Comparison of protein electrostatic potential along the catalytic triad of serine proteinases

János Angyan, G. Náray-Szabó

Research output: Contribution to journalArticle

29 Citations (Scopus)

Abstract

Intraproteic electrostatic potentials along the catalytic triad in serine proteinases are compared for eight enzymes for which three-dimensional co-ordinates are available. We used our bond-increment method to calculate the potential and we considered all protein atoms, including hydrogens. It was found that counter ions which may be located in the vicinity of charged surface side chains play a decisive role in determining enzymatic action. If ionizable side chains are neutralized the electrostatic potential curve across the catalytic triad is of minimum character in all investigated enzymes. It stabilizes the (-+-) charge distribution which models the Ser--His+-Asp- transition state structure which is formed during the catalytic process. Based on the close similarity of the electrostatic pattern in various enzymes we call attention to the possibility that convergent evolution produced not only the effective catalytic triad but also a minimum-type potential which accelerates the enzymatic reaction.

Original languageEnglish
Pages (from-to)349-356
Number of pages8
JournalJournal of Theoretical Biology
Volume103
Issue number3
DOIs
Publication statusPublished - Aug 7 1983

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Serine Proteases
serine proteinases
Static Electricity
Electrostatics
Enzymes
Proteins
Protein
enzymes
Transition State
Radiation counters
Hydrogen Atom
convergent evolution
proteins
Charge distribution
enzymatic reactions
Increment
hydrogen
Accelerate
Hydrogen
Charge

ASJC Scopus subject areas

  • Agricultural and Biological Sciences(all)

Cite this

Comparison of protein electrostatic potential along the catalytic triad of serine proteinases. / Angyan, János; Náray-Szabó, G.

In: Journal of Theoretical Biology, Vol. 103, No. 3, 07.08.1983, p. 349-356.

Research output: Contribution to journalArticle

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