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the substrate for lyase is sucrase
Lyase enzymes catalyze the breaking of chemical bonds in molecules without using water, while ligase enzymes catalyze the formation of new bonds between molecules using energy from ATP. Lyase enzymes work by eliminating groups from substrates, while ligase enzymes work by joining two molecules together.
Ligase is an enzyme that catalyzes the joining of two molecules by forming a new chemical bond, usually between nucleic acid strands. Lyase is an enzyme that catalyzes the cleavage of a molecule into two separate molecules without the addition of water. In summary, ligase joins molecules, while lyase splits molecules.
Lyase enzymes are found throughout the human body, with different specific lyase enzymes located in various organs and tissues. They play critical roles in various metabolic pathways by catalyzing the removal or addition of functional groups to substrates. Examples include carbon-carbon lyases found in the liver and kidney that are involved in amino acid metabolism.
Phosphoenolpyruvate carboxykinase (PEPCK) is an enzyme in the lyase family.
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Neil Christopher Doherty has written: 'A molecular analysis of hyaluronate lyase production in Streptococcus pneumoniae'
There are a few companies out there that will help with the diagnosis of an amino acid deficiency. ASAL stands for "argininosuccinic acid lyase". One such company is NewBornScreening.
Hugh John Craig has written: 'Molecular analysis of intragenic complementation at the human argininosuccinic acid lyase locus'
DNA ligase catalyzes the formation of a covalent bond between adjacent DNA strands. It plays a crucial role in joining DNA fragments during processes like DNA replication and repair.
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synthases do not use energy from NTP's, sythetases do! synthase can be used with any enzyme that catalyzes synthesis (whether or not it uses nucleoside triphosphates), whereas synthetase is to be used synonymously with 'ligase'.