting nerve injury repair and maintaining synaptic plasticity, making it a potential therapeutic target for the treatment of nerve injury and neurodegenerative diseases. The present study aimed to obtain an active, unlabeled neuritin protein. Initially, a neuritin protein expression system with an enterokinase site was constructed in Escherichia coli. After optimizing induction conditions and screening for high expression, a neuritin recombinant protein with purity exceeding 85 % was obtained through Ni-affinity chromatography. Subsequently, unlabeled neuritin with a molecular weight of 11 kDa was obtained through the enzymatic cleavage of the His label using an enterokinase. Furthermore, a neuritin recombinant protein with purity exceeding 95 % was obtained using gel chromatography. Functional investigations revealed that neurite outgrowth of PC12 cells was stimulated by the isolated neuritin. This study establishes a method to obtain active and unlabeled neuritin protein, providing a foundation for subsequent research on its biological functions.

01 Nov 2024·Journal of Invertebrate Pathology

Bombyx mori serpin 3 is involved in innate immunity by interacting with serine protease 7 to regulate prophenoloxidase activation

Article

Author: Kong, Wei-Wei ; Wang, Jie ; Ayaz, Sadaf ; Wang, Yu-Ling ; Toufeeq, Shahzad ; Cao, Hui-Hua ; Xu, Jia-Ping ; Liu, Shi-Huo

A subfamily of conserved proteins called serpins plays crucial roles in various physiological functions, particularly in the activation pathway of the serine protease cascade, an essential component of insect innate immunity. Here, we found Bombyx mori serpin 3 (BmSerpin3) was most highly expressed in the fat body, and was up-regulated after exposure to bacteria, fungus and virus. Further, the expression of BmSerpin3 in the hemocytes, fat body, midgut of silkworm larvae, and BmN cells was up-regulated upon Bombyx mori nucleopolyhedrovirus (BmNPV) infection. Through Bac-to-Bac expression system, we obtained the active protein of BmSerpin3, and the enzyme activity assay showed that BmSerpin3 significantly inhibited the activity of both subtilisin and trypsin. In addition, BmSerpin3 could inhibit the activation of prophenoloxidase (PPO) in larvae. The knockdown of BmSerpin3 showed increased phenoloxidase (PO) activity compared to control after BmNPV infection. Ultimately, we confirmed that BmSerpin3 interacts with B. mori Serine Protease 7 (BmSP7). Hence, we hypothesize that BmSerpin3 is involved in innate immunity by interacting with BmSP7 to regulate the PPO activation cascade. Taken together, these results showed that BmSerpin3 play a role in silkworm innate immunity and lay a foundation for studying its functions.

08 Oct 2024·Analytical Chemistry

Development of an Ultrasensitive Competitive Double-Enzyme Cascade Fluorescence Signal Amplification Method for Factor XIa Inhibitor Screening

Article

Author: Zhan, Yujuan ; Ding, Ya ; Shu, Chang ; Yan, Zelong ; Chen, Haotian ; Ning, Jiangyue ; Bao, Xingyan ; Ding, Li ; Hu, Penghui

Coagulation factor XIa (FXIa) is associated with a low risk of bleeding and has been identified as an effective and safe target for the development of novel anticoagulant drugs. In this study, we established an ultrasensitive competitive dual-enzyme cascade signal amplification method for the quantitative analysis and screening of FXIa inhibitors. Due to the specific recognition of FXIa's active site by the aptamer AptE40, the AptE40-QDs-EK recognition probe modified with enterokinase (EK) and the aptamer AptE40, was attached to the MNPs-FXIa capture probe. When FXIa inhibitor was present, it competed with AptE40 for binding to FXIa, resulting in the detachment of AptE40-QDs-EK from MNPs-FXIa. After magnetic separation, the enterokinase of AptE40-QDs-EK in the supernatant hydrolyzed N-terminal hexapeptide of trypsinogen, leading to the production of a large amount of trypsin as part of the first-stage signal cascade amplification. Next, trypsin could hydrolyze the hexameric arginine peptide (RRRRRR, R6), leading to the dissociation of RQDs from the R6-RQDs signal probe; this resulted in a dramatic increase in the fluorescence intensity of the supernatant as the second-stage signal cascade was amplified. The feasibility of the method was investigated using the FXIa inhibitor aptamer FELIAP as a positive model drug. Furthermore, the method was applied to screen the FXIa inhibitors in Eupolyphaga sinensis Walker. Two fractions with more active anticoagulated ingredients were successfully identified and validated via the conventional method, and the results were consistent. The established method provides a key technique for the sensitive detection, high-throughput analysis, and screening of the FXIa inhibitors.

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enteropeptidase

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