(4,6'-Bi-2H-1-benzopyran)-3,3',5,5',7,7'-hexol, 2,2'-bis(3,4-dihydroxyphenyl)-3,3',4,4'-tetrahydro-, (2R-(2-alpha,3-alpha,4-beta(2'R*,3'R*)))-/Procyanidin dimer B5/(2R,3R)-2-(3,4-dihydroxyphenyl)-6-[(2R,3R,4S)-2-(3,4-dihydroxyphenyl)-3,5,7-trihydroxy-3,4-dihydro-2H-chromen-4-yl]-3,4-dihydro-2H-chromene-3,5,7-triol/Procyanidol B5/(2R,2?R,3R,3?R,4S)-2,2'-bis(3,4-dihydroxyphenyl)-3,3?,4,4?-tetrahydro-2H,2?H-4,6?-bichromene-3,3?,5,5?,7,7?-hexol/Proanthocyanidin B5/Procyanidin B5
1009.6ºC at 760 mmHg
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provides coniferyl ferulate(CAS#:12798-57-1) MSDS, density, melting point, boiling point, structure, formula, molecular weight etc. Articles of coniferyl ferulate are included as well.>> amp version: coniferyl ferulate
Protein ageing is often mediated by the formation of succinimide intermediates. These short-lived intermediates derive from asparaginyl deamidation and aspartyl dehydration and are rapidly converted into β-aspartyl or d-aspartyl residues. Here we report the presence of a highly stable succinimide intermediate in the glutaminase subunit of GMP synthetase from the hyperthermophile Methanocaldoccocus jannaschii. By comparing the biophysical properties of the wild-type protein and of several mutants, we show that the presence of succinimide increases the structural stability of the glutaminase subunit. The protein bearing this modification in fact remains folded at 100 °C and in 8 M guanidinium chloride. Mutation of the residue following the reactive asparagine provides insight into the factors that contribute to the hydrolytic stability of the succinimide. Our findings suggest that sequences that stabilize succinimides from hydrolysis may be evolutionarily selected to confer extreme thermal stability.
Unexpected functional implication of a stable succinimide in the structural stability of Methanocaldococcus jannaschii glutaminase
Sanjeev Kumar,1 Sunita Prakash,2 Kallol Gupta,2,* Aparna Dongre,1 Padmanabhan Balaram,2 and Hemalatha Balarama,1
The ability to apply rules for environmental adaptation is crucial for human life. This capacity may require high-order cognitive control, such as when managing personal behavior by selecting among context-dependent internal rules. This process is poorly understood in children, especially in terms of the age at which multiple-rules processing becomes possible. We created a child-appropriate “rule management paradigm” to elucidate developmental changes in rule processing, and used it to investigate the trajectory of the rule management system in 322 children aged 4 to 6 years, with comparison to 57 adults. We found age-specific capacities in multiple-rules processing, with the majority of 4-year-olds failing at concurrent management of multiple-rules processing, a capacity that became well developed by age 6. Task performance in multiple-rules processing improved steeply with age and approached the adult level by late age 6. By contrast, single-rule processing on single-feature stimuli approached the adult level by age 5. Our main findings suggest that the critical period for the development of the multiple-rules processing system occurs before age 7, and is associated with the developmental period of the rule management system and other cognitive resources.
Developmental trajectory of rule management system in children
Taeko Harada,corresponding author1 Motoharu Tsuruno,2 and Tetsuya Shirokawa3
N-alkylated polyamine analogues have potential as anticancer and antiparasitic drugs. However, their metabolism in the host has remained incompletely defined thus potentially limiting their utility. Here, we have studied the degradation of three different spermine analogues N,N′-bis-(3-ethylaminopropyl)butane-1,4-diamine (DESPM), N-(3-benzyl-aminopropyl)-N’-(3-ethylaminopropyl)butane-1,4-diamine (BnEtSPM) and N,N′-bis-(3-benzylaminopropyl)butane-1,4-diamine (DBSPM) and related mono-alkylated derivatives as substrates of recombinant human polyamine oxidase (APAO) and spermine oxidase (SMO). APAO and SMO metabolized DESPM to EtSPD (Km(APAO)=10μM, kcat(APAO)=1.1s?1 and Km(SMO)=28μM, kcat(SMO)=0.8s?1, respectively), metabolized BnEtSPM to EtSPD (Km(APAO)=0.9 μM, kcat(APAO)=1.1s?1 and Km(SMO)=51μM, kcat(SMO)=0.4s?1, respectively), and metabolized DBSPM to BnSPD (Km(APAO)=5.4μM, kcat(APAO)= 2.0s?1 and Km(SMO)=33μM, kcat(SMO)=0.3s?1, respectively). Interestingly, mono-alkylated spermine derivatives were metabolized by APAO and SMO to SPD (EtSPM Km(APAO)=16μM, kcat(APAO)=1.5s?1; Km(SMO)=25μM, kcat(SMO) =8.2s?1; BnSPM Km(APAO)=6.0μM, kcat(APAO)=2.8s?1; Km(SMO)=19μM, kcat(SMO)=0.8s?1, respectively). Surprisingly, E t S P D ( Km(APAO)=37μM, kcat(APAO)=0.1s?1; Km(SMO)=48μM, kcat(SMO)=0.05s?1) and BnSPD (Km(APAO)=2.5μM, kcat(APAO)=3.5s?1; Km(SMO)=60μM, kcat(SMO)=0.54s?1) were metabolized to SPD by both the oxidases. Furthermore, we studied the degradation of DESPM, BnEtSPM or DBSPM in the DU145 prostate carcinoma cell line. The same major metabolites EtSPD and/or BnSPD were detected both in the culture medium and intracellularly after 48 hours of culture. Moreover, EtSPM and BnSPM were detected from cell samples. Present data shows that inducible SMO parallel with APAO could play an important role in polyamine based drug action, i.e. degradation of parent drug and its metabolites, having significant impact on efficiency of these drugs, and hence for the development of novel N-alkylated polyamine analogues.
Polyamines, N-alkylated polyamine analogues, Flavin-dependent amino-oxidoreductases, Spermine oxidase, Polyamine oxidase
METABOLISM OF N-ALKYLATED SPERMINE ANALOGUES BY POLYAMINE AND SPERMINE OXIDASES
Merja R. Hakkinen,1 Mervi T. Hyvonen,2 Seppo Auriola,3 Robert A. Casero, Jr,4 Jouko Vepsalainen,1 Alex R. Khomutov,5 Leena Alhonen,2 and Tuomo A. Keinanen2
2010 Nov 29.