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
Link To Document :
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