EzCatDB: S00845
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DB codeS00845
CATH domainDomain 11.50.10.10 : GlycosyltransferaseCatalytic domain
E.C.5.1.3.8

CATH domainRelated DB codes (homologues)
1.50.10.10 : GlycosyltransferaseS00531,S00048,D00167,D00500,M00192,T00245,T00246

Enzyme Name
UniProtKBKEGG

A4UA16P17560
Protein name
N-acylglucosamine 2-epimeraseN-Acylglucosamine 2-epimerase
Acylglucosamine 2-epimerase
N-Acetylglucosamine 2-epimerase
SynonymsN-acetyl-D-glucosamine 2-epimerase
EC 5.1.3.8
N-acetyl-D-glucosamine 2-epimerase
GlcNAc 2-epimerase
AGE
Renin-binding protein
RnBP
RefSeq
NP_999065.1 (Protein)
NM_213900.1 (DNA/RNA sequence)
PfamPF07221 (GlcNAc_2-epim)
[Graphical view]
PF07221 (GlcNAc_2-epim)
[Graphical view]

KEGG pathways
MAP codePathways
MAP00530Aminosugars metabolism

UniProtKB:Accession NumberA4UA16P17560
Entry nameA4UA16_9NOSTRENBP_PIG
Activity
N-acyl-D-glucosamine = N-acyl-D-mannosamine.
Subunit
Homodimer.
Subcellular location

Cofactor


Compound table: links to PDB-related databases & PoSSuM

CofactorsSubstratesProducts
KEGG-idC00002C03000C00625
CompoundATPN-acyl-D-glucosamineN-acyl-D-mannosamine
Typeamine group,nucleotideamide group,carbohydrateamide group,carbohydrate
ChEBI15422


PubChem5957


           
2gz6A00UnboundUnboundUnbound
2gz6B00UnboundUnboundUnbound
1fp3A00UnboundUnboundUnbound
1fp3B00UnboundUnboundUnbound

Active-site residues
resource
literature [6]&[7]
pdbCatalytic residues
         
2gz6A00ARG 57;HIS 239;GLU 242;GLU 308;HIS 372
2gz6B00ARG 57;HIS 239;GLU 242;GLU 308;HIS 372
1fp3A00ARG 60;HIS 248;GLU 251;GLU 318;HIS 382
1fp3B00ARG 60;HIS 248;GLU 251;GLU 318;HIS 382

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[6]Figure 5, p.904-905
[7]Figure 6, p.1453-1455

references
[1]
CommentsX-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
PubMed ID11061972
JournalJ Mol Biol
Year2000
Volume303
Pages733-44
AuthorsItoh T, Mikami B, Maru I, Ohta Y, Hashimoto W, Murata K
TitleCrystal structure of N-acyl-D-glucosamine 2-epimerase from porcine kidney at 2.0 A resolution.
Related PDB1fp3
Related UniProtKBP17560
[2]
PubMed ID11706991
JournalCell Mol Life Sci
Year2001
Volume58
Pages1650-65
AuthorsAllard ST, Giraud MF, Naismith JH
TitleEpimerases: structure, function and mechanism.
[3]
PubMed ID11726282
JournalJ Biochem
Year2001
Volume130
Pages815-21
AuthorsTakahashi S, Hori K, Takahashi K, Ogasawara H, Tomatsu M, Saito K
TitleEffects of nucleotides on N-acetyl-d-glucosamine 2-epimerases (renin-binding proteins): comparative biochemical studies.
[4]
PubMed ID12137277
JournalNat Prod Rep
Year2002
Volume19
Pages261-77
AuthorsSamuel J, Tanner ME
TitleMechanistic aspects of enzymatic carbohydrate epimerization.
[5]
PubMed ID16011304
JournalBiomed Res
Year2005
Volume26
Pages117-21
AuthorsTakahashi S, Ogasawara H, Hiwatashi K, Hata K, Hori K, Koizumi Y, Sugiyama T
TitleAmino acid residues conferring the nucleotide binding properties of N-acetyl-D-glucosamine 2-epimerase (renin binding protein).
[6]
CommentsNUCLEOTIDE SEQUENCE.
PubMed ID17292397
JournalJ Mol Biol
Year2007
Volume367
Pages895-908
AuthorsLee YC, Wu HM, Chang YN, Wang WC, Hsu WH
TitleThe 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.
Related PDB2gz6
Related UniProtKBA4UA16
[7]
PubMed ID18328504
JournalJ Mol Biol
Year2008
Volume377
Pages1443-59
AuthorsItoh T, Mikami B, Hashimoto W, Murata K
TitleCrystal structure of YihS in complex with D-mannose: structural annotation of Escherichia coli and Salmonella enterica yihS-encoded proteins to an aldose-ketose isomerase.
[8]
PubMed ID19330485
JournalBiotechnol Lett
Year2009
Volume
Pages
AuthorsIto S, Hamada S, Ito H, Matsui H, Ozawa T, Taguchi H, Ito S
TitleSite-directed mutagenesis of possible catalytic residues of cellobiose 2-epimerase from Ruminococcus albus.

comments
Although this enzyme binds ATP at the site, which is composed of Trp56, Arg60 and Phe122 (of PDB;1fp3), its role in catalysis has not been elucidated yet (see [7]).
This enzyme catalyzes the following reactions (see [6] & [7]):
(A) Ring opening; intramolecular elimination:
(B) Isomerization; Shift of double-bond from O=C-C to O-C=C, forming an enediol intermediate:
(C) Isomerization; Shift of double-bond from C=C-O to C-C=O:
(D) Ring closure; intramolecular addition:

createdupdated
2009-06-152010-03-29


Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2012 - March 2013)
Supported by the commission for the Development of Artificial Gene Synthesis Technology for Creating Innovative Biomaterial from the Ministry of Economy, Trade and Industry (METI) (October 2012 - )
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