1urt
From Proteopedia
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MURINE CARBONIC ANHYDRASE V
Overview
Carbonic anhydrase V (CA V) is a mitochondrial enzyme that catalyzes the, hydration of CO2 to produce bicarbonate and a proton. The catalytic, properties of wild-type murine CA V suggest the presence of a proton, shuttle residue having pKa = 9.2, the role of which is to transfer a, proton from zinc-bound water to solution in the hydration direction to, regenerate the zinc hydroxide form of the enzyme. Two likely candidates, for shuttle residues are the tyrosines at positions 64 and 131 in the, active site cavity. The crystal structure of wild-type carbonic anhydrase, V [Boriack-Sjodin et al. (1995) Proc. Natl. Acad. Sci. U.S.A. 92, 10949-10953] shows that the side chain of Tyr 64 is forced into an, orientation pointing away from the zinc by Phe 65, although Tyr 131 is, oriented toward the ... [(full description)]
About this Structure
1URT is a [Single protein] structure of sequence from [Mus musculus] with ZN as [ligand]. Active as [[1]], with EC number [4.2.1.1]. Full crystallographic information is available from [OCA].
Reference
Structure-based design of an intramolecular proton transfer site in murine carbonic anhydrase V., Heck RW, Boriack-Sjodin PA, Qian M, Tu C, Christianson DW, Laipis PJ, Silverman DN, Biochemistry. 1996 Sep 10;35(36):11605-11. PMID:8794740
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