Structural and mutagenesis studies of leishmania triosephosphate isomerase: A point mutation can convert a mesophilic enzyme into a superstable enzyme without losing catalytic power

Protein Engineering

Volumn 12, Issue 3, 1999, Pages 243-250

  Williams, John C ^a,f   Zeelen, Johan P ^a,g   Neubauer, Gitte ^a   Vriend, Gert ^a   Backmann, Jan ^b   Michels, Paul A M ^c   Lambeir, Anne Marie ^d   Wierenga, Rik K ^e  

^a EUROPEAN MOLECULAR BIOLOGY LABORATORY   (Germany)

^b VRIJE UNIVERSITEIT BRUSSEL   (Belgium)

^c DE DUVE INSTITUTE   (Belgium)

^d UNIVERSITY OF ANTWERP   (Belgium)

^e UNIVERSITY OF OULU   (Finland)

^f Och Spine at New York Presbyterian Hospitals   (United States)

^g MAX PLANCK INSTITUTE OF BIOPHYSICS   (Germany)

Author keywords

Enzymology; Leishmania; Stability; Structure; Triosephosphate isomerase

Indexed keywords

DIMER; GLUTAMINE; LYSINE; OXYGEN; TRIOSEPHOSPHATE ISOMERASE;

ARTICLE; CATALYSIS; ENZYME STABILITY; ENZYME STRUCTURE; HYDROGEN BOND; LEISHMANIA; NONHUMAN; PH; POINT MUTATION; PRIORITY JOURNAL; SEQUENCE HOMOLOGY; TEMPERATURE;

LEISHMANIA MEXICANA; PROTOZOA; TRYPANOSOMA; TRYPANOSOMA BRUCEI;

EID: 0032929094     PISSN: 02692139     EISSN: None     Source Type: Journal    
DOI: 10.1093/protein/12.3.243     Document Type: Article

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