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 original | English |
|---|---|
| Páginas (desde-hasta) | 4909-4914 |
| Número de páginas | 6 |
| Publicación | Journal of Biological Chemistry |
| Volumen | 248 |
| N.º | 14 |
| Estado | Published - 1973 |
Huella dactilar
ASJC Scopus subject areas
- Biochemistry
- Medicine(all)
- Molecular Biology
- Cell Biology
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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.
UR - http://www.scopus.com/inward/record.url?scp=0015799117&partnerID=8YFLogxK
M3 - Article
VL - 248
SP - 4909
EP - 4914
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
SN - 0021-9258
IS - 14
ER -