Proteinase‐Catalyzed Synthesis of Peptide Bonds

Fruton, Joseph S.

doi:10.1002/9780470122983.ch7

Cited by 87 publications

(13 citation statements)

References 259 publications

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“…Our findings are in contrast to Chellapan et al (2011) who reported only ~90.0% activity with diethyl ether (1-10%, v/v) and ~80.0% with acetone (5.0%, v/v) after 30 min of incubation. Application of proteases for the production of certain oligopeptides has received a great attention as a viable alternative to chemical approach (Fruton, 1982;Lee et al, 1993). However, less specificity and instability of the enzyme in the presence of organic solvents are the limiting factors for use of proteases in peptide synthesis as the reaction conducted in non aqueous conditions (Ghorbel et al, 2003).…”

Section: Effect Of Organic Solvents On Stability Of Alkaline Proteasementioning

confidence: 99%

Purification, biochemical characterization and performance evaluation of an alkaline serine protease from Aspergillus flavus MTCC 9952 mutant

Yadav

Bisht²,

Tiwari

et al. 2015

Biocatalysis and Agricultural Biotechnology

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Section: Effect Of Organic Solvents On Stability Of Alkaline Proteasementioning

confidence: 99%

Purification, biochemical characterization and performance evaluation of an alkaline serine protease from Aspergillus flavus MTCC 9952 mutant

Yadav

Bisht²,

Tiwari

et al. 2015

Biocatalysis and Agricultural Biotechnology

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“…The nature and type of organic solvent have a strong effect on protease activity [35]. Application of proteases for production of certain oligopeptides has attracted great attention as a viable alternative to chemical approach [19,41]. However, use of proteases for peptide synthesis is limited by the specificity and instability of the enzyme in the presence of organic solvents, since the reaction occurs in organic media.…”

Section: Effect Of Organic Solvents On Protease Activitymentioning

confidence: 99%

Characterization of an extracellular alkaline serine protease from marine Engyodontium album BTMFS10

Chellappan

Jasmin

Basheer

et al. 2010

J Ind Microbiol Biotechnol

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An alkaline protease from marine Engyodontium album was characterized for its physicochemical properties towards evaluation of its suitability for potential industrial applications. Molecular mass of the enzyme by matrix-assisted laser desorption ionization-mass spectrometry (MALDI-MS) analysis was calculated as 28.6 kDa. Isoelectric focusing yielded pI of 3-4. Enzyme inhibition by phenylmethylsulfonyl fluoride (PMSF) and aprotinin confirmed the serine protease nature of the enzyme. K (m), V (max), and K (cat) of the enzyme were 4.727 x 10⁻² mg/ml, 394.68 U, and 4.2175 x 10⁻² s⁻¹, respectively. Enzyme was noted to be active over a broad range of pH (6-12) and temperature (15-65 °C), with maximum activity at pH 11 and 60 °C. CaCl₂ (1 mM), starch (1%), and sucrose (1%) imparted thermal stability at 65 °C. Hg²⁺, Cu²⁺, Fe³⁺, Zn²⁺, Cd⁺, and Al³⁺ inhibited enzyme activity, while 1 mM Co²⁺ enhanced enzyme activity. Reducing agents enhanced enzyme activity at lower concentrations. The enzyme showed considerable storage stability, and retained its activity in the presence of hydrocarbons, natural oils, surfactants, and most of the organic solvents tested. Results indicate that the marine protease holds potential for use in the detergent industry and for varied applications.

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“…A review of the older literature on cysteine proteinases, published in 1987 [133], includes an account of their primary and secondary specificity characteristics [164] (updated in [20]). The specificity characteristics of papain were studied extensively by Schechter and Berger [165][166][167] using diastereoisomeric peptides of alanine from Ala2 to Ala6.…”

Section: Cysteine Proteinasesmentioning

confidence: 99%

“…They concluded that the papain active center comprises seven subsites, each capable of accommodating a single amino acid residue of substrate. This classic study gave rise to the now widely used P and P 0 notation for oligomeric substrates and the related S and S 0 notation for the assumed complementary enzyme subsites, although the possibility of a continuum of flexibility needs to be kept in mind [164]. The P 1 and P 0 1 residues contribute the carbonyl and amino groups respectively of the scissile P 1 P 0 1 bond.…”

Section: Cysteine Proteinasesmentioning

confidence: 99%

Substrate Recognition

Brocklehurst

Gul

Pickersgill

2009

Amino Acids, Peptides and Proteins in Organic Chemistry

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Specific molecular recognition processes by which molecules recognize and discriminate between closely related partners are involved in essentially all aspects of biological function, ranging in complexity from enzyme-inhibitor and enzymesubstrate systems to phenomena such as gene expression, the immune system, and synaptic transmission, and these are important considerations in drug design [1]. This chapter is concerned with general concepts exemplified by a selection of relatively well-defined enzyme-substrate and, by extension, enzyme-inhibitor systems. The original concept of recognition by complementarity in the enzymesubstrate adsorptive (Michaelis) complex was suggested by Emil Fischer in 1894 using his well-known lock-and-key analogy [2]. It is now generally accepted that this has now been superseded by complementarity in the reaction transition state, based on the ideas reported by J.B.S. Haldane [3] in 1930 and elaborated by Linus Pauling [4] in 1946. The catalytic potential of enzymes derives from stabilization in the transition state relative to any stabilization in the Michaelis complex. The latter is anticatalytic in that the free energy expended in stabilizing the adsorptive complex offsets the transition-state stabilization energy (e.g., [5]).Valuable chapters and books on enzyme catalysis and inhibition are available (e.g., [5][6][7][8][9][10][11]) and detailed mechanistic studies on many individual enzymes are described in Sinnot [12]. Macromolecular catalysis includes also catalysis by catalytic antibodies [13] and by synthetic polymers [14], including molecularly imprinted polymers [15]. The contributions of selections of various types of chemical catalysis such as acid-base, nucleophilic, and electrophilic catalysis [5,6,8] are almost always insufficient to account for the high catalytic efficiency of enzymes. A particularly important additional contribution is the entropic advantage that derives from the fact that enzyme catalysis occurs within an enzyme-substrate complex. The complex is essentially a single molecular species and the catalytic act involves one or more unimolecular steps during which there is no loss of translational or rotational entropy

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Proteinase‐Catalyzed Synthesis of Peptide Bonds

Cited by 87 publications

References 259 publications

Purification, biochemical characterization and performance evaluation of an alkaline serine protease from Aspergillus flavus MTCC 9952 mutant

Purification, biochemical characterization and performance evaluation of an alkaline serine protease from Aspergillus flavus MTCC 9952 mutant

Characterization of an extracellular alkaline serine protease from marine Engyodontium album BTMFS10

Substrate Recognition

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