PDK1 / [Pyruvate Dehydrogenase (Acetyl-Transferring)] Kinase Isozyme 1 Recombinant Protein | PDK1 recombinant protein

Human PDK1 / [Pyruvate Dehydrogenase (Acetyl-Transferring)] Kinase Isozyme 1, Mitochondrial Recombinant Protein

• Applications: ELISA, Western Blot
• Purity: >95% by SDS-PAGE
• Synonyms: PDK1 / [Pyruvate Dehydrogenase (Acetyl-Transferring)] Kinase Isozyme 1; Human PDK1 / [Pyruvate Dehydrogenase (Acetyl-Transferring)] Kinase Isozyme 1; Mitochondrial Recombinant Protein; [Pyruvate dehydrogenase (acetyl-transferring)] kinase isozyme 1; mitochondrial; Pyruvate dehydrogenase kinase isoform 1; PDH kinase 1; PDHK1; PDK1 recombinant protein

• Host: E Coli
• Purity/Purification: >95% by SDS-PAGE
• Form/Format: Liquid; 50mM NaH2PO4, 500mM NaCl Buffer with 500mM Imidazole, 10% Glycerol (PH8.0)
• Concentration: Reconstitution Dependent (varies by lot)
• Sequence Length: 436

• Applicable Applications for PDK1 recombinant protein: ELISA (EIA), Western Blot (WB), Antigen Protein (AP), Protein Array
• Species: Human
• Tag: His
• Subunit: Homodimer, and heterodimer with PDK2. Interacts with the pyruvate dehydrogenase complex subunit DLAT, and is part of the multimeric pyruvate dehydrogenase complex that contains multiple copies of pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (DLAT, E2) and lipoamide dehydrogenase (DLD, E3).
• Entry Function: Kinase that plays a key role in regulation of glucose and fatty acid metabolism and homeostasis via phosphorylation of the pyruvate dehydrogenase subunits PDHA1 and PDHA2. This inhibits pyruvate dehydrogenase activity, and thereby regulates metabolite flux through the tricarboxylic acid cycle, down-regulates aerobic respiration and inhibits the formation of acetyl-coenzyme A from pyruvate. Plays an important role in cellular responses to hypoxia and is important for cell proliferation under hypoxia. Protects cells against apoptosis in response to hypoxia and oxidative stress.
• Preparation and Storage: Store at -20 degree C. Avoid repeated freezing and thawing.

NCBI and Uniprot Product Information

• NCBI GI #: 4505689
• NCBI GeneID: 5163
• NCBI Accession #: NP_002601.1
• NCBI GenBank Nucleotide #: NP_002601.1
• UniProt Accession #: Q15118
• NCBI Official Full Name: [Pyruvate dehydrogenase (acetyl-transferring)] kinase isozyme 1, mitochondrial isoform 2
• NCBI Official Synonym Full Names: pyruvate dehydrogenase kinase 1
• NCBI Official Symbol: PDK1
• NCBI Protein Information: [Pyruvate dehydrogenase (acetyl-transferring)] kinase isozyme 1, mitochondrial; pyruvate dehydrogenase (acetyl-transferring) kinase isozyme 1, mitochondrial
• UniProt Protein Name: [Pyruvate dehydrogenase [lipoamide]] kinase isozyme 1, mitochondrial
• Protein Family: [Pyruvate dehydrogenase
• UniProt Gene Name: PDK1
• UniProt Synonym Gene Names: PDHK1; PDH kinase 1
• UniProt Entry Name: PDK1_HUMAN

NCBI Description

Pyruvate dehydrogenase (PDH) is a mitochondrial multienzyme complex that catalyzes the oxidative decarboxylation of pyruvate and is one of the major enzymes responsible for the regulation of homeostasis of carbohydrate fuels in mammals. The enzymatic activity is regulated by a phosphorylation/dephosphorylation cycle. Phosphorylation of PDH by a specific pyruvate dehydrogenase kinase (PDK) results in inactivation. Multiple alternatively spliced transcript variants have been found for this gene. [provided by RefSeq, Jun 2013]

Uniprot Description

PDHK1: an ubiquitously expressed, atypical protein kinase associated with the mitochondrial matrix. The PDHKs play crucial roles in switching metabolic flux from oxidative phosphorylation towards glycolysis. PDHK1 is detected in heart, pancreatic islets, and skeletal muscles. Contains a HATPase_c catalytic domain, found in several ATP-binding proteins including protein histidine kinases (PHKs), PHDKs, DNA gyrase B, topoisomerases, heat shock proteins, and DNA mismatch repair proteins. PDHK regulates glucose oxidation through inhibitory phosphorylation of the E1 alpha subunit of the mitochondrial pyruvate dehydrogenase complex (PDHC) at any one of 3 inhibitory serine residues. Inhibitory sites 1, 2, and 3 correspond to S293, S300, and S232 in human PDHA1, respectively. Four PDHK isoenzymes have been described, each with different site specificity: all four phosphorylate sites 1 and 2 but at different rates; for site 1 PDHK2 >PDHK4 >PDHK1 >PDHK3; for site 2, PDHK3> PDHK4 > PDHK2 > PDHK1. Only PDHK1 phosphorylates site 3. PDHKs are recruited to the PDHC by binding to a lipoyl group covalently attached to the inner lipoyl domain of the E2 component. PDHA1 deficiency is the most common enzyme defect in patients with primary lactic acidosis. PDHK1 is a direct HIF-1 target gene. Suppression of PDH by PDHK inhibits the conversion of pyruvate to acetyl-CoA, attenuates mitochondrial respiration, and may contribute to the increased lactate production observed in many tumors. The PDH pathway is repressed in a majority of non-small cell lung carcinomas. Inhibited by AZD7545, dichloroacetate (DCA) and radicicol. Radicicol inhibits kinase activity by binding directly to the ATP-binding pocket of PDHK, similar to HSP90 from the same ATPase/kinase superfamily.

Protein type: Kinase, protein; EC 2.7.11.2; Protein kinase, atypical; Mitochondrial; ATYPICAL group; PDHK family

Chromosomal Location of Human Ortholog: 2q31.1

Cellular Component: mitochondrion; mitochondrial matrix; mitochondrial pyruvate dehydrogenase complex

Molecular Function: protein binding; pyruvate dehydrogenase (acetyl-transferring) kinase activity; ATP binding; protein kinase activity

Biological Process: cell proliferation; cellular metabolic process; glucose metabolic process; regulation of acetyl-CoA biosynthetic process from pyruvate; pyruvate metabolic process; induction of apoptosis by oxidative stress; protein amino acid phosphorylation