Search results
Results from the WOW.Com Content Network
The naming of ligases is inconsistent and so these enzymes are commonly known by several different names. Generally, the common names of ligases include the word "ligase", such as in DNA ligase , an enzyme commonly used in molecular biology laboratories to join together DNA fragments.
Herbivores and carnivores are examples of organisms that obtain carbon and electrons or hydrogen from living organic matter. Chemoorganotrophs are organisms which use the chemical energy in organic compounds as their energy source and obtain electrons or hydrogen from the organic compounds, including sugars (i.e. glucose ), fats and proteins. [ 2 ]
Function: Amylase is an enzyme that is responsible for the breaking of the bonds in starches, polysaccharides, and complex carbohydrates to be turned into simple sugars that will be easier to absorb. Clinical Significance: Amylase also has medical history in the use of Pancreatic Enzyme Replacement Therapy (PERT). One of the components is ...
The structure of this enzyme is highly conserved to maintain precisely the alignment of electron donor NADPH and acceptor FAD for efficient electron transfer. [26] The two electrons in reduced FAD are transferred one a time to adrenodoxin which in turn donates the single electron to the heme group of the mitochondrial P450. [27]
EcoRI for example generates an AATT end, and since A and T have lower melting temperature than C and G, its melting temperature T m is low at around 6 ° C. [21] For most restriction enzymes, the overhangs generated have a T m that is around 15 ° C. [20] For practical purposes, sticky end ligations are performed at 12-16 ° C, or at room ...
For example, an enzyme that catalyzed this reaction would be an oxidoreductase: A – + B → A + B – In this example, A is the reductant (electron donor) and B is the oxidant (electron acceptor). In biochemical reactions, the redox reactions are sometimes more difficult to see, such as this reaction from glycolysis:
This enzyme catalyses the removal of two reducing equivalents from the cysteine residue of the C-terminal meso-lanthionine of epidermin to form a --C==C-- double bond [12] The B chain of dipicolinate synthase, an enzyme which catalyses the formation of dipicolinic acid from dihydroxydipicolinic acid [13]
Examples include the active sites of a number of enzymes: Structure of the FeMoco cluster in nitrogenase. The cluster is linked to the protein by the amino acid residues cysteine and histidine. Nitrogenase include two P-clusters ([8Fe-7S]) and two FeMocos ([7Fe-9S-C-Mo-R homocitrate]). [8]