Histidine‐containing cyclic dipeptides as catalysts in the hydrolysis of carbonic acid <i>p</i>‐nitrophenyl esters

Imanishi, Yukio; Tanihara, Masao; Sugihara, Toshiharu; Higashimura, Toshinobu

doi:10.1002/bip.1977.360161009

Cited by 22 publications

(8 citation statements)

References 21 publications

(3 reference statements)

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“…The synthesis and purification of these compounds have been described. 1 As carboxylic acid esters carrying a negative charge, 3-acyloxy-4-nitrobenzoic acids (S;, n=2, 10, 12, and 18) were prepared, where n is the number of carbon atoms in the acyloxy group. They were synthesized in a manner similar to that reported by Overberger, et al 4 • 5 3-Acetoxy-4-nitrobenzoic acid (S:Z) was recrystallized from methanol; mp 182°C.…”

Section: Substratesmentioning

confidence: 99%

Catalytic Hydrolysis of Charged Carboxylic Acid Active Esters with Cyclic Dipeptides Carrying Hydrophobic and Nucleophilic Groups

Kawaguchi

Tanihara

Imanishi

1983

Polym J

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KEY WORDSCyclo(o-or L-Leu-L-His) I Charged Carboxylic Acid Ester I Hydrophobic Interaction I Hydrolytic Reaction IThe special arrangement of functional groups and their cooperative interactions constitute an essential part of the molecular mechanism of enzyme reactions. Cyclic peptides carrying functional groups fixed at specific positions along the molecular skeleton are suitable model compounds for enzymes in studying the structure-<:atalytic activity relationship. The specific arrangement of the functional groups in cyclic peptides can be determined by NMR and CD spectroscopy.In our previous studies, two cyclic dipeptides carrying nucleophilic groups, i.e., cyclo(o-Leu-LHis) and cyclo(o-Val-L-His), were found to show specific and effective catalyses for the hydrolyses of hydrophobic active esters, i.e., p-nitrophenyl esters of lauric acid [CH 3 (CH 2 ) 10 C00Ph(N0 2 )] and decanoic acid [CH 3 (CH2)8C00Ph(N02)]. 1 ' 2 Conformational analysis of the cyclic dipeptides mainly by NMR indicated the catalytic effectiveness to be controlled by the substrate binding due to hydrophobic interactions and the stereochemical fit of functional groups in the peptide-substrate complex to enhance the intramolecular nucleophilic attack. 2 · 3In order to design an effective catalyst on the basis of a hydrophobic interaction the hydrophobicities of the catalyst and the substrate should be maximized. However, an increase in the hydrophobicity of the substances simultaneously decreases their solubility in water, resulting in a complexity due to molecular associations. 2 In the present study, active esters with long hydrocarbon chains and positive or negative charges were prepared and subjected to catalytic hydrolysis using hydrophobic cyclic peptides. These substrates were expected to be hydrophobic but still have good solubility in water.

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Section: Substratesmentioning

confidence: 99%

Catalytic Hydrolysis of Charged Carboxylic Acid Active Esters with Cyclic Dipeptides Carrying Hydrophobic and Nucleophilic Groups

Kawaguchi

Tanihara

Imanishi

1983

Polym J

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“…The second-order rate constants, k,,, obtained for the PNPL hydrolysis by the present peptides, are summarized in Table 1 with those for PNPA, which were measured under the same reaction conditions. This substrate has a long methylene chain and is far more hydrophobic than PNPA (11). Table 1 shows that the k , y values were smaller than the k z A values in all cases.…”

Section: Resultsmentioning

confidence: 94%

Hydrolysis of various types of ester substrates with linear, cyclic and polymeric peptides containing His, Ser and Asp residues

Nishi

Nakajima

Morishige

et al. 1986

International Journal of Peptide and Protein Research

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Catalytic activities of linear, cyclic and polymeric peptides having the sequences of ‐Asp‐ßAla‐Gly‐His‐ßAla‐Gly‐(nonapeptide series) and ‐Asp‐eAhx‐Ser‐eAhx‐His‐eAhx‐ (hexapeptide series) in the hydrolysis of various types of ester substrates were compared with one another and with that of poly (‐His‐ßAla‐Gly) (Poly‐3) which has no Ser or Asp residues. Hydrolytic activity of the hexapeptide series, the cyclic form in particular, was larger than that of the nonapeptide series in many cases such as in the hydrolysis of N‐protected amino acid p‐nitrophenyl esters (Z‐Gly‐ONp, Boc‐Ala‐ONp, Z‐ (l and d) ‐Leu‐ONp, Boc‐ (l and) ‐Phe‐ONp) and anionic 3‐nitro‐4‐acetoxybenzoic acid (NABA). The activities of the polymeric peptides were generally smaller than those of the linear or cyclic peptides. None of the peptides showed the remarkable activity to the hydrophobic substrate with long chain, p‐nitrophenyl laurate (PNPL), and they were almost inactive to bulky p‐nitrophenyl trimethylacetate (PNPTMA) and cationic 3‐acetoxy‐N‐trimethylanilinium iodide (ANTI). Enantiomer‐selectivity in the hydrolysis of N‐protected amino acid p‐nitrophenyl esters and solvent isotope effect in the hydrolysis of p‐nitrophenyl acetate (PNPA) are also reported.

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“…Recently, we have shown, mainly from kinetic investigations, that polymerization according to the activated-NCA mechanism is highly ste-reosele~tive.~-~ Since stereoselectivity was observed in the polymerization of Val NCA and Ile NCA, whose growing chains do not readily take the a-helical conformation, the stereoselectivity cannot entirely be ascribed to a chiral secondary structure of a growing chain. 8 We therefore investigated, as a model for the polymerization, the addition reaction t o N-substituted NCA of a-amino acid hydantoins, which have a very similar structure to NCAs. The effects of the chiralities of the terminal unitlo and of the penultimate unitll were investigated separately in the model reactions, and both units were found to affect the enantiomer selectivity.…”

Section: Introductionmentioning

confidence: 99%

Contribution from the chirality of the growing chain to the enantiomer selectivity in activated‐NCA polymerization of α‐amino acid N‐carboxyanhydride

Hashimoto

Imanishi

1981

Biopolymers

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SynopsisAs a model compound for the growing chain in the activated-NCA type of polymerization of a-amino acid N-carboxyanhydride (NCA), 3-[w-acetylglycyl-poly(cu-amino acid) acylla-amino acid NCA (called the prepolymer) having various degrees of polymerization (DPs) was synthesized by the polymerization of Phe, Val, Glu(OEt), and Asp(0Bzl) NCA in the presence of AcGly NCA by the tertiary amine. Activated (S)-Phe, Val, Glu(OEt), and Asp(0Bzl) NCA were added to the terminal cyclic group of the corresponding (S)-or (R)-prepolymer, and the enantiomer selectivity in the reaction was investigated. With prepolymers having DPs ranging from 1 to 15, the addition reaction always took place preferentially between species having the same configuration, and the degree of the enantiomer selection increased with increasing D P of the prepolymer. With prepolymers having D P = 1 and 2, we found contributions from the chiral terminal unit and the chiral penultimate unit to the enantiomer selection, respectively. Prepolymer having D P = 5 was shown to take a &type conformation, which led to higher enantiomer selection; and prepolymers having DP = 10 and 15 were shown to take an a-helix conformation, which led to much higher enantiomer selection than did the P-type conformation. In the present investigation the mechanisms of terminal-unit control, penultimate-unit control, and conformational control of the enantiomer selection in the activated-NCA type of polymerization were clearly observed.

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Histidine‐containing cyclic dipeptides as catalysts in the hydrolysis of carbonic acid p‐nitrophenyl esters

Cited by 22 publications

References 21 publications

Catalytic Hydrolysis of Charged Carboxylic Acid Active Esters with Cyclic Dipeptides Carrying Hydrophobic and Nucleophilic Groups

Catalytic Hydrolysis of Charged Carboxylic Acid Active Esters with Cyclic Dipeptides Carrying Hydrophobic and Nucleophilic Groups

Hydrolysis of various types of ester substrates with linear, cyclic and polymeric peptides containing His, Ser and Asp residues

Contribution from the chirality of the growing chain to the enantiomer selectivity in activated‐NCA polymerization of α‐amino acid N‐carboxyanhydride

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