EurekaMag
+ Most Popular
Cunninghamia lanceolata plantations in China
Mammalian lairs in paleo ecological studies and palynology
Studies on technological possibilities in utilization of anhydrous milk fat for production of recombined butter-like products
Should right-sided fibroelastomas be operated upon?
Large esophageal lipoma
Apoptosis in the mammalian thymus during normal histogenesis and under various in vitro and in vivo experimental conditions
Poissons characoides nouveaux ou non signales de l'Ilha do Bananal, Bresil
Desensitizing efficacy of Colgate Sensitive Maximum Strength and Fresh Mint Sensodyne dentifrices
Administration of fluid by subcutaneous infusion: revival of a forgotten method
Tundra mosquito control - an impossible dream?
Schizophrenia for primary care providers: how to contribute to the care of a vulnerable patient population
Geochemical pattern analysis; method of describing the Southeastern limestone regional aquifer system
Incidence of low birth weights in a hospital of Mexico City
Tabanidae
Graded management intensity of grassland systems for enhancing floristic diversity
Microbiology and biochemistry of cheese and fermented milk
The ember tetra: a new pygmy characid tetra from the Rio das Mortes, Brazil, Hyphessobrycon amandae sp. n. (Pisces, Characoidei)
Risk factors of contrast-induced nephropathy in patients after coronary artery intervention
Renovation of onsite domestic wastewater in a poorly drained soil
Observations of the propagation velocity and formation mechanism of burst fractures caused by gunshot
Systolic blood pressure in a population of infants in the first year of life: the Brompton study
Haematological studies in rats fed with metanil yellow
Studies on pasteurellosis. I. A new species of Pasteurella encountered in chronic fowl cholera
Dormancy breaking and germination of Acacia salicina Lindl. seeds
therapy of lupus nephritis. a two-year prospective study

Conformational aspects of beta-trypsin interaction with substrates and pancreatic trypsin inhibitor. I. Conformational properties of residues in the enzyme-active center and the structure of a non-valent enzyme-substrate complex


Conformational aspects of beta-trypsin interaction with substrates and pancreatic trypsin inhibitor. I. Conformational properties of residues in the enzyme-active center and the structure of a non-valent enzyme-substrate complex



Molekuliarnaia Biologiia 20(1): 102-119



ISSN/ISBN: 0026-8984

PMID: 3951435

The theoretical conformational analysis of potential surfaces of Ser-195, His-57, Asp-102 and Gln-192 side chains in the active center of native beta-trypsin has been carried out. The above residues are shown to exist in low-energy conformational states in the free enzyme and in its nonbonded substrate complexes. Interrelations between the flexibility of the residues and their catalytical functions were revealed. Conformational aspects of interaction of trypsin with N-acetyl-L-lysine and N-acetyl-L-alanyl--L-alanyl--L-lysyl--L-alanyl methyl amide and with the Gly-12--Ile-19 BPTI fragment were analysed. The productive binding of the substrate at the nonbonded complex stage is shown to take place exclusively in the lowest energy conformation of the enzyme-substrate complex. Basing on theoretical and experimental evidence, the problems of primary and secondary specificity of trypsin, and potential properties of the native protein to form a productive nonbonded complex and to react at the subsequent stages of the catalytical act are discussed. Conformational changes in the active center and interactions with a substrate are shown to result from stabilizing enzyme-substrate interactions. Trypsin inhibition by BPTI molecule does not take place at the nonbonded complex stage.

Please choose payment method:






(PDF emailed within 1 workday: $29.90)

Accession: 039660205

Download citation: RISBibTeXText

Related references

Conformational aspects of interactions of beta trypsin with substrates and pancreatic trypsin inhibitor i. conformational properties of residues in enzyme active center and structure of nonbonded enzyme substrate complex. Molekulyarnaya Biologiya (Moscow) 20(1): 102-119, 1986

Conformational aspects of interactions of beta trypsin with substrates and pancreatic trypsin inhibitor ii. structures of tetrahedral adducts and of acyl enzyme. Molekulyarnaya Biologiya (Moscow) 20(2): 346-356, 1986

Conformational aspects of beta-trypsin interaction with substrates and pancreatic trypsin inhibitor. III. Catalytic act of trypsin and its inhibition. Molekuliarnaia Biologiia 20(2): 357-368, 1986

Conformational aspects of interactions of beta trypsin with substrates and pancreatic trypsin in inhibitor iii. the catalytic act of trypsin and its bovine pancreatic trypsin inhibitor inhibition. Molekulyarnaya Biologiya (Moscow) 20(2): 357-368, 1986

Conformational aspects of beta-trypsin interactions with substrates and pancreatic trypsin inhibitor. II. Structure of tetrahedral adducts and acylenzyme. Molekuliarnaia Biologiia 20(2): 346-356, 1986

Study of trypsin-substrate and trypsin-inhibitor complexes. 1. Conformation of Asp-102, His-57 and Ser-195 residues in the trypsin active center. Molekuliarnaia Biologiia 18(5): 1432-1435, 1984

Refined 2.5 angstrom x ray crystal structure of the complex formed by porcine kallikrein a and the bovine pancreatic trypsin inhibitor crystallization patterson search structure determination refinement structure and comparison with its components and with the bovine trypsin pancreatic trypsin inhibitor complex. Journal of Molecular Biology 164(2): 283-312, 1983

Refined 2.5 A X-ray crystal structure of the complex formed by porcine kallikrein A and the bovine pancreatic trypsin inhibitor. Crystallization, Patterson search, structure determination, refinement, structure and comparison with its components and with the bovine trypsin-pancreatic trypsin inhibitor complex. Journal of Molecular Biology 164(2): 283-311, 1983

Circular dichroism spectroscopy of bovine pancreatic trypsin inhibitor and five altered conformational states. Relationship of conformation and the refolding pathway of the trypsin inhibitor. Biochemistry 20(20): 5744-5754, 1981

Further evidence for an active center in streptokinase-plasminogen complex; interaction with pancreatic trypsin inhibitor. Biochemical and Biophysical Research Communications 51(3): 672-679, 1973

Refined 1.6 A resolution crystal structure of the complex formed between porcine beta-trypsin and MCTI-A, a trypsin inhibitor of the squash family. Detailed comparison with bovine beta-trypsin and its complex. Journal of Molecular Biology 229(4): 1022-1036, 1993

The conformational properties of the basic pancreatic trypsin-inhibitor. European Journal of Biochemistry 23(3): 401-411, 1971

Conformational changes of the chaperone SecB upon binding to a model substrate--bovine pancreatic trypsin inhibitor (BPTI). Biological Chemistry 392(10): 849-858, 2011

Pmr investigation of the conformational properties of the basic pancreatic trypsin inhibitor. S Letters: 114-118, 1973

Conformational adaptability of the active site of beta-galactosidase. Interaction of the enzyme with some substrate analogous effectors. Journal of Biological Chemistry 253(3): 833-837, 1978