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Last update 08 May 2025

DLD

Last update 08 May 2025

Basic Info

Synonyms

dihydrolipoamide dehydrogenase, Dihydrolipoyl dehydrogenase, mitochondrial, DLD

+ [7]

Introduction

Lipoamide dehydrogenase is a component of the glycine cleavage system as well as an E3 component of three alpha-ketoacid dehydrogenase complexes (pyruvate-, alpha-ketoglutarate-, and branched-chain amino acid-dehydrogenase complex) (PubMed:15712224, PubMed:16442803, PubMed:16770810, PubMed:17404228, PubMed:20160912, PubMed:20385101). The 2-oxoglutarate dehydrogenase complex is mainly active in the mitochondrion (PubMed:29211711). A fraction of the 2-oxoglutarate dehydrogenase complex also localizes in the nucleus and is required for lysine succinylation of histones: associates with KAT2A on chromatin and provides succinyl-CoA to histone succinyltransferase KAT2A (PubMed:29211711). In monomeric form may have additional moonlighting function as serine protease (PubMed:17404228). Involved in the hyperactivation of spermatazoa during capacitation and in the spermatazoal acrosome reaction (By similarity).

Drugs associated with DLD

CN118878536

Patent Mining

Target

DLD x mTOR

Mechanism

DLD inhibitors [+1]

Active Org.

Qilu Normal University

Originator Org.

Qilu Normal University

Active Indication

Neoplasms

Inactive Indication-

Drug Highest PhaseDiscovery

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

WO2023250157

Patent Mining

Target

DLD

Mechanism-

Active Org.

The Scripps Research Institute [+1]

Originator Org.

Cornell University [+1]

Active Indication

Tuberculosis

Inactive Indication-

Drug Highest PhaseDiscovery

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

100 Clinical Results associated with DLD

100 Translational Medicine associated with DLD

0 Patents (Medical) associated with DLD

861

Literatures (Medical) associated with DLD

01 Jul 2025·Water Research

Antibiotics shape the core microbial community distribution between floc and biofilm in an endogenous partial denitrification system: Insight from metabolic pathway

Article

Author: Yao, Wei ; Pang, Jin-Luo ; Dong, Kai-Yue ; Chang, Rong-Rong ; Huang, Bao-Cheng ; Jin, Ren-Cun ; Chen, Ke-Yu ; Yang, Chao-Xi

The response mechanism of microorganisms in partial denitrification (PD) system under antibiotic stress, particularly microbial energy metabolism and electron transfer, remain inadequately understood. This knowledge gap hinders the establishment of ecological links between microbial dynamics and macro-level reactor performance. To address this, moving bed biofilm reactors were employed to investigate the dynamic changes of microbial community and metabolism under sulfadiazine (SDZ) and ciprofloxacin (CIP) stress. Results showed that dosing 2 mg/L SDZ or CIP accelerated nitrite accumulation, achieving this milestone 15 days earlier than in the control group. At the end of the operational phase, nitrate removal efficiencies reached 90.3 ± 18.3 % (Control), 83.5 ± 16.2 % (SDZ-treated) and 93.9 ± 12.4 % (CIP-treated), with nitrate-to nitrite-transformation rates of 61.3 ± 12.7 %, 65.6 ± 13.1 % and 58.0 ± 21.2 %, respectively. The abundances of energy supply related genes, i.e., sucC and PK were higher in the CIP-treated group, while those in the other two groups were similar. The promoted tricarboxylic acid cycle and glycolysis led to NADH and ATP accumulation, accelerating nitrogen metabolism and benefiting early nitrite accumulation in the antibiotic-stressed system. More importantly, increasing antibiotics concentration from 2 mg/L to 4 mg/L induced selective migration of Thauera from floc to biofilm (abundance in floc reduced to < 2.01 %). Metagenomic sequencing indicated that the higher abundance of narGHI in biofilms, compared to flocs, was crucial for maintaining stable PD performance under antibiotic stress. The electron transport related genes, such as IDH1, DLD and DLAT, were more abundant in biofilms than in flocs after SDZ and CIP addition. These findings provide a theoretical basis for understanding the response mechanism of PD consortia to antibiotic.

01 Jul 2025·Cellular Signalling

Expression of SLC2A1 is upregulated in a mouse model of age-related hearing loss

Article

Author: Xie, Wen ; Liu, Yuehui ; Peng, Haisen ; Hu, Shuihua ; Li, Chunhua ; Zhang, Zhilin ; Liu, Jiali

BACKGROUNDAge-related hearing loss (ARHL) is a common issue associated with aging. One of the typical causes of hearing loss is the irreversible death of hair cells. In addition, oxidative stress contributes to ARHL. However, the underlying molecular mechanism in ARHL is not well understood.METHODSThe ARHL samples were from GSE153882 datasets of the Gene Expression Omnibus database. The Limma R-package was used to identify differentially expressed genes. The hub gene was obtained via intersection of oxidative stress genes and cuproptosis genes. Hearing function was measured using the auditory brainstem response (ABR). Western blot and immunofluorescence were used to examine solute carrier family 2 member 1 protein (SLC2A1), dihydrolipoyl transacetylase (DLAT) an dihydrolipoamide dehydrogenase (DLD) in vitro and in vivo.RESULTSOxidative stress gene SLC2A1 (also named GLUT1) is related to cuproptosis gene in age-related hearing loss. In the ARHL mice model, SLC2A1, DLAT and DLD were elevated. The ABR recordings showed that SLC2A1 knockdown lowered the average thresholds of mice. Knockdown SLC2A1 alleviated DLAT and DLD in vitro and in vivo.CONCLUSIONOur findings highlight SLC2A1 as an essential driver of cuproptosis and ARHL. Knockdown SLC2A1 suppresses ARHL progression via inhibiting cuproptosis.

01 Mar 2025·Biotechnology and Bioengineering

Kinetic Modeling of the Antibody Disulfide Bond Reduction Reaction With Integrated Prediction of the Drug Load Profile for Cysteine‐Conjugated ADCs

Article

Author: Hui, Kimberly ; Wendeler, Michaela ; González, Pedro ; Weggen, Jan Tobias ; Bean, Ryan ; Hubbuch, Jürgen

ABSTRACTAntibody‐drug conjugates (ADC) constitute a groundbreaking advancement in the field of targeted therapy. In the widely utilized cysteine conjugation, the cytotoxic payload is attached to reduced interchain disulfides which involves a reduction of the native monoclonal antibody (mAb). This reaction needs to be thoroughly understood and controlled as it influences the critical quality attributes (CQAs) of the final ADC product, such as the drug‐to‐antibody ratio (DAR) and the drug load distribution (DLD). However, existing methodologies lack a mechanistic description of the relationship between process parameters and CQAs. In this context, kinetic modeling provides comprehensive reaction understanding, facilitating the model‐based optimization of reduction reaction parameters and potentially reduces the experimental effort needed to develop a robust process. With this study, we introduce an integrated modeling framework consisting of a reduction kinetic model for the species formed during the mAb reduction reaction in combination with a regression model to quantify the number of conjugated drugs by DAR and DLD. The species formed during reduction will be measured by analytical capillary gel electrophoresis (CGE), and the DAR and DLD will be derived from reversed‐phase (RP) chromatography. First, we present the development of a reduction kinetic model to describe the impact of reducing agent excess and reaction temperature on the kinetic, by careful investigation of different reaction networks and sets of kinetic rates. Second, we introduce a cross‐analytical approach based on multiple linear regression (MLR), wherein CGE data is converted into the RP‐derived DAR/DLD. By coupling this with the newly developed reduction kinetic model, an integrated model encompassing the two consecutive reaction steps, reduction and conjugation, is created to predict the final DAR/DLD from initial reduction reaction conditions. The integrated model is finally utilized for an in silico screening to analyze the effect of the reduction conditions, TCEP excess, temperature and reaction time, directly on the final ADC product.

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