The different pH optima and substrate specificities of extracellular and vacuolar invertases from plants are determined by a single amino-acid substitution

Plant Journal

Volumn 20, Issue 6, 1999, Pages 707-711

  Goetz, Marc ^a   Roitsch, Thomas ^a  

^a UNIVERSITY OF REGENSBURG   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID SUBSTITUTION; BETA FRUCTOFURANOSIDASE; ENZYME SPECIFICITY; ENZYME SUBSTRATE; GENE MUTATION; HETEROLOGOUS PRODUCT; ISOENZYME; PH; PROTEIN EXPRESSION; RAFFINOSE; SACCHAROMYCES CEREVISIAE; TARGETED MUTAGENESIS;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; BASE SEQUENCE; BETA-FRUCTOFURANOSIDASE; CHENOPODIACEAE; CONSERVED SEQUENCE; DNA PRIMERS; EXTRACELLULAR SPACE; GLYCOSIDE HYDROLASES; HYDROGEN-ION CONCENTRATION; ISOENZYMES; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PHYLOGENY; PLANTS; SACCHAROMYCES CEREVISIAE; SEQUENCE HOMOLOGY, AMINO ACID; SUBSTRATE SPECIFICITY; VACUOLES;

EID: 0033399634     PISSN: 09607412     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-313X.1999.00628.x     Document Type: Article

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