HLCS Enzyme: Biotin Biosynthesis and Drug Target (G3141)

Target Name: HLCS

NCBI ID: G3141

HLCS

Other Name(s): biotin--[methylmalonyl-CoA-carboxytransferase] ligase | biotin apo-protein ligase | Biotin--[propionyl-CoA-carboxylase [ATP-hydrolyzing]] ligase | HCS | holocarboxylase synthetase | Holocarboxylase synthetase, transcript variant 1 | holocarboxylase synthetase (biotin-(proprionyl-CoA-carboxylase (ATP-hydrolysing)) ligase) | Biotin--protein ligase | Biotin apo-protein ligase | Biotin--protein ligase isoform 1 | Holocarboxylase synthetase (biotin-[proprionyl-Coenzyme A-carboxylase (ATP-hydrolysing)] ligase) | holocarboxylase synthetase (biotin-(proprionyl-Coenzyme A-carboxylase (ATP-hydrolysing)) ligase) | biotin--[acetyl-CoA-carboxylase] ligase | BPL1_HUMAN | HLCS variant 1 | biotin--[methylcrotonoyl-CoA-carboxylase] ligase | Holocarboxylase synthetase

HLCS Enzyme: Biotin Biosynthesis and Drug Target

HLCS (biotin--[methylmalonyl-CoA-carboxytransferase] ligase) is a enzyme that plays a crucial role in the biosynthesis of the vitamin B7 (biotin), also known as vitamin H or folic acid. Biotin is a water-soluble vitamin that is essential for the growth, development, and function of all living organisms. It is synthesized from the amino acid tryptophan, which is derived from the protein tryptophan hydroxylase.

The HLCS enzyme is a key enzyme in the biosynthesis pathway of biotin. It catalyzes the transfer of the methyl group from the amino acid malonyl-CoA to the carbon atom of the amino acid tryptophan, resulting in the formation of 6-methyl-7-carboxy-CoA. This intermediate step is crucial in the biosynthesis pathway, as it allows the construction of the key structural unit of the vitamin B7 molecule.

HLCS is a enzyme that is expressed in various organisms, including bacteria, archaea, and eukaryotes. It is highly conserved across different organisms, and its sequence has been highly characterized. The HLCS enzyme has a single known substrate, malonyl-CoA, and it has a unique catalytic mechanism.

The HLCS enzyme uses a unique Michaelis-Menten kinetics to catalyze the transfer of the methyl group from malonyl-CoA to tryptophan. The kinetics of the reaction are Michaelis-Menten, which means that the rate of the reaction increases as the concentration of the substrate increases. This is in contrast to classic Michaelis-Menten kinetics, where the rate of the reaction decreases as the concentration of the substrate increases.

The Michaelis-Menten kinetics of the HLCS reaction are a result of the unique substrate binding site and the catalytic mechanism. The substrate binding site of the HLCS enzyme is specific for malonyl-CoA, and it has been shown to have high affinity for this ligand. The high affinity of the HLCS enzyme for malonyl-CoA allows it to efficiently transfer the methyl group from malonyl-CoA to tryptophan.

The HLCS enzyme has a unique catalytic mechanism that allows it to efficiently transfer the methyl group from malonyl-CoA to tryptophan. The HLCS enzyme has a single known substrate, malonyl-CoA, and it has a unique catalytic mechanism that allows it to efficiently transfer the methyl group from malonyl-CoA to tryptophan.

The HLCS enzyme has a unique catalytic mechanism that allows it to efficiently transfer the methyl group from malonyl-CoA to tryptophan. The HLCS enzyme has a single known substrate, malonyl-CoA, and it has a unique catalytic mechanism that allows it to efficiently transfer the methyl group from malonyl-CoA to tryptophan.

The HLCS enzyme has been shown to be involved in various cellular processes, including metabolism, growth, and development. It has been shown to be involved in the biosynthesis of tryptophan, which is essential for the growth, development, and function of all living organisms. The HLCS enzyme has also been shown to be involved in the metabolism of other molecules, including nucleotides, lipids, and proteins.

The HLCS enzyme is a potential drug target or biomarker, and it has been shown to have a unique mechanism of action. The HLCS enzyme has a unique catalytic mechanism that allows it to efficiently transfer the methyl group from malonyl-CoA to tryptophan, and this mechanism may be targeted by drugs as a potential therapeutic approach. Further research is needed to fully understand the role of the HLCS enzyme in

Protein Name: Holocarboxylase Synthetase

Functions: Biotin--protein ligase catalyzing the biotinylation of the 4 biotin-dependent carboxylases acetyl-CoA-carboxylase, pyruvate carboxylase, propionyl-CoA carboxylase, and methylcrotonyl-CoA carboxylase

The "HLCS Target / Biomarker Review Report" is a customizable review of hundreds up to thousends of related scientific research literature by AI technology, covering specific information about HLCS comprehensively, including but not limited to:
•   general information;
•   protein structure and compound binding;
•   protein biological mechanisms;
•   its importance;
•   the target screening and validation;
•   expression level;
•   disease relevance;
•   drug resistance;
•   related combination drugs;
•   pharmacochemistry experiments;
•   related patent analysis;
•   advantages and risks of development, etc.
The report is helpful for project application, drug molecule design, research progress updates, publication of research papers, patent applications, etc. If you are interested to get a full version of this report, please feel free to contact us at BD@silexon.ai

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