Title of article
Mycobacterium tuberculosis Ribose-5-phosphate Isomerase has a Known Fold, but a Novel Active Site
Author/Authors
Annette K. Roos، نويسنده , , C. Evalena Andersson، نويسنده , , Terese Bergfors، نويسنده , , Micael Jacobsson، نويسنده , , Anders Karlén، نويسنده , , Torsten Unge، نويسنده , , T.Alwyn Jones، نويسنده , , Andrzej Joachimiak and Sherry L. Mowbray، نويسنده ,
Issue Information
روزنامه با شماره پیاپی سال 2004
Pages
11
From page
799
To page
809
Abstract
Ribose-5-phosphate isomerases (EC 5.3.1.6) inter-convert ribose-5-phosphate and ribulose-5-phosphate. This reaction allows the synthesis of ribose from other sugars, as well a means for salvage of carbohydrates after nucleotide breakdown. Two unrelated types of enzyme are known to catalyze the isomerization. The most common one, RpiA, is present in almost all organisms. The second type, RpiB, is found in many bacterial species.
Keywords
ribose-5-phosphate isomerase , pentose phosphate pathway , X-ray crystallography , rv2465c
Journal title
Journal of Molecular Biology
Serial Year
2004
Journal title
Journal of Molecular Biology
Record number
1243302
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