Mutagenesis of endopolygalacturonase from fusarium moniliforme : Histidine residue 234 is critical for enzymatic and macerating activities and not for binding to polygalacturonase-inhibiting protein (PGIP)

Molecular Plant-Microbe Interactions

Volumn 9, Issue 7, 1996, Pages 617-624

  Caprari, C ^a   Mattei, B ^a   Basile, M L ^a   Salvi, G ^a   Crescenzi, V ^a   De Lorenzo, G ^a   Cervone, F ^a  

^a SAPIENZA UNIVERSITY OF ROME   (Italy)

Author keywords

Surface plasmon resonance; Yeast

Indexed keywords

ENZYME INHIBITOR; HISTIDINE; PGIP PROTEIN, PLANT; POLYGALACTURONASE; PRIMER DNA; RECOMBINANT PROTEIN; VEGETABLE PROTEIN;

AMINO ACID SEQUENCE; ARTICLE; BINDING SITE; CHEMISTRY; ENZYMOLOGY; FUSARIUM; LEGUME; MEDICINAL PLANT; METABOLISM; MOLECULAR CLONING; NUCLEOTIDE SEQUENCE; SACCHAROMYCES CEREVISIAE; SITE DIRECTED MUTAGENESIS;

AMINO ACID SEQUENCE; BASE SEQUENCE; BINDING SITES; CLONING, MOLECULAR; CONSERVED SEQUENCE; DNA PRIMERS; ENZYME INHIBITORS; FABACEAE; FUSARIUM; HISTIDINE; MUTAGENESIS, SITE-DIRECTED; PLANT PROTEINS; PLANTS, MEDICINAL; POLYGALACTURONASE; RECOMBINANT PROTEINS; SACCHAROMYCES CEREVISIAE;

FUSARIUM; GIBBERELLA FUJIKUROI; PHASEOLUS VULGARIS; SACCHAROMYCES CEREVISIAE; SOLANUM TUBEROSUM;

EID: 0030237034     PISSN: 08940282     EISSN: None     Source Type: Journal    
DOI: 10.1094/MPMI-9-0617     Document Type: Article

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