Structural highlights
Function
[XYLA_STRRU] Involved in D-xylose catabolism.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The time-of-flight neutron Laue technique has been used to determine the location of hydrogen atoms in the enzyme d-xylose isomerase (XI). The neutron structure of crystalline XI with bound product, d-xylulose, shows, unexpectedly, that O5 of d-xylulose is not protonated but is hydrogen-bonded to doubly protonated His54. Also, Lys289, which is neutral in native XI, is protonated (positively charged), while the catalytic water in native XI has become activated to a hydroxyl anion which is in the proximity of C1 and C2, the molecular site of isomerization of xylose. These findings impact our understanding of the reaction mechanism.
Hydrogen location in stages of an enzyme-catalyzed reaction: time-of-flight neutron structure of D-xylose isomerase with bound D-xylulose.,Kovalevsky AY, Katz AK, Carrell HL, Hanson L, Mustyakimov M, Fisher SZ, Coates L, Schoenborn BP, Bunick GJ, Glusker JP, Langan P Biochemistry. 2008 Jul 22;47(29):7595-7. Epub 2008 Jun 26. PMID:18578508[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Kovalevsky AY, Katz AK, Carrell HL, Hanson L, Mustyakimov M, Fisher SZ, Coates L, Schoenborn BP, Bunick GJ, Glusker JP, Langan P. Hydrogen location in stages of an enzyme-catalyzed reaction: time-of-flight neutron structure of D-xylose isomerase with bound D-xylulose. Biochemistry. 2008 Jul 22;47(29):7595-7. Epub 2008 Jun 26. PMID:18578508 doi:10.1021/bi8005434
