3453-33-6Relevant articles and documents
Multiple catalytic aldolase antibodies suitable for chemical programming
Goswami, Rajib Kumar,Huang, Zheng-Zheng,Forsyth, Jane S.,Felding-Habermann, Brunhilde,Sinha, Subhash C.
, p. 3821 - 3824 (2009)
Chemical programming of nine murine antibodies with catalytic aldolase activity was examined using compounds, equipped with diketone or pro-vinyl ketone linkers that inhibit integrin adhesion receptor functions. The results showed that most Abs were progr
A modular assembly strategy for improving the substrate specificity of small catalytic peptides
Tanaka, Fujie,Barbas III, Carlos F.
, p. 3510 - 3511 (2002)
In contrast to large proteins, small peptide catalysts typically display limited specificity for small molecule substrates. This is presumably a result of the limited opportunities small peptides have to fold in a manner that provides for the formation of an isolated reaction vessel that effectively binds and sequesters substrates from bulk solvent while at the same time catalyzing their transformation. For the preparation of small peptide catalysts that possess improved substrate specificity, we have developed a modular assembly strategy that involves appending phage display-derived substrate binding-domain modules to catalytically active peptide domains. We demonstrate the potential of this strategy with the construction of a small 35-amino acid residue aldolase peptide with improved substrate specificity. The advantages of this approach are that it reduces the demand on the functionalization of the catalytic site and it is modular, therefore making its adaptation to a variety of specificities rapid. The modular assembly strategy studied here may present advantages over exhaustive searches of large random-sequence peptide libraries for peptides with singular function. Copyright
Origins of catalysis by computationally designed retroaldolase enzymes
Lassila, Jonathan K.,Baker, David,Herschlag, Daniel
, p. 4937 - 4942 (2010)
We have investigated recently reported computationally designed retroaldolase enzymes with the goal of understanding the extent and the origins of their catalytic power. Direct comparison of the designed enzymes to primary amine catalysts in solution revealed a rate acceleration of 105-fold for the most active of the designed retroaldolases. Through pH-rate studies of the designed retroaldolases and evaluation of a Bronsted correlation for a series of amine catalysts, we found that lysine pKa values are shifted by 3-4 units in the enzymes but that the catalytic contributions fromthe shifted pKa values are estimated to be modest, about 10-fold. For the most active of the reported enzymes, we evaluated the catalytic contribution of two other design components: a motif intended to stabilize a bound water molecule and hydrophobic substrate binding interactions. Mutational analysis suggested that the bound water motif does not contribute to the rate acceleration. Comparison of the rate acceleration of the designed substrate relative to a minimal substrate suggested that hydrophobic substrate binding interactions contribute around 103-fold to the enzymatic rate acceleration. Altogether, these results suggest that substrate binding interactions and shifting the pKa of the catalytic lysine can account for much of the enzyme's rate acceleration. Additional observations suggest that these interactions are limited in the specificity of placement of substrate and active site catalytic groups. Thus, future design efforts may benefit from a focus on achieving precision in binding interactions and placement of catalytic groups.
Quantitative Packaging of Active Enzymes into a Protein Cage
Azuma, Yusuke,Zschoche, Reinhard,Tinzl, Matthias,Hilvert, Donald
, p. 1531 - 1534 (2016)
Genetic fusion of cargo proteins to a positively supercharged variant of green fluorescent protein enables their quantitative encapsulation by engineered lumazine synthase capsids possessing a negatively charged lumenal surface. This simple tagging system provides a robust and versatile means of creating hierarchically ordered protein assemblies for use as nanoreactors. The generality of the encapsulation strategy and its effect on enzyme function were investigated with eight structurally and mechanistically distinct catalysts.
Preparation method of 6-methoxy-2-naphthaldehyde
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Paragraph 0016-0035, (2021/11/19)
The invention discloses a preparation method of 6-methoxy-2-naphthaldehyde. The preparation method comprises the following step: carrying out a chemical reaction on 6-methoxy-2-acetonaphthone and a catalyst in an organic solvent, wherein gas is introduced when the reaction is started, a molar ratio of the 6-methoxy-2-acetonaphthone to the catalyst is 1: (0.01-10), a reaction temperature is 20-180 DEG C, and reaction time is 0.1-72 hours. According to the preparation method disclosed by the invention, no harsh reaction conditions such as high temperature and high pressure exist in a process route, the process route is simple, reaction conditions are mild, the raw materials are cheap and easy to obtain, operation is simple and convenient, and the preparation method is suitable for environment-friendly industrial production of the 6-methoxy-2-naphthaldehyde.
Continuous flow synthesis of aryl aldehydes by Pd-catalyzed formylation of phenol-derived aryl fluorosulfonates using syngas
Hanselmann, Paul,Hone, Christopher A.,Hu, Guixian,K?ckinger, Manuel,Kappe, C. Oliver
, p. 22449 - 22453 (2020/07/03)
This communication describes the palladium-catalyzed reductive carbonylation of aryl fluorosulfonates (ArOSO2F) using syngas as an inexpensive and sustainable source of carbon monoxide and hydrogen. The conversion of phenols to aryl fluorosulfonates can be conveniently achieved by employing the inexpensive commodity chemical sulfuryl fluoride (SO2F2) and base. The developed continuous flow formylation protocol requires relatively low loadings for palladium acetate (1.25 mol%) and ligand (2.5 mol%). Good to excellent yields of aryl aldehydes were obtained within 45 min for substrates containing electron withdrawing substituents, and 2 h for substrates containing electron donating substituents. The optimal reaction conditions were identified as 120 °C temperature and 20 bar pressure in dimethyl sulfoxide (DMSO) as solvent. DMSO was crucial in suppressing Pd black formation and enhancing reaction rate and selectivity. This journal is
