103290-07-9Relevant articles and documents
Specificity of lysine: N6-hydroxylase: A hypothesis for a reactive substrate intermediate in the catalytic mechanism
Marrone,Siemann,Beecroft,Viswanatha
, p. 401 - 416 (1996)
The recombinant cytoplasmic preparation of lysine: N6-hydroxylase catalyzes the conversion of L-lysine to its N6-hydroxy derivative when supplemented with the cofactors NADPH and FAD. A number of lysine analogs reflecting minor alterations in the inherent structural features of the amino acid as well compounds with relatively high affinity for lysine binding domains in other proteins were examined for their ability to serve as substrates of lysine: N6-hydroxylase. These studies have revealed that the enzyme does not tolerate any change in the structural features of L-lysine, its preferred substrate, with the exception of the replacement of the C(γ)H2-methylene group by sulfur, as in (S)-2-aminoethyl-L-cysteine. L-Norleucine is a potent inhibitor of the enzyme while L-norvaline and L-α-aminobutyric acid do not exhibit such effect, indicating the importance of a C4 hydrophobic side chain for effective interaction with the enzyme. Among the N-alkyl amides of hydrophobic amino acids, only L-norleucine methylamide and L-α-aminobutyric acid ethylamide serve as moderate inhibitors of lysine: N6-hydroxylase. Based on the enzyme's stringent substrate specificity, a mechanism involving the conversion of L-lysine to 2-aminocaprolactam prior to its oxygenation by the 4α-peroxyflavin intermediate in the catalytic cycle is proposed.
Microporous Molecular Materials from Dipeptides Containing Non-proteinogenic Residues
Yadav, Vitthal N.,Comotti, Angiolina,Sozzani, Piero,Bracco, Silvia,Bonge-Hansen, Tore,Hennum, Martin,G?rbitz, Carl Henrik
, p. 15684 - 15688 (2015)
Dipeptides with two hydrophobic side chains have proved to be an exceptional source of microporous organic materials, but since previous structures were limited to the incorporation of only proteinogenic residues, their full potential as adsorbents has remained unexplored. Single-crystal XRD data for ten new compounds with non-proteinogenic L-2-aminobutanoic acid and/or L-2-amino-pentanoic acid are presented. The gas-phase accessibility of their crystal pores, with cross-sections of 2.3 to 5.1?, was monitored by CO2 and CH4 adsorption isotherms. Included CO2 was also detected spectroscopically by 2D MAS NMR. An extensive conformational analysis reveals that the use of linear rather than branched side chains (such as L-valine and L-isoleucine) affords peptides with a greater degree of conformational freedom and yields more-flexible channel surfaces that may easily adapt to a series of potential guest molecules.
Domino Aryne Annulation via a Nucleophilic-Ene Process
Xu, Hai,He, Jia,Shi, Jiarong,Tan, Liang,Qiu, Dachuan,Luo, Xiaohua,Li, Yang
supporting information, p. 3555 - 3559 (2018/03/21)
1,2-Benzdiyne equivalents possess the unique property that they can react with two arynophiles through iteratively generated 1,2- and 2,3-aryne intermediates. Upon rational modification on the second leaving group of these aryne precursors, a domino aryne annulation approach was developed through a nucleophilic-ene reaction sequence. Various benzo-fused N-heterocyclic frameworks were achievable under transition metal-free conditions with a broad substrate scope.
Expanding the peptide β -turn in α γ hybrid sequences: 12 atom hydrogen bonded helical and hairpin turns
Chatterjee, Sunanda,Vasudev, Prema G.,Raghothama, Srinivasarao,Ramakrishnan, Chandrasekharan,Shamala, Narayanaswamy,Balaram, Padmanabhan
supporting information; experimental part, p. 5956 - 5965 (2009/09/24)
Hybrid peptide segments containing contiguous a and y amino acid residues can form C 12 hydrogen bonded turns which may be consideredas backbone expanded analogues of C 10 OS-turns) found in aa segments. Exploration of the regular hy
