HYKK Human

Hydroxylysine Kinase Human Recombinant
Cat. No.
BT10381
Source
E.coli.
Synonyms
Hydroxylysine kinase, AGPHD1, 5-hydroxy-L-lysine kinase, HYKK, Aminoglycoside phosphotransferase domain-containing protein 1.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 90% as determined by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

HYKK Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 396 amino acids (1-373a.a) and having a molecular mass of 44.3kDa.
HYKK is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
Hydroxylysine Kinase, also known as HYKK, is a protein-coding gene. HYKK, a member of the aminoglycoside phosphotransferase family, catalyzes the GTP-dependent phosphorylation of 5-hydroxy-L-lysine.
Description
Recombinant human HYKK, produced in E. coli, is a single, non-glycosylated polypeptide chain containing 396 amino acids (residues 1-373) and having a molecular mass of 44.3 kDa. HYKK is fused to a 23 amino acid His-tag at the N-terminus and purified using proprietary chromatographic techniques.
Physical Appearance
Sterile, colorless solution.
Formulation
HYKK solution (0.5 mg/mL) contains Phosphate Buffered Saline (pH 7.4), 40% glycerol, 1 mM DTT, and 0.1 mM PMSF.
Stability
Store at 4°C if the entire vial will be used within 2-4 weeks. Store frozen at -20°C for longer periods. For long-term storage, adding a carrier protein (0.1% HSA or BSA) is recommended. Avoid multiple freeze-thaw cycles.
Purity
Greater than 90% purity as determined by SDS-PAGE.
Synonyms
Hydroxylysine kinase, AGPHD1, 5-hydroxy-L-lysine kinase, HYKK, Aminoglycoside phosphotransferase domain-containing protein 1.
Source
E.coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMSSGNYQ QSEALSKPTF SEEQASALVE SVFGLKVSKV RPLPSYDDQN FHVYVSKTKD GPTEYVLKIS NTKASKNPDL IEVQNHIIMF LKAAGFPTAS VCHTKGDNTA SLVSVDSGSE IKSYLVRLLT YLPGRPIAEL PVSPQLLYEI GKLAAKLDKT LQRFHHPKLS SLHRENFIWN LKNVPLLEKY LYALGQNRNR EIVEHVIHLF KEEVMTKLSH FRECINHGDL NDHNILIESS KSASGNAEYQ VSGILDFGDM SYGYYVFEVA ITIMYMMIES KSPIQVGGHV LAGFESITPL TAVEKGALFL LVCSRFCQSL VMAAYSCQLY PENKDYLMVT AKTGWKHLQQ MFDMGQKAVE EIWFETAKSY ESGISM.

Product Science Overview

Introduction

Hydroxylysine kinase (HYKK) is an enzyme that plays a crucial role in the metabolism of lysine, an essential amino acid. This enzyme is responsible for the phosphorylation of 5-hydroxy-L-lysine, a post-translationally modified form of lysine, using GTP as a phosphate donor . The human recombinant form of this enzyme is produced through recombinant DNA technology, allowing for its study and application in various research and therapeutic contexts.

Gene and Protein Information

The HYKK gene, also known as AGPHD1 (Aminoglycoside Phosphotransferase Domain-Containing Protein 1), is located on chromosome 15 in humans . The gene encodes a protein that is involved in the lysine degradation pathway, specifically in the saccharopine pathway . The enzyme is predicted to be located in the mitochondrial matrix, where it catalyzes the GTP-dependent phosphorylation of 5-hydroxy-L-lysine .

Enzymatic Activity

Hydroxylysine kinase catalyzes the following chemical reaction: [ \text{GTP} + \text{5-hydroxy-L-lysine} \rightarrow \text{GDP} + \text{5-phosphonooxy-L-lysine} ] This reaction is essential for the metabolism of hydroxylysine, converting it into a phosphorylated form that can be further processed by other enzymes .

Biological Significance

The phosphorylation of hydroxylysine by HYKK is a critical step in the lysine degradation pathway. This pathway is important for the catabolism of lysine, which is necessary for maintaining amino acid balance and producing energy in the form of ATP . Additionally, the products of lysine degradation are involved in various metabolic processes, including the synthesis of carnitine, a molecule essential for fatty acid metabolism .

Recombinant Production

The human recombinant form of hydroxylysine kinase is produced using recombinant DNA technology. This involves inserting the HYKK gene into a suitable expression vector, which is then introduced into a host organism, such as E. coli or yeast. The host organism expresses the HYKK protein, which can be purified and used for research or therapeutic purposes .

Research and Therapeutic Applications

Recombinant hydroxylysine kinase is valuable for studying the enzyme’s structure, function, and role in lysine metabolism. It can also be used to investigate the molecular mechanisms underlying certain metabolic disorders, such as 5-hydroxylysinuria, which is characterized by the accumulation of hydroxylysine in the body . Furthermore, understanding the function of HYKK may provide insights into the development of new therapeutic strategies for treating metabolic diseases.

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