Isoenzymes. Alloenzymes . Allozymes . Isozymes . Structurally related forms of an enzyme. Each isoenzyme has the same mechanism and classification, but differs in its chemical, physical, or immunological characteristics. . 1.00
Myosins. ATPase, Actin-Activated . ATPase, Actomyosin . ATPase, Myosin . Actin-Activated ATPase . Actomyosin ATPase . Actomyosin Adenosinetriphosphatase . Adenosine Triphosphatase, Myosin . Adenosinetriphosphatase, Actomyosin . Adenosinetriphosphatase, Myosin . Myosin . Myosin Adenosinetriphosphatase . ATPase, Actin Activated . Actin Activated ATPase . Myosin Adenosine Triphosphatase . Myosin ATPase . ACTOMYOSIN ADENOSINETRIPHOSPHATASE . ADENOSINETRIPHOSPHATASE, ACTOMYOSIN . ADENOSINETRIPHOSPHATASE, MYOSIN . ATPASE, ACTOMYOSIN . ATPASE, MYOSIN . MYOSIN ADENOSINETRIPHOSPHATASE . MYOSIN ISOENZYMES . MYOSIN ISOZYMES . MYOSIN . A diverse superfamily of proteins that function as translocating proteins. They share the common characteristics of being able to bind ACTINS and hydrolyze MgATP. Myosins generally consist of heavy chains which are involved in locomotion, and light chains which are involved in regulation. Within the structure of myosin heavy chain are three domains: the head, the neck and the tail. The head region of the heavy chain contains the actin binding domain and MgATPase domain which provides energy for locomotion. The neck region is involved in binding the light-chains. The tail region provides the anchoring point that maintains the position of the heavy chain. The superfamily of myosins is organized into structural classes based upon the type and arrangement of the subunits they contain. . 0.75
Creatine Kinase. ADP Phosphocreatine Phosphotransferase . ATP Creatine Phosphotransferase . Macro-Creatine Kinase . Creatine Phosphotransferase, ATP . Kinase, Creatine . Macro Creatine Kinase . Phosphocreatine Phosphotransferase, ADP . Phosphokinase, Creatine . Phosphotransferase, ADP Phosphocreatine . Phosphotransferase, ATP Creatine . Creatine Phosphokinase . CREATINE KINASE ISOENZYMES . CREATINE KINASE ISOZYMES . A transferase that catalyzes formation of PHOSPHOCREATINE from ATP + CREATINE. The reaction stores ATP energy as phosphocreatine. Three cytoplasmic ISOENZYMES have been identified in human tissues: the MM type from SKELETAL MUSCLE, the MB type from myocardial tissue and the BB type from nervous tissue as well as a mitochondrial isoenzyme. Macro-creatine kinase refers to creatine kinase complexed with other serum proteins. . 0.62
beta-N-Acetylhexosaminidases. N-Acetyl-beta-D-hexosaminidase . beta-Hexosaminidase . beta-N-Acetyl-D-hexosaminidase . beta-N-Acetyl-hexosaminidase . N Acetyl beta D hexosaminidase . beta Hexosaminidase . beta N Acetyl D hexosaminidase . beta N Acetyl hexosaminidase . beta N Acetylhexosaminidase . beta N Acetylhexosaminidases . beta-N-Acetylhexosaminidase . beta-Hexosaminidase . HEXOSAMINIDASE ISOENZYMES . HEXOSAMINIDASE ISOZYMES . A hexosaminidase specific for non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides. It acts on GLUCOSIDES; GALACTOSIDES; and several OLIGOSACCHARIDES. Two specific mammalian isoenzymes of beta-N-acetylhexoaminidase are referred to as HEXOSAMINIDASE A and HEXOSAMINIDASE B. Deficiency of the type A isoenzyme causes TAY-SACHS DISEASE, while deficiency of both A and B isozymes causes SANDHOFF DISEASE. The enzyme has also been used as a tumor marker to distinguish between malignant and benign disease. . 0.61
L-Lactate Dehydrogenase. Dehydrogenase, L-Lactate . Dehydrogenase, Lactate . L Lactate Dehydrogenase . Lactate Dehydrogenase . LACTATE DEHYDROGENASE ISOENZYMES . LACTATE DEHYDROGENASE ISOZYMES . A tetrameric enzyme that, along with the coenzyme NAD+, catalyzes the interconversion of LACTATE and PYRUVATE. In vertebrates, genes for three different subunits (LDH-A, LDH-B and LDH-C) exist. . 0.57
Muramidase. Leftose . N-Acetylmuramide Glycanhydrolase . Glycanhydrolase, N-Acetylmuramide . N Acetylmuramide Glycanhydrolase . Lysozyme . A basic enzyme that is present in saliva, tears, egg white, and many animal fluids. It functions as an antibacterial agent. The enzyme catalyzes the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrin. EC 3.2.1.17. . 0.51
Carbonic Anhydrase IV. Carbonic Anhydrase 4 . Carbonic Anhydrase Isozyme IV . Anhydrase 4, Carbonic . A membrane-bound carbonic anhydrase found in lung capillaries and kidney. . 0.50
Carbonic Anhydrase V. Carbonic Anhydrase Isozyme V . A carbonic anhydrase isoenzyme found in MITOCHONDRIA where it provides bicarbonate ions that are components in the urea cycle and in GLUCONEOGENESIS. . 0.49