lyase

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Related to Lyases: Isomerases, Transferases

ly·ase

 (lī′ās′)
n.
Any of a class of enzymes that catalyze the cleavage of bonds without hydrolysis or oxidation, often resulting in a new double bond or ring structure, or that catalyze the addition of chemical groups to double bonds.

[Greek lūein, to loosen; see leu- in Indo-European roots + -ase.]

lyase

(ˈlaɪeɪz)
n
(Biochemistry) any enzyme that catalyses the separation of two parts of a molecule by the formation of a double bond between them
[C20: from Greek lusis a loosening + -ase]
Translations
liasa
References in periodicals archive ?
Scott et al., "Characterization of secreted sphingosine-1-phosphate lyases required for virulence and intracellular survival of Burkholderia pseudomallei," Molecular Microbiology, vol.
The aim of this project is to provide training in the multidisciplinary fields of organic chemistry, bio-catalysis, molecular biology, biochemistry and microbiology to design and develop artificial cascades by combining various types of enzymes such as L-amino acid oxidases, alcohol dehydrogenases and lyases. This is a truly competitive, innovative and timely field in which to work, and for sure the results derived from this cutting-edge project will be published in top ranked journals contributing to European Excellence.
Over 30% of known enzymes are metalloenzymes, covering all major enzyme classes: oxidoreductases, transferases, hydrolases, lyases, isomerases, and ligases.
We know that DMSP and DMS production is highly variable between and within the different groups of producers, but the reasons for this variability are not understood, mainly because genes encoding DMSP synthesis enzymes have yet to be identified and DMSP lyases have only just been identified in a DMSP-producing organism.
We applied dbCAN [30] with default parameters and identified a total of 301 CAZyme-coding gene homologs (Appendix S4), which includes 127 glycoside hydrolases (GH), 64 glycosyltransferases (GT), 55 carbohydrate esterases (CE), 30 with auxiliary activities (AA), 19 carbohydrate binding module (CBM), and 6 polysaccharide lyases (PL).
They cover considerations for applying process technologies in laboratory-scale and pilot-scale biocatalysis for chemical synthesis; cytochrome P450 progress in biocatalysis for synthetic organic chemistry; using hydrolases and related enzymes for synthesis; non-redux lyases and transferases for forming bonds of carbon with carbon, oxygen, sulfur, and nitrogen; oxidations; reductions; halogenation and dehalogenation; cascade reactions; and biocatalysis for industrial process development.
Snake venom is a mixture of different enzymes like Oxydoreductase Transferase Hydrolases and Lyases.
The former enzyme deesterifies pectin by the removal of methoxy residues and is called pectin methoxy esterase (PME), while the latter splits the main chain and is further classified as polygalacturonase (PG) and pectin lyases (PL) [17-19].
Increased activity of polyphenol oxidase (PPO), peroxidase (POX), phenylalanine ammonia lyase (PAL), and tyrosine ammonia lyases (TAL) had been reported in plants treated with various biotic and abiotic inducers of resistance [33-35].
Differing from other polysaccharide lyases acting on the polysaccharide backbone, xanthan lyase could cleave the linkage between the terminal mannosyl and the glucuronyl residues on the side chain by a [beta]-elimination reaction, introducing a double bond between C4 and C5 of the uronosyl residue and subsequently might be exploited for further chemical modification [13].
According to the mode of action and preferred substrate, pectinases can be briefly classified into two main groups [39]: de-esterification (pectin methyl esterase) which removes methoxyl groups from pectin, and depolymerization (hydrolyses and lyases) which cleaves the bonds between galacturonic acid units.
He covers chiral discrimination in the active site of oxidoreductases, transferases and chiral discrimination, the influence of chirality on the hydrolysis reactions within the active site of hydrolases, the influence of chirality on the reactions in the active site of lyases, and chiral discrimination in the active site of ligases.