2ch5
From Proteopedia
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{{STRUCTURE_2ch5| PDB=2ch5 | SCENE= }} | {{STRUCTURE_2ch5| PDB=2ch5 | SCENE= }} | ||
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===CRYSTAL STRUCTURE OF HUMAN N-ACETYLGLUCOSAMINE KINASE IN COMPLEX WITH N-ACETYLGLUCOSAMINE=== | ===CRYSTAL STRUCTURE OF HUMAN N-ACETYLGLUCOSAMINE KINASE IN COMPLEX WITH N-ACETYLGLUCOSAMINE=== | ||
+ | {{ABSTRACT_PUBMED_17010375}} | ||
- | + | ==Function== | |
- | + | [[http://www.uniprot.org/uniprot/NAGK_HUMAN NAGK_HUMAN]] Converts endogenous N-acetylglucosamine (GlcNAc), a major component of complex carbohydrates, from lysosomal degradation or nutritional sources into GlcNAc 6-phosphate. Involved in the N-glycolylneuraminic acid (Neu5Gc) degradation pathway: although human is not able to catalyze formation of Neu5Gc due to the inactive CMAHP enzyme, Neu5Gc is present in food and must be degraded. Also has ManNAc kinase activity.<ref>PMID:22692205</ref> | |
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==About this Structure== | ==About this Structure== | ||
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==Reference== | ==Reference== | ||
- | <ref group="xtra">PMID:017010375</ref><references group="xtra"/> | + | <ref group="xtra">PMID:017010375</ref><references group="xtra"/><references/> |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: N-acetylglucosamine kinase]] | [[Category: N-acetylglucosamine kinase]] |
Revision as of 08:52, 23 April 2014
Contents |
CRYSTAL STRUCTURE OF HUMAN N-ACETYLGLUCOSAMINE KINASE IN COMPLEX WITH N-ACETYLGLUCOSAMINE
Template:ABSTRACT PUBMED 17010375
Function
[NAGK_HUMAN] Converts endogenous N-acetylglucosamine (GlcNAc), a major component of complex carbohydrates, from lysosomal degradation or nutritional sources into GlcNAc 6-phosphate. Involved in the N-glycolylneuraminic acid (Neu5Gc) degradation pathway: although human is not able to catalyze formation of Neu5Gc due to the inactive CMAHP enzyme, Neu5Gc is present in food and must be degraded. Also has ManNAc kinase activity.[1]
About this Structure
2ch5 is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
- Weihofen WA, Berger M, Chen H, Saenger W, Hinderlich S. Structures of human N-Acetylglucosamine kinase in two complexes with N-Acetylglucosamine and with ADP/glucose: insights into substrate specificity and regulation. J Mol Biol. 2006 Dec 1;364(3):388-99. Epub 2006 Sep 3. PMID:17010375 doi:10.1016/j.jmb.2006.08.085
- ↑ Bergfeld AK, Pearce OM, Diaz SL, Pham T, Varki A. Metabolism of vertebrate amino sugars with N-glycolyl groups: elucidating the intracellular fate of the non-human sialic acid N-glycolylneuraminic acid. J Biol Chem. 2012 Aug 17;287(34):28865-81. doi: 10.1074/jbc.M112.363549. Epub, 2012 Jun 12. PMID:22692205 doi:http://dx.doi.org/10.1074/jbc.M112.363549
Categories: Homo sapiens | N-acetylglucosamine kinase | Berger, M. | Chen, H. | Hinderlich, S. | Saenger, W. | Weihofen, W A. | Closed conformation | Domain rotation | Glcnac | Hypothetical protein | N-acetylglucosamine | Open conformation | Ribonuclease h fold | Sugar kinase | Sugar kinase/hsp70/actin superfamily | Transferase