Ask about this productRelated genes to: THTPA antibody
- Gene:
- THTPA NIH gene
- Name:
- thiamine triphosphatase
- Previous symbol:
- -
- Synonyms:
- THTPASE
- Chromosome:
- 14q11.2
- Locus Type:
- gene with protein product
- Date approved:
- 2002-07-25
- Date modifiied:
- 2015-08-14
Related products to: THTPA antibody
Related articles to: THTPA antibody
- Thiamine (vitamin B1) and its phosphates are essential for almost all organisms. Thiamine diphosphate (ThDP) is the major intracellular derivative which is considered the only form functioning as a coenzyme. Thiamine triphosphate (ThTP), another ubiquitous derivative, lacks a clear physiological function and is usually kept at low levels. However, it can accumulate up to 87% of total thiamine in animal tissues lacking cytosolic thiamine triphosphatase (THTPA) activity. Studies of ThTP coenzyme function have always faced the problem of ThTP hydrolysis to ThDP. To avoid such interference a synthetic stable ThTP analog, bismethylene ThTP (bmThTP), has been synthesized. Given that ThTP accumulation is caused by cytosolic THTPA suppression, cytosolic ThDP-dependent transketolase (TKT) is the primary target for probing (bm)ThTP's coenzyme function. Indeed, bmThTP acts as a TKT coenzyme, with the apparent K(bmThTP) of 16.3 µM. However, bmThTP binding slightly differs from that of ThTP. Molecular docking was used to estimate affinities of ThDP, ThTP and bmThTP, also allowing us to avoid ThTP hydrolysis. Despite almost identical localization within the active site, bmThTP could not bind as well as ThTP, resulting in a 2.36 kcal/mol difference in estimated ΔG. Based on our data, calculated K(ThTP) for TKT is about 0.07-0.08 µM, only 1.6-2 times that of K(ThDP). Such a small difference implies that ThTP could physiologically act as the main TKT coenzyme form upon its accumulation in muscles, at least in a few known animal species. - Source: PubMed
Publication date: 2026/02/14
Artiukhov Artem VKazantsev Alexey VSolovjeva Olga NAleshin Vasily A - Although previous studies have examined the relationship between obesity and genetics in response to the growing obesity epidemic, research on the relationship between obesity and long-term changes in body mass index (BMI) is limited. To investigate this relationship, data from 1030 cases in the Anseong and Ansan cohorts were collected from the Korean Genome and Epidemiology Study conducted by the Korea National Institute of Health between 2000 and 2014. Cases lacking participants' BMI data throughout the study were excluded, resulting in a final sample size of 3074. An increase or decrease in BMI was analyzed using PLINK, STRING, and DAVID, with significant differences observed in the , , , , , , , , and genes. These genes were observed to cluster with pathways related to type 2 diabetes, cardiovascular disease, metabolic processes, and endocytosis-related genes. These results suggest that several genes are involved in BMI changes and that several pathways are associated with obesity risk. Moreover, some genetic variants appear to influence BMI changes in Korean adults. - Source: PubMed
Publication date: 2024/08/19
Lee Sang-ImKim Su-KangKang Sang-Wook - The devastating impact of the ongoing coronavirus disease 2019 (COVID-19) on public health, caused by the Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2) has made targeting the COVID-19 pandemic a top priority in medical research and pharmaceutical development. Surveillance of SARS-CoV-2 mutations is essential for the comprehension of SARS-CoV-2 variant diversity and their impact on virulence and pathogenicity. The SARS-CoV-2 open reading frame 10 (ORF10) protein interacts with multiple human proteins CUL2, ELOB, ELOC, MAP7D1, PPT1, RBX1, THTPA, TIMM8B, and ZYG11B expressed in lung tissue. Mutations and co-occurring mutations in the emerging SARS-CoV-2 ORF10 variants are expected to impact the severity of the virus and its associated consequences. In this article, we highlight 128 single mutations and 35 co-occurring mutations in the unique SARS-CoV-2 ORF10 variants. The possible predicted effects of these mutations and co-occurring mutations on the secondary structure of ORF10 variants and host protein interactomes are presented. The findings highlight the possible effects of mutations and co-occurring mutations on the emerging 140 ORF10 unique variants from secondary structure and intrinsic protein disorder perspectives. - Source: PubMed
Publication date: 2021/12/02
Hassan Sk SarifLundstrom KennethSerrano-Aroca ÁngelAdadi PariseAljabali Alaa A ARedwan Elrashdy MLal AmosKandimalla RameshEl-Aziz Tarek Mohamed AbdPal Choudhury PabitraAzad Gajendra KumarSherchan Samendra PChauhan GauravTambuwala MurtazaTakayama KazuoBarh DebmalyaPalu GiorgioBasu PallabUversky Vladimir N - While the cellular functions of the coenzyme thiamine (vitamin B1) diphosphate (ThDP) are well characterized, the triphosphorylated thiamine derivatives, thiamine triphosphate (ThTP) and adenosine thiamine triphosphate (AThTP), still represent an intriguing mystery. They are present, generally in small amounts, in nearly all organisms, bacteria, fungi, plants, and animals. The synthesis of ThTP seems to require ATP synthase by a mechanism similar to ATP synthesis. In , ThTP is synthesized during amino acid starvation, while in plants, its synthesis is dependent on photosynthetic processes. In , ThTP synthesis probably requires oxidation of pyruvate and may play a role at the interface between energy and amino acid metabolism. In animal cells, no mechanism of regulation is known. Cytosolic ThTP levels are controlled by a highly specific cytosolic thiamine triphosphatase (ThTPase), coded by , and belonging to the ubiquitous family of the triphosphate tunnel metalloenzymes (TTMs). While members of this protein family are found in nearly all living organisms, where they bind organic and inorganic triphosphates, ThTPase activity seems to be restricted to animals. In mammals, THTPA is ubiquitously expressed with probable post-transcriptional regulation. Much less is known about the recently discovered AThTP. In , AThTP is synthesized by a high molecular weight protein complex from ThDP and ATP or ADP in response to energy stress. A better understanding of these two thiamine derivatives will require the use of transgenic models. - Source: PubMed
Publication date: 2021/11/07
Bettendorff Lucien - Simultaneous photothermal therapy (PTT) and photodynamic therapy (PDT) is beneficial for enhanced cancer therapy due to the synergistic effect. Conventional materials developed for synergistic PTT/PDT are generally multicomponent agents that need complicated preparation procedures and be activated by multiple laser sources. The emerging monocomponent diketopyrrolopyrrole (DPP)-based conjugated small molecular agents enable dual PTT/PDT under a single laser irradiation, but suffer from low singlet oxygen quantum yield, which severely restricts the therapeutic efficacy. Herein, we report acceptor-oriented molecular design of a donor-acceptor-donor (D-A-D) conjugated small molecule (IID-ThTPA)-based phototheranostic agent, with isoindigo (IID) as selective acceptor and triphenylamine (TPA) as donor. The strong D-A strength and narrow singlet-triplet energy gap endow IID-ThTPA nanoparticles (IID-ThTPA NPs) high mass extinction coefficient (18.2 L g cm), competitive photothermal conversion efficiency (35.4%), and a dramatically enhanced singlet oxygen quantum yield (84.0%) comparing with previously reported monocomponent PTT/PDT agents. Such a high PTT/PDT performance of IID-ThTPA NPs achieved superior tumor cooperative eradicating capability in vitro and in vivo. - Source: PubMed
Publication date: 2020/07/13
Shao WeiYang ChuangLi FangyuanWu JiaheWang NanDing QiangGao JianqingLing Daishun