Results 21 to 30 of about 101,870 (311)
Current Research in Food Science, 2023 Alginate lyase is essential for the production of alginate oligosaccharides (AOSs), which exhibit diverse bioactivities and have numerous applications in the food and pharmaceutical industries.
Yuting Zheng +5 more
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Marine Drugs, 2021 Alginate, a major acidic polysaccharide in brown algae, has attracted great attention as a promising carbon source for biorefinery systems. Alginate lyases, especially exo-type alginate lyase, play a critical role in the biorefinery process.
Rui Yin +5 more
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Journal of Lipid Research, 2020 Sphingosine 1-phosphate (S1P) lyase is an intracellular enzyme that catalyzes the irreversible degradation of S1P and has been suggested as a therapeutic target for the treatment of psoriasis vulgaris. Because S1P induces differentiation of keratinocytes,
Suwon Jeon +9 more
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Journal of Chemistry, 2020 An important component of the pectinase enzyme complex is pectin lyase (polymethylgalacturonate lyase; EC 4.2.2.10). In this study, extracellular pectin lyase enzyme was produced from Acinetobacter calcoaceticus bacteria.
Esen Tasgin +2 more
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Molecules, 2020 Pectinases are an important class of enzymes distributed in many higher plants and microorganisms. One of these enzymes is pectin lyase which has an important role in industrial applications such as clarification of fruit juices.
Esen Tasgin +3 more
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Adenylosuccinate lyase deficiency [PDF]
Journal of Inherited Metabolic Disease, 2014 AbstractAdenylosuccinate lyase ADSL) deficiency is a defect of purine metabolism affecting purinosome assembly and reducing metabolite fluxes through purine de novo synthesis and purine nucleotide recycling pathways. Biochemically this defect manifests by the presence in the biologic fluids of two dephosphorylated substrates of ADSL enzyme ...
Jurecka, Agnieszka +3 more
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FEMS Microbiology Reviews, 1995 Polysaccharide lyases are the products of various microorganisms, bacteriophage and some eukaryotes. All such enzymes cleave a hexose-1,4-alpha- or beta-uronic acid sequence by beta-elimination. They are in some examples, the only known type of enzymes degrading their polyanionic substrates.
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CyanoLyase: a database of phycobilin lyase sequences, motifs and functions [PDF]
, 2012 CyanoLyase (http://cyanolyase.genouest.org/) is a manually curated sequence and motif database of phycobilin lyases and related proteins. These enzymes catalyze the covalent ligation of chromophores (phycobilins) to specific binding sites of ...
Schluchter, Wendy M. +10 more
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Argininosuccinate lyase deficiency [PDF]
Genetics in Medicine, 2012 The urea cycle consists of six consecutive enzymatic reactions that convert waste nitrogen into urea. Deficiencies of any of these enzymes of the cycle result in urea cycle disorders (UCDs), a group of inborn errors of hepatic metabolism that often result in life-threatening hyperammonemia. Argininosuccinate lyase (ASL) catalyzes the fourth reaction in
Sandesh C S, Nagamani +2 more
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Cryoradiolysis of oxygenated cytochrome P450 17A1 with lyase substrates generates expected products
, 2021 When subjected to γ-irradiation at cryogenic temperatures the oxygenated complexes of Cytochrome P450 17A1 bound with either of the lyase substrates, 17-OH PREG or 17-OH PROG are shown here to generate the corresponding lyase products ...
James, Kincaid +3 more
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