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

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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Abstract

The enzymes N'-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide isomerase (HisA) and phosphoribosylanthranilate isomerase (TrpF) are sugar isomerases that are involved in histidine and tryptophan biosynthesis, respectively. Both enzymes have the (betaalpha)(8)-barrel fold and catalyze Amadori rearrangements of a thermolabile aminoaldose into the corresponding ...

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Item type:Article
Date:2002
Institutions:Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Reinhard Sterner
Identification Number:
ValueType
12356303PubMed ID
Classification:
NotationType
Aldose-Ketose Isomerases/metabolismMESH
Amino Acid SequenceMESH
Binding SitesMESH
Circular DichroismMESH
Conserved SequenceMESH
Crystallography, X-RayMESH
Enzyme StabilityMESH
Escherichia coliMESH
Histidine/biosynthesisMESH
Hot TemperatureMESH
LigandsMESH
Molecular Sequence DataMESH
MutationMESH
Thermotoga maritima/metabolismMESH
Tryptophan/biosynthesisMESH
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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