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UDP-galactose 4-epimerase (GalE) catalyzes the interconversion of UDP-glucose (UDP-Glc) and UDP-galactose (UDP-Gal), which is a pivotal step in the Leloir pathway for d-galactose metabolism. Although GalE is widely distributed in prokaryotes and eukaryotes, little information is available regarding hyperthermophilic GalE. We overexpressed the TM0509 gene, encoding a putative GalE from Thermotoga maritima (TMGalE), in Escherichia coli and characterized the encoded protein. To further investigate the molecular basis of this enzyme's catalytic function, we determined the crystal structures of TMGalE and TMGalE bound to UDP-Glc at resolutions of 1.9 Å and 2.0 Å, respectively. The enzyme was determined to be a homodimer with a molecular mass of 70 kDa. The enzyme could reversibly catalyze the epimerization of UDP-GalNAc/UDP-GlcNAc as well as UDP-Gal/UDP-Glc at elevated temperatures, with an apparent optimal temperature and pH of 80 °C and 7.0, respectively. Our data showed that TM0509 is a UDP-galactosugar 4-epimerase involved in d-galactose metabolism; consequently, this study provides the first detailed characterization of a hyperthermophilic GalE. Moreover, the promiscuous substrate specificity of TMGalE, which is more similar to human GalE than E. coli GalE, supports the notion that TMGalE might exhibit the earliest form of sugar-epimerizing enzymes in the evolution of galactose metabolism.

Titel:	The structural basis of substrate promiscuity in UDP-hexose 4-epimerase from the hyperthermophilic Eubacterium Thermotoga maritima.
Autor/in / Beteiligte Person:	Shin, SM ; Choi, JM ; di Luccio E ; Lee, YJ ; Lee, SJ ; Lee, SH ; Lee, DW
Link:	Zum Volltext
Zeitschrift:	Archives of biochemistry and biophysics, Jg. 585 (2015-11-01), S. 39
Veröffentlichung:	<2000- > : San Diego, CA : Elsevier ; <i>Original Publication</i>: New York, NY : Academic Press, 2015
Medientyp:	academicJournal
ISSN:	1096-0384 (electronic)
DOI:	10.1016/j.abb.2015.08.025
Schlagwort:	Amino Acid Sequence Bacterial Proteins antagonists & inhibitors Bacterial Proteins genetics Biological Evolution Catalytic Domain Crystallography, X-Ray Escherichia coli genetics Escherichia coli metabolism Gene Expression Hot Temperature Kinetics Models, Molecular Molecular Sequence Data Phylogeny Protein Multimerization Protein Structure, Secondary Recombinant Proteins chemistry Recombinant Proteins genetics Sequence Alignment Substrate Specificity Thermotoga maritima classification Thermotoga maritima enzymology UDPglucose 4-Epimerase antagonists & inhibitors UDPglucose 4-Epimerase genetics Bacterial Proteins chemistry Thermotoga maritima chemistry UDPglucose 4-Epimerase chemistry Uridine Diphosphate Galactose chemistry Uridine Diphosphate Glucose chemistry
Sonstiges:	Nachgewiesen in: MEDLINE Sprachen: English Publication Type: Journal Article; Research Support, Non-U.S. Gov't Language: English [Arch Biochem Biophys] 2015 Nov 01; Vol. 585, pp. 39-51. <i>Date of Electronic Publication: </i>2015 Sep 03. MeSH Terms: Bacterial Proteins / chemistry ; Thermotoga maritima / chemistry ; UDPglucose 4-Epimerase / chemistry ; Uridine Diphosphate Galactose / chemistry ; Uridine Diphosphate Glucose / *chemistry ; Amino Acid Sequence ; Bacterial Proteins / antagonists & inhibitors ; Bacterial Proteins / genetics ; Biological Evolution ; Catalytic Domain ; Crystallography, X-Ray ; Escherichia coli / genetics ; Escherichia coli / metabolism ; Gene Expression ; Hot Temperature ; Kinetics ; Models, Molecular ; Molecular Sequence Data ; Phylogeny ; Protein Multimerization ; Protein Structure, Secondary ; Recombinant Proteins / chemistry ; Recombinant Proteins / genetics ; Sequence Alignment ; Substrate Specificity ; Thermotoga maritima / classification ; Thermotoga maritima / enzymology ; UDPglucose 4-Epimerase / antagonists & inhibitors ; UDPglucose 4-Epimerase / genetics Contributed Indexing: Keywords: Crystal structure; Evolution; Hyperthermophiles; Substrate specificity; UDP-galactose 4-epimerase Substance Nomenclature: 0 (Bacterial Proteins) ; 0 (Recombinant Proteins) ; 2956-16-3 (Uridine Diphosphate Galactose) ; EC 5.1.3.2 (UDPglucose 4-Epimerase) ; V50K1D7P4Y (Uridine Diphosphate Glucose) Entry Date(s): Date Created: 20150908 Date Completed: 20160125 Latest Revision: 20180318 Update Code: 20240513

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The structural basis of substrate promiscuity in UDP-hexose 4-epimerase from the hyperthermophilic Eubacterium Thermotoga maritima.