N-acylglucosamine 2-epimerase (AGE, EC:5.3.1.8) reversibly converts N-acyl-D-glucosamine to N-acyl-D-mannosamine, the latter ultimately being converted to cytidine 5'- monophospho-N-acetylneuraminic acid, which is used as a precursor for the synthesis of connective tissues, blood cells and cellular macromolecules. AGE is a renin-binding protein (RnBP), which might act as a cellular rennin inhibitor. AGE functions as a homodimer, where monomer has an alpha(6)/alpha(6)-barrel structure commonly found in glucoamylases and cellulases [1]. This family contains a number of eukaryotic and bacterial AGE enzymes.
Itoh T, Mikami B, Maru I, Ohta Y, Hashimoto W, Murata K.
Crystal structure of N-acyl-D-glucosamine 2-epimerase from porcine kidney at 2.0 A resolution.
J. Mol. Biol. 303 733-44 2000
[PubMed: 11061972] http://dx.doi.org/10.1006/jmbi.2000.4188
Lee YC, Wu HM, Chang YN, Wang WC, Hsu WH.
The central cavity from the (alpha/alpha)6 barrel structure of Anabaena sp. CH1 N-acetyl-D-glucosamine 2-epimerase contains two key histidine residues for reversible conversion.
J. Mol. Biol. 367 2007 895-908
[PubMed: 17292397] http://dx.doi.org/10.1016/j.jmb.2006.11.001
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