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Last update 23 Jan 2025

MetDC

Last update 23 Jan 2025

Basic Info

Synonyms-

Introduction-

Drugs associated with MetDC

SYNB-1353

Target

MetDC x MetP

Mechanism

MetDC stimulants [+3]

Active Org.

Synlogic, Inc.

Originator Org.

Synlogic, Inc.

Active Indication

Homocystinuria

Inactive Indication-

Drug Highest PhasePhase 1

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

Clinical Trials associated with MetDC

NCT05462132

/ CompletedPhase 1

A Phase 1, Dose-escalation, Randomized, Placebo-Controlled Study to Assess the Safety, Tolerability, and Pharmacodynamics of SYNB1353 in Healthy Volunteers

This is a Phase 1, double-blind (Sponsor-open), placebo-controlled, randomized, dose-escalation, inpatient study using a multiple-ascending dose (MAD) design to assess the safety, tolerability, and PD of SYNB1353 in HVs.

Start Date07 Jul 2022

Sponsor / Collaborator

Synlogic, Inc.

100 Clinical Results associated with MetDC

100 Translational Medicine associated with MetDC

0 Patents (Medical) associated with MetDC

468

Literatures (Medical) associated with MetDC

01 Jan 2025·International Journal of Biological Macromolecules

An engineered dual-functional L-DOPA decarboxylase enables a minimized hydroxytyrosol cascade

Article

Author: Liao, Daocheng ; Lin, Ying ; Huo, Ying ; Zheng, Suiping ; Zhang, Zhiteng ; Tang, Shiming ; Ouyang, Zhilin

Hydroxytyrosol has been proven beneficial to human health. However, the process involving the conversion of L-DOPA to 3,4-dihydroxyphenylacetaldehyde (3,4-DHPAA) in hydroxytyrosol biosynthesis typically required the simultaneous use of decarboxylase and oxidative deaminase. In addition, phenylacetaldehyde reductase from Solanum lycopersicum (SlPAR) in hydroxytyrosol biosynthesis exhibits poor thermal stability. In this study, we unexpectedly discovered that L-DOPA decarboxylase from Pseudomonas putida (PpDODC) exhibits weak dual-functional activity for both decarboxylation and oxidative deamination of L-DOPA. Through a dual-function reshaping strategy, the best dual-functional mutant PpDODC/Y79F/Y324F achieved an enzyme activity of 0.95 U/mg and exhibited a 256.8-fold increase in activity compared to the wild-type. Through rational design of SlPAR, the optimal mutant SlPAR/G52D/V188I/N234W/Q286P (SlPAR-M4) maintained stability after 12 h' treatment at 40 °C. Based on these mutants, we established a simplified cascade to synthesize hydroxytyrosol from L-DOPA, achieving a hydroxytyrosol yield of 31.4 mM from 32 mM L-DOPA in a 5-hour reaction. This process achieved the highest molar conversion rate (98.2 %) currently reported for the synthesis of hydroxytyrosol from L-DOPA. This study provides a novel solution for hydroxytyrosol synthesis from a new perspective, and the mutants hold promise for widespread application in biotransformation studies of hydroxytyrosol and other structurally-similar compounds.

01 Jan 2025·Current Microbiology

First Detection of Vibrio parahaemolyticus in Migratory Birds in Egypt: Antibiogram, Virulence, and Resistance Gene Profiles Indicating Zoonotic and Public Health Risks

Article

Author: Al-Sultan, Saad Ibrahim ; Abdel-Raheem, Sherief M ; El-Tarabili, Reham M

This study examined the occurrence of Vibrio parahaemolyticus obtained from migrating birds, marking the first instance of such research conducted in Egypt. The study assessed potential risks using an antibiogram, virulence characteristics, antibiotic-resistance, and gene profile. Randomly collected 80 samples were tested for V. parahaemolyticus. Eleven (13.75%) samples were V. parahaemolyticus-contaminated. All isolates were positive for 16SrRNA and species-specific toxR genes. Interestingly, our strain is genetically similar to human and shrimp isolates, suggesting zoonotic transmission may pose a health danger. All isolates had 100% l-lysine decarboxylase, 45.45% beta-hemolytic, and 100% l-ornithine decarboxylase activity. All isolates displayed no l-arginine decarboxylase activity. Notably, every isolate possessed a minimum of two virulence genes. In addition, the profiles of virulence genes were identified, tdh + /trh + (27.3%), tdh-/trh + (27.3%), and tdh + /trh- (45.4%). Out of the V. parahaemolyticus isolates, 18.2% (2/11) were extensively drug-resistant (XDR) to six different antimicrobials classes and possessed the bla_TEM, bla_OXA, sul1, and tetA genes. Furthermore, 63.6% of the isolates displayed multidrug resistance (MDR). The correlation highlights a strong relationship between phenotypic and genotypic resistance. Besides the strong correlation between virulence and resistance genes. In summary, this work highlighted the presence of newly identified MDR and XDR V. parahaemolyticus carried toxR, trh, and tdh virulence genes, as well as bla_TEM, bla_OXA, sul1, and tetA resistance genes in migratory birds, indicating a significant public health risk.

01 Dec 2024·International Journal of Biological Macromolecules

Discovery and characterization of temperature adaptation modules by mining L-glutamate decarboxylase derived from psychrophilic microorganisms

Article

Author: Wang, Qiong ; Song, Chenshuo ; Qiao, Jun ; Luo, Jie ; Liu, Zhongmei ; Cheng, Zhongyi ; Zhou, Zhemin ; Han, Laichuang

Directed alterations of the enzyme's temperature adaptations, such as thermostability and optimal catalytic temperature (T_opt), are usually the way to go in order to meet the applications, however they are limited by the understanding between protein structure and function. Glutamate decarboxylase (GADs) is a common enzyme in the food industry. In this study, we identified and characterized three novel L-glutamate decarboxylases from psychrophilic microorganisms. Interestingly, the two enzymes (Gad Psy.Y/Gad Psy.F) showed significant differences in temperature adaptation. Through multiple sequence alignment and structural analysis, two potential regions that may affect the T_opt and thermostability of the GAD, termed temperature adaptation modules (TAMs), were targeted. To validate the role of TAMs, we constructed mutants with bi-directional transplants of TAMs, which ultimately significantly altered the temperature adaptation of Gad Psy.Y and Gad Psy.F. Molecular dynamics simulations analysis demonstrated that the introduction and disruption of salt bridges in the mutant TAMs are crucial for this alteration. These findings deepen the understanding of the mechanisms of protein temperature adaptation and provide implications for protein engineering, while also offering advantageous enzymes to support the biosynthesis of GABA.

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