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In biochemistry, isozymes (also known as isoenzymes or more generally as multiple forms of enzymes) are enzymes that differ in amino acid sequence but catalyze the same chemical reaction. Isozymes usually have different kinetic parameters (e.g. different K M values), or are regulated differently.
Four isozymes of pyruvate kinase expressed in vertebrates: L (liver), R (erythrocytes), M1 (muscle and brain) and M2 (early fetal tissue and most adult tissues). The L and R isozymes are expressed by the gene PKLR, whereas the M1 and M2 isozymes are expressed by the gene PKM2. The R and L isozymes differ from M1 and M2 in that they are ...
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In cell biology, protein kinase C, commonly abbreviated to PKC (EC 2.7.11.13), is a family of protein kinase enzymes that are involved in controlling the function of other proteins through the phosphorylation of hydroxyl groups of serine and threonine amino acid residues on these proteins, or a member of this family.
Two isozymes are encoded by the PKM gene: PKM1 and PKM2. The M-gene consists of 12 exons and 11 introns.PKM1 and PKM2 are different splicing products of the M-gene (exon 9 for PKM1 and exon 10 for PKM2) and solely differ in 23 amino acids within a 56-amino acid stretch (aa 378–434) at their carboxy terminus.
228026 Ensembl ENSG00000152256 ENSMUSG00000006494 UniProt Q15118 Q8BFP9 RefSeq (mRNA) NM_001278549 NM_002610 NM_172665 NM_001360002 RefSeq (protein) NP_001265478 NP_002601 NP_766253 NP_001346931 Location (UCSC) Chr 2: 172.56 – 172.61 Mb Chr 2: 71.7 – 71.73 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Pyruvate dehydrogenase lipoamide kinase isozyme 1, mitochondrial is an enzyme ...
This 85-kDa protein is one of two subunit types that comprise the seven tetrameric PFK isozymes. [6] [7] The muscle isozyme is composed solely of PFKM.[6] [8] [9] The liver PFK (PFK-5) contains solely the second subunit type, PFKL, while the erythrocyte PFK includes five isozymes composed of different combinations of PFKM and PFKL.
The primary sequencing between the four isozymes are conserved with 70% identity. The greatest differences occur near the N-terminus. [2] PDK1 is the largest of the four with 436 residues while PDK2, PDK3 and PDK4 have 407, 406, and 411 residues respectively. The isozymes have different activity and phosphorylation rates at each site.