The Consequences of Replacing Histidine 356 in Isocitrate Lyase fromEscherichia coli

Isocitrate lyase fromEscherichia colihas been expressed in transformedE. coliJE10 cells lacking the isocitrate lyase (icl) gene. After directed mutagenesis oficlby the restriction-site elimination method, partially purified isocitrate lyase mutants in which His 356 has been converted to Lys, Arg, Gl...

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Veröffentlicht in:Archives of biochemistry and biophysics 1996-12, Vol.336 (2), p.309-315
Hauptverfasser: Rehman, Abdur, Mcfadden, Bruce A.
Format: Artikel
Sprache:eng
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Zusammenfassung:Isocitrate lyase fromEscherichia colihas been expressed in transformedE. coliJE10 cells lacking the isocitrate lyase (icl) gene. After directed mutagenesis oficlby the restriction-site elimination method, partially purified isocitrate lyase mutants in which His 356 has been converted to Lys, Arg, Gln, Asp, or Leu have been characterized after induction of transformed, induced JE10 cells. Values ofkcatcompared to those for wild-type (wt) enzyme (100) at 37°C, pH 7.3, are 18, 1,
ISSN:0003-9861
1096-0384
DOI:10.1006/abbi.1996.0562