Last update 01 Nov 2024

scaaE3

Last update 01 Nov 2024

Basic Info

Synonyms-

Introduction-

Drugs associated with scaaE3

SYNB-8802

Target

frc x oxdC x oxlT x scaaE3

Mechanism

frc stimulants [+5]

Active Org.

Synlogic, Inc.

Originator Org.

Synlogic, Inc.

Active Indication

Hyperoxaluria [+1]

Inactive Indication-

Drug Highest PhasePhase 1

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

Clinical Trials associated with scaaE3

NCT05377112 / CompletedEarly Phase 1

A Double-Blind, Randomized, Placebo-controlled Study to Assess the Safety, Tolerability, and Pharmacodynamics of SYNB8802v1 in Subjects With History of Gastric Bypass Surgery or Short-bowel Syndrome

Study SYNB8802-CP-002 is designed to assess safety, tolerability, and oxalate lowering, in subjects with a history of gastric bypass surgery or short-bowel syndrome. In addition, this study will explore other PD effects relative to baseline as well as predictors of efficacy and tolerability.

Start Date29 Mar 2022

Sponsor / Collaborator

Synlogic, Inc.

NCT04629170 / CompletedPhase 1

A Double-Blind, Randomized, Placebo-Controlled Study to Assess the Safety, Tolerability, and Pharmacodynamics of SYNB8802 in Healthy Volunteers and in Patients With Enteric Hyperoxaluria

This Phase 1a/b, first-in-human, multiple dose-escalation, randomized, double-blinded, placebo-controlled study is evaluating SYNB8802 in healthy volunteers (HV) and subjects diagnosed with enteric hyperoxaluria (EH). Eligible subjects receive investigational product (IP) and undergo safety monitoring, evaluations, and subsequent follow-up after IP administration.
In Part 2, all evaluations and assessments throughout this study may be conducted either at the clinical site or by a home healthcare professional at an alternative location (e.g., EH patient's home, hotel).

Start Date04 Nov 2020

Sponsor / Collaborator

Synlogic, Inc.

100 Clinical Results associated with scaaE3

100 Translational Medicine associated with scaaE3

0 Patents (Medical) associated with scaaE3

Literatures (Medical) associated with scaaE3

18 Sep 2020·ACS Synthetic BiologyQ2 · BIOLOGY

Development of a Biosensor for Crotonobetaine-CoA Ligase Screening Based on the Elucidation of Escherichia coli Carnitine Metabolism

Q2 · BIOLOGY

Article

Author: Kugler, Pierre ; Fröhlich, Deborah ; Wendisch, Volker F.

l-Carnitine is essential in the intermediary metabolism of eukaryotes and is involved in the β-oxidation of medium- and long-chain fatty acids; thus, it has applications for medicinal purposes and as a dietary supplement. In addition, l-carnitine plays roles in bacterial physiology and metabolism, which have been exploited by the industry to develop biotechnological carnitine production processes. Here, on the basis of studies of l-carnitine metabolism in Escherichia coli and its activation by the transcriptional activator CaiF, a biosensor was developed. It expresses a fluorescent reporter gene that responds in a dose-dependent manner to crotonobetainyl-CoA, which is an intermediate of l-carnitine metabolism in E. coli and is proposed to be a coactivator of CaiF. Moreover, a dual-input biosensor for l-carnitine and crotonobetaine was developed. As an application of the biosensor, potential homologues of the betaine:CoA ligase CaiC from Citrobacter freundii, Proteus mirabilis, and Arcobacter marinus were screened and shown to be functionally active CaiC variants. These variants and the developed biosensor may be valuable for improving l-carnitine production processes.

03 Jan 2014·FEBS LettersQ3 · BIOLOGY

An oxalyl‐CoA synthetase is important for oxalate metabolism in Saccharomyces cerevisiae

Q3 · BIOLOGY

Article

Author: Nakata, Paul A ; Foster, Justin

Although oxalic acid is common in nature our understanding of the mechanism(s) regulating its turnover remains incomplete. In this study we identify Saccharomyces cerevisiae acyl‐activating enzyme 3 (ScAAE3) as an enzyme capable of catalyzing the conversion of oxalate to oxalyl‐CoA. Based on our findings we propose that ScAAE3 catalyzes the first step in a novel pathway of oxalate degradation to protect the cell against the harmful effects of oxalate derived from an endogenous process or an environmental source.

01 Jan 1996·Journal of Biochemical Toxicology

Interaction of salicylate and ibuprofen with the carboxylic acid: CoA ligases from bovine liver mitochondria

Article

Author: Donald A. Vessey ; Jie Hu ; Michael Kelley

Neither salicylate nor ibuprofen was a substrate or inhibitor of the long-chain fatty acid:CoA ligase. In contrast, all three xenobiotic-metabolizing medium-chain fatty acid:CoA ligases (XL-I, XL-II, and XL-III) had activity toward salicylate. The K(m) value for salicylate was similar for all three forms (2 to 3 microM), but XL-II and XL-III had higher activity at Vmax. For ibuprofen, only XL-III catalyzed its activation, and it had a K(m) for ibuprofen of 36 microM. Studies of salicylate inhibition of XL-I, XL-II, and XL-III revealed that it inhibited the benzoate activity of all three forms with K1 values of ca. 2 microM, which is in agreement with the K(m) values obtained with salicylate as substrate. Kinetic analysis revealed that salicylate conjugation by all three forms is characterized by substrate inhibition when salicylate exceeds ca. 20 microM. Substrate inhibition was more extensive with XL-I and XL-III. Previous work on the ligases employed assay concentrations of salicylate in the range of 0.1 to 1.0 mM, which are clearly inhibitory, particularly toward XL-I and XL-III. Thus, activity was not properly measured in previous studies, which accounts for the fact that salicylate conjugation was only found with one form, which is most likely XL-II since it has the highest Vmax activity and shows the least amount of substrate inhibition. Studies with ibuprofen indicated that it inhibited XL-I, XL-II, and XL-III, with KI values being in the range of 75-125 microM. The short-chain ligase was inhibited by both salicylate and ibuprofen with KI values of 93 and 84 microM, respectively. It was concluded that pharmacological doses of salicylate, but not ibuprofen, will affect the metabolism of medium-chain fatty acids and carboxylic acid xenobiotics and that the previously described mitochondrial ibuprofen:CoA ligase activity is attributable to XL-III.

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scaaE3

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