ILVBL

Last update 08 May 2025

Basic Info

Synonyms

2-hydroxyacyl-CoA lyase 2, 209L8, Acetolactate synthase-like protein

+ [10]

Introduction

Endoplasmic reticulum 2-OH acyl-CoA lyase involved in the cleavage (C1 removal) reaction in the fatty acid alpha-oxydation in a thiamine pyrophosphate (TPP)-dependent manner. Involved in the phytosphingosine degradation pathway.

100 Clinical Results associated with ILVBL

100 Translational Medicine associated with ILVBL

0 Patents (Medical) associated with ILVBL

347

Literatures (Medical) associated with ILVBL

01 Feb 2025·Bioresource Technology

High yield production of L-isoleucine through readjusting the ratio of two direct precursors in Escherichia coli

Article

Author: Lin, Baixue ; Tao, Yong ; Huo, Xiaojing ; Shi, Congrong ; You, Ran

L-isoleucine (L-Ile) is an essential amino acid, which biosynthesis has been studied extensively. L-valine (L-Val) is a major by-product that limits L-Ile yield. Here, multiple strategies were employed to enhance L-Ile production and reduce L-Val in Escherichia coli. The biosynthetic pathway of L-Ile was divided into L-threonine (L-Thr) and L-Ile modules. In the L-Ile module, AHAS and IlvC were screened for high affinity toward 2-oxobutanoate and α-aceto-α-hydroxybutyrate, respectively, enhancing L-Ile yield. The L-Thr module was optimized via the overexpression of key enzymes, increasing 2-oxobutanoate supply. Furthermore, the deletion ofptsGandpykFand overexpression of citramalate synthase were employed to balance the precursors ratio. The engineered strain achieved a high yield of 0.40 mol L-Ile/mol glucose, a high productivity of 0.83 g/L/h, and significantly reduced L-Val accumulation, which would facilitate the subsequent separation and purification of L-Ile. This work provides a sustainable platform for the production of L-Ile derivatives.

01 Feb 2025·The Journal of Antibiotics

Inhibitors of acetohydroxyacid synthase as promising agents against non-tuberculous mycobacterial diseases

Article

Author: Nguyen, Tam Doan ; Kim, Jaewhan ; Kim, Hwa-Jung ; Song, Chang-Hwa ; Son, Doyi ; Lim, Hee-Jong ; Chae, Chong Hak ; Choi, Ji-Ae ; Lee, Junghwan ; Son, Sang-Hun

Acetohydroxyacid synthase (AHAS), exclusively present in microorganisms and plants, is a promising target for several herbicides due to its catalytic role in the branched-chain amino acid biosynthetic pathway. Previous studies have shown that K13787, a pyrazolopyrimidine sulfonamide AHAS inhibitor, was moderately effective against pulmonary infection caused by M. tuberculosis and nontuberculous mycobacteria (NTM). In this study, we synthesized various structural derivatives of K13787 based on the molecular docking studies and assessed their MICs against mycobacteria species. Among the synthetic compounds screened, K13787, along with KNT2077 and KNT2099, exhibited inhibitory efficacy against M. avium and M. abscessus, including CLR-resistant NTM species. Notably, these compounds displayed a synergistic effect (FIC ≤ 0.5) when combined with CLR against M. avium and M. abscessus. Our findings suggest that these newly identified AHAS-targeted compounds hold promise as lead candidates for novel antimycobacterial agents against NTM infections. Considering the structure-activity relationship, K13787, KNT2077, and KTN2099 emerge as potential treatments for NTM species.

01 Feb 2025·Pest Management Science

Allelic interactions defining Raphanus raphanistrumAHAS resistance level: strong vs weak target‐site AHAS resistance alleles

Article

Author: Powles, Stephen B. ; Vila‐Aiub, Martin ; Nestares, Graciela ; Garcia, Federico ; Gundel, Pedro E. ; Han, Heping ; Ochogavía, Ana C. ; Gil, Mercedes ; Yu, Qin ; Breccia, Gabriela

AbstractBACKGROUNDChlorsulfuron resistance and genetic dominance was evaluated in Raphanus raphanistrum genotypes homozygous (122‐RR, 376‐RR), heterozygous (122‐RS, 376‐RS) and compound heterozygous (122‐R/376‐R) for the target‐site resistance mutations Ala‐122‐Tyr and Asp‐376‐Glu in the AHAS (acetohydroxyacid synthase) gene.RESULTSAt the AHAS level, 122‐RR and 122‐RS plants exhibited significantly higher I50 values than 376‐RR and 376‐RS plants, respectively. However, plants of the compound heterozygous genotype (122‐R/376‐R), showed no difference in AHAS activity compared to the 122‐RS genotype but lower activity than the 122‐RR genotype, and showed a nearly 400‐fold greater I50 value than both genotypes (376‐RR and 376‐RS) carrying the 376‐Glu allele. At the whole‐plant level, 100% survival was observed for 122‐RR plants at the highest chlorsulfuron dose of 640 g ha−1, yet 376‐RR plants showed no survival at 380 g ha−1. Thus, this survival difference resulted in different median lethal dose (LD50) estimates [>640 (122‐RR) versus 330 g ha−1(376‐RR)]. The effect of chlorsulfuron in reducing aboveground growth of surviving plants also was markedly lower for the homozygous 122‐RR (GR50 = 566 g ha−1) than for 376‐RR plants (GR50 = 66). Heterozygous plants carrying the 122‐Tyr allele (122‐RS) exhibited two‐ and five‐fold higher LD50 values than both homozygous and heterozygous plants carrying the 376‐Glu allele (376‐RR, 376‐RS), respectively. Along the difference in plant survival, 122‐RS plants also showed four‐fold higher GR50 than both 376‐RR and 376‐RS plants. Survival of plants with the compound heterozygous genotype (122‐R/376‐R) under increasing chlorsulfuron doses was similar to 122‐RR or 122‐RS genotypes. However, this compound heterozygous genotype showed two‐ and six‐fold higher LD50 values than 376‐RR or 376‐RS genotypes, respectively. However, both resistance 122‐Tyr and 376‐Glu alleles were dominant or nearly dominant over the wild‐type susceptible alleles (ALA‐122 and ASP‐376), and the resistance 122‐Tyr allele was dominant over the 376‐Glu allele.CONCLUSIONSThese results broaden our understanding of AHAS target‐site resistance in R. raphanistrum and strengthens the hypothesis that the AHAS 122‐Tyr allele corresponds to a stronger target‐site resistance allele than the 376‐Glu allele. © 2024 Society of Chemical Industry.

Analysis

Perform a panoramic analysis of this field.

view full example data

AI Agents Built for Biopharma Breakthroughs

Accelerate discovery. Empower decisions. Transform outcomes.

Get started for free today!

Accelerate Strategic R&D decision making with Synapse, PatSnap’s AI-powered Connected Innovation Intelligence Platform Built for Life Sciences Professionals.

Start your data trial now!

Synapse data is also accessible to external entities via APIs or data packages. Empower better decisions with the latest in pharmaceutical intelligence.

Bio

Bio Sequences Search & Analysis

Chemical

Chemical Structures Search & Analysis

ILVBL

Basic Info

Related

Analysis