Preparation and kinetic properties of a new form of chymotrypsin which is active at alkaline pH

α1 chymotrypsin

P. Valenzuela, M. L. Bender

Resultado de la investigación: Article

11 Citas (Scopus)

Resumen

The preparation of a new stable and active form of chymotrypsin is described. The enzyme possesses the threonine 147 instead of alanine 149 as the NH2 terminal group of the C chain and has been called α1 chymotrypsin. The conformational transition that affects chymotrypsins at alkaline pH was investigated and compared with that of α- and δ chymotrypsins by studying the kinetic constants and their pH dependencies for the hydrolysis of various specific ester substrates. The k(cat) values obtained with α1 chymotrypsin are similar to those of α- and δ chymotrypsins. The K(m) values showed a progressive increase toward the alkaline pH region. The shape of the K(m) pH profiles closely resemble those of δ chymotrypsin and differ considerably from the behavior of α chymotrypsin. The results strongly implicate the participation of the alanine 149 amino group in the reversible inactivation of α chymotrypsin at high pH.

Idioma originalEnglish
Páginas (desde-hasta)4909-4914
Número de páginas6
PublicaciónJournal of Biological Chemistry
Volumen248
N.º14
EstadoPublished - 1973

Huella dactilar

Chymotrypsin
Kinetics
Alanine
Threonine
Hydrolysis
Esters
Substrates
Enzymes

ASJC Scopus subject areas

  • Biochemistry
  • Medicine(all)
  • Molecular Biology
  • Cell Biology

Citar esto

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abstract = "The preparation of a new stable and active form of chymotrypsin is described. The enzyme possesses the threonine 147 instead of alanine 149 as the NH2 terminal group of the C chain and has been called α1 chymotrypsin. The conformational transition that affects chymotrypsins at alkaline pH was investigated and compared with that of α- and δ chymotrypsins by studying the kinetic constants and their pH dependencies for the hydrolysis of various specific ester substrates. The k(cat) values obtained with α1 chymotrypsin are similar to those of α- and δ chymotrypsins. The K(m) values showed a progressive increase toward the alkaline pH region. The shape of the K(m) pH profiles closely resemble those of δ chymotrypsin and differ considerably from the behavior of α chymotrypsin. The results strongly implicate the participation of the alanine 149 amino group in the reversible inactivation of α chymotrypsin at high pH.",
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Preparation and kinetic properties of a new form of chymotrypsin which is active at alkaline pH : α1 chymotrypsin. / Valenzuela, P.; Bender, M. L.

En: Journal of Biological Chemistry, Vol. 248, N.º 14, 1973, p. 4909-4914.

Resultado de la investigación: Article

TY - JOUR

T1 - Preparation and kinetic properties of a new form of chymotrypsin which is active at alkaline pH

T2 - α1 chymotrypsin

AU - Valenzuela, P.

AU - Bender, M. L.

PY - 1973

Y1 - 1973

N2 - The preparation of a new stable and active form of chymotrypsin is described. The enzyme possesses the threonine 147 instead of alanine 149 as the NH2 terminal group of the C chain and has been called α1 chymotrypsin. The conformational transition that affects chymotrypsins at alkaline pH was investigated and compared with that of α- and δ chymotrypsins by studying the kinetic constants and their pH dependencies for the hydrolysis of various specific ester substrates. The k(cat) values obtained with α1 chymotrypsin are similar to those of α- and δ chymotrypsins. The K(m) values showed a progressive increase toward the alkaline pH region. The shape of the K(m) pH profiles closely resemble those of δ chymotrypsin and differ considerably from the behavior of α chymotrypsin. The results strongly implicate the participation of the alanine 149 amino group in the reversible inactivation of α chymotrypsin at high pH.

AB - The preparation of a new stable and active form of chymotrypsin is described. The enzyme possesses the threonine 147 instead of alanine 149 as the NH2 terminal group of the C chain and has been called α1 chymotrypsin. The conformational transition that affects chymotrypsins at alkaline pH was investigated and compared with that of α- and δ chymotrypsins by studying the kinetic constants and their pH dependencies for the hydrolysis of various specific ester substrates. The k(cat) values obtained with α1 chymotrypsin are similar to those of α- and δ chymotrypsins. The K(m) values showed a progressive increase toward the alkaline pH region. The shape of the K(m) pH profiles closely resemble those of δ chymotrypsin and differ considerably from the behavior of α chymotrypsin. The results strongly implicate the participation of the alanine 149 amino group in the reversible inactivation of α chymotrypsin at high pH.

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