GCAT Human

Glycine C-Acetyltransferase Human Recombinant

Cat. No.

BT4560

Source

Escherichia Coli.

Synonyms

2-amino-3-ketobutyrate coenzyme A ligase mitochondrial, AKB ligase, EC 2.3.1.29, Aminoacetone synthase, Glycine acetyltransferase, GCAT, KBL.

Appearance

Sterile Filtered clear solution.

Purity

Greater than 85.0% as determined by SDS-PAGE.

Usage

Prospec's products are furnished for LABORATORY RESEARCH USE ONLY. They may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

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Description

GCAT Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 419 amino acids (22-419 a.a) and having a molecular mass of 45kDa.
GCAT is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction

The degradation of L-threonine to glycine involves a two-step biochemical pathway that utilizes the enzymes L-threonine dehydrogenase and 2-amino-3-ketobutyrate coenzyme A ligase. In the first step, L-threonine dehydrogenase converts L-threonine into 2-amino-3-ketobutyrate. Glycine C-Acetyltransferase (GCAT), the second enzyme in this pathway, then catalyzes the reaction between 2-amino-3-ketobutyrate and coenzyme A, resulting in the formation of glycine and acetyl-CoA. GCAT, classified as a class II pyridoxal-phosphate-dependent aminotransferase, exhibits high expression levels in vital organs such as the heart, brain, liver, and pancreas, with detectable expression in the lungs as well.

Description

Recombinant human GCAT, expressed in E. coli, is a non-glycosylated monomeric polypeptide chain consisting of 419 amino acids (specifically, residues 22-419). It has a molecular weight of 45 kDa. The protein includes a 21 amino acid His-tag fused at the N-terminus to facilitate purification, which is achieved through proprietary chromatographic techniques.

Physical Appearance

The product is a clear, sterile-filtered solution.

Formulation

The GCAT protein solution is provided at a concentration of 1 mg/ml and is formulated in a buffer containing 20 mM Tris-HCl (pH 8.0), 0.4 M urea, and 10% glycerol.

Stability

For short-term storage (2-4 weeks), the product can be stored at 4°C. For extended storage, it is recommended to store the product frozen at -20°C. The addition of a carrier protein (0.1% HSA or BSA) is advised for long-term storage. To maintain product integrity, avoid repeated freeze-thaw cycles.

Purity

The purity of the GCAT protein is greater than 85.0% as determined by SDS-PAGE analysis.

Synonyms

2-amino-3-ketobutyrate coenzyme A ligase mitochondrial, AKB ligase, EC 2.3.1.29, Aminoacetone synthase, Glycine acetyltransferase, GCAT, KBL.

Source

Escherichia Coli.

Amino Acid Sequence

MGSSHHHHHH SSGLVPRGSH MSALAQLRGI LEGELEGIRG AGTWKSERVI TSRQGPHIRV DGVSGGILNF CANNYLGLSS HPEVIQAGLQ ALEEFGAGLS SVRFICGTQS IHKNLEAKIA RFHQREDAIL YPSCYDANAG LFEALLTPED AVLSDELNHA SIIDGIRLCK AHKYRYRHLD MADLEAKLQE AQKHRLRLVA TDGAFSMDGD IAPLQEICCL ASRYGALVFM DECHATGFLG PTGRGTDELL GVMDQVTIIN STLGKALGGA SGGYTTGPGP LVSLLRQRAR PYLFSNSLPP AVVGCASKAL DLLMGSNTIV QSMAAKTQRF RSKMEAAGFT ISGASHPICP VMLGDARLAS RMADDMLKRG IFVIGFSYPV VPKGKARIRV QISAVHSEED IDRCVEAFVE VGRLHGALP.

Product Science Overview

Function and Mechanism

The primary function of Glycine C-Acetyltransferase is to catalyze the reaction between 2-amino-3-ketobutyrate and coenzyme A, resulting in the formation of glycine and acetyl-CoA . This reaction is essential for various metabolic pathways, including the metabolism of amino acids and the development of the nervous system.

Genetic Information

The GCAT gene is located on chromosome 22q13.1. It is a protein-coding gene associated with several diseases, such as rheumatic myocarditis and phosphoglycerate dehydrogenase deficiency. The enzyme is a class II pyridoxal-phosphate-dependent aminotransferase, which means it requires vitamin B6 (pyridoxal 5′-phosphate) for its activity.

Expression and Localization

GCAT mRNA is strongly expressed in various human tissues, including the heart, brain, liver, and pancreas. The enzyme’s activity is crucial for maintaining normal physiological processes, and its deficiency or malfunction can lead to metabolic disorders.

Clinical Relevance

The enzyme’s role in glycine metabolism is significant, especially in the context of insulin resistance and diabetes. Plasma glycine levels are often lower in patients with obesity or diabetes, and improving insulin resistance can increase glycine concentration. This highlights the enzyme’s potential impact on metabolic health and its relevance in clinical research.

Recombinant Production

Human recombinant Glycine C-Acetyltransferase is produced using recombinant DNA technology, which involves inserting the human GCAT gene into a suitable expression system, such as bacteria or yeast. This allows for the large-scale production of the enzyme for research and therapeutic purposes.

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GCAT Human

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