Sah Hydrolase
Sah Hydrolase - Related Videos
01:22
Lysosomal Hydrolases
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2023
Lysosomes are the site for the degradation of macromolecules and biological polymers released during membrane trafficking events such as secretory, endocytic, autophagic, and phagocytic pathways. The membrane-enclosed area of the lysosome, called the lumen, contains hydrolytic enzymes active in an acidic environment. These acid hydrolases are functional at a pH between 4.5 and 5 and are involved in cellular processes such as cell signaling, energy metabolism, restoration of the plasma membrane,...
10:21
Expression, Purification, Crystallization, and Enzyme Assays of Fumarylacetoacetate Hydrolase Domain-Containing Proteins
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Cited by 6 •
2019
Expression and purification of fumarylacetoacetate hydrolase domain-containing proteins is described with examples (expression in E. coli, FPLC). Purified proteins are used for crystallization and antibody production and employed for enzyme assays. Selected photometric assays are presented to display the multi-functionality of FAHD1 as oxaloacetate decarboxylase and acylpyruvate hydrolase.
17:12
Profiling of Methyltransferases and Other S-adenosyl-L-homocysteine-binding Proteins by Capture Compound Mass Spectrometry (CCMS)
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Cited by 13 •
2010
Capture Compounds are trifunctional small molecules to reduce the complexity of the proteome by functional reversible small molecule-protein interaction followed by photo-crosslinking and purification. Here we use a Capture Compound with S-adenosyl-L-homocysteine-binding as selectivity function to isolate methyltransferases from an Escherichia coli whole cell lysate and identify them by MS.
06:14
Growth, Purification, and Titration of Oncolytic Herpes Simplex Virus
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Cited by 6 •
2021
In this manuscript, we describe a simple method of growth, purification, and titration of the oncolytic herpes simplex virus for preclinical use.
16:38
Bridging the Bio-Electronic Interface with Biofabrication
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Cited by 3 •
2012
This article describes a biofabrication approach: deposition of stimuli-responsive polysaccharides in the presence of biased electrodes to create biocompatible films which can be functionalized with cells or proteins. We demonstrate a bench-top strategy for the generation of the films as well as their basic uses for creating interactive biofunctionalized surfaces for lab-on-a-chip applications.
FAQs
NAD+ supports the redox chemistry that enables SAH hydrolase to process its substrate. Rather than serving only as a passive binding component, it participates in the enzyme’s NAD+-dependent reaction mechanism, allowing the reversible conversion to proceed. This links methylation control to redox-dependent enzyme function and provides a mechanistic basis for studying the protein in cellular metabolism.
Because the reaction is reversible, the concentrations of its products, adenosine and homocysteine, influence its net direction. Removing these products helps pull the reaction toward SAH breakdown. This principle is important biologically because efficient product removal can support continued clearance of SAH, reducing pressure on methyltransferase reactions that are sensitive to SAH levels.
SAH inhibits many methyltransferases that use S-adenosylmethionine-dependent chemistry. If SAH is not effectively processed, this inhibition can restrict methyl-group transfer to DNA, RNA, proteins, and small molecules. SAH hydrolase therefore affects methylation indirectly: its activity helps preserve conditions in which diverse methyltransferase-dependent reactions can continue.
Research on this enzyme can connect metabolic regulation with epigenetic control and disease mechanisms. Investigators can consider how altered SAH processing may influence methylation involving DNA, RNA, proteins, or small molecules. Examining these relationships helps place the enzyme within broader biological systems rather than treating it as an isolated catalyst.
Its relevance arises through control of SAH, an inhibitor of many methyltransferases. Since methylation reactions can involve DNA and RNA, changes in SAH hydrolase function may affect the biochemical environment supporting these modifications. This makes the enzyme useful in studies linking metabolic regulation with epigenetic control and with biological outcomes associated with altered methylation.
Inhibiting SAH hydrolase can be studied as a way to alter SAH-dependent control of methyltransferases. The resulting effects on methylation provide a rationale for examining the enzyme in disease-related research and in efforts to develop antiviral compounds. Its therapeutic interest therefore comes from manipulating a metabolic regulator that influences several methylation-dependent processes.