Two (betaalpha)(8)-barrel enzymes of histidine and tryptophan biosynthesis have similar reaction mechanisms and common strategies for protecting their labile substrates.

Article

Henn-Sax, Martina, Thoma, Ralf, Schmidt, Steffen, Hennig, Michael, Kirschner, Kasper and Sterner, Reinhard (2002) Two (betaalpha)(8)-barrel enzymes of histidine and tryptophan biosynthesis have similar reaction mechanisms and common strategies for protecting their labile substrates. Biochemistry 41 (40), pp. 12032-42.

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• Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Reinhard Sterner

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Details

Item type	Article
Journal or Publication Title	Biochemistry
Volume	41
Number of Issue or Book Chapter	40
Page Range	pp. 12032-42
Date	2002
Date of publication	22 Mar 2010 08:32
Institutions	Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Reinhard Sterner
Identification Number	Value Type 12356303 PubMed ID
Classification	Notation Type Aldose-Ketose Isomerases/metabolism MESH Amino Acid Sequence MESH Binding Sites MESH Circular Dichroism MESH Conserved Sequence MESH Crystallography, X-Ray MESH Enzyme Stability MESH Escherichia coli MESH Histidine/biosynthesis MESH Hot Temperature MESH Ligands MESH Molecular Sequence Data MESH Mutation MESH Thermotoga maritima/metabolism MESH Tryptophan/biosynthesis MESH
Dewey Decimal Classification	500 Science > 570 Life sciences
Status	Published
Refereed	Yes, this version has been refereed
Created at the University of Regensburg	Yes
Item ID	13689

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