WebThiomorpholine forms complexes with Cu(II), Pt(II) and Ni(II) salts and their catalytic activity has been investigated. Application. Thiomorpholine has been used in the preparation of: … WebApr 11, 2024 · Biotransformation of lignocellulose-derived synthetic gas (syngas) into acetic acid is a promising way of creating biochemicals from lignocellulosic waste materials. Acetic acid has a growing market with applications within food, plastics and for upgrading into a wide range of biofuels and bio-products. In this paper, we will review the microbial …
UniProt
WebNov 22, 2024 · Described herein are compounds and methods for tethering proteins. For example, dimers of Protein X listed in Table 1 are described, where the dimers are formed by the covalent bonding of a cysteine on the first monomer to a cysteine on the second monomer via a cyclic disulfide linker. The covalently attached dimers exhibit increased … Webthiomorpholine-carboxylate dehydrogenase from Creative Enzymes. Be the first to write a review! Citations: Description The product is the cyclic imine of the 2-oxoacid corresponding to S-(2-aminoethyl)cysteine. In the reverse direction, a number of other cyclic unsaturated compounds can act as substrates, but more slowly html lateral bar
Rat Thiomorpholine-carboxylate dehydrogenase ELISA Kit
WebApr 10, 2024 · 2.2.2 Aldehyde dehydrogenase and aldehyde reductase The thioester may also be formed by a proteinogenic cysteine. A recent publication showed that the adenosine monophosphate (AMP)-anhydride of hydroxylated 2,2′-bipyridine-1-carboxylate reacted with a C-terminal cysteine of CaeB2, a protein with high similarity to NADPH-dependent … WebThe systematic name of this enzyme class is thiomorpholine-3-carboxylate:NAD(P)+ 5,6-oxidoreductase. Other names in common use include ketimine reductase, and ketimine-reducing enzyme. CRYM, a taxon-specific crystallin protein that also binds thyroid hormones has thiomorpholine-carboxylate dehydrogenase activity. References http://amigo.geneontology.org/amigo/term/GO:0047127 html li padding left