The Enzyme Database

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EC 5.3.1.3     
Accepted name: D-arabinose isomerase
Reaction: D-arabinose = D-ribulose
Other name(s): D-arabinose(L-fucose) isomerase; L-fucose isomerase; D-arabinose ketol-isomerase; arabinose isomerase (misleading)
Systematic name: D-arabinose aldose-ketose-isomerase
Comments: Requires a divalent metal ion (the enzyme from the bacterium Escherichia coli prefers Mn2+). The enzyme binds the closed form of the sugar and catalyses ring opening to generate a form of open-chain conformation that facilitates the isomerization reaction, which proceeds via an ene-diol mechanism [3]. The enzyme catalyses the aldose-ketose isomerization of several sugars. Most enzymes also catalyse the reaction of EC 5.3.1.25, L-fucose isomerase [3]. The enzyme from the bacterium Falsibacillus pallidus also converts D-altrose to D-psicose [4]. cf. EC 5.3.1.4, L-arabinose isomerase.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, CAS registry number: 9023-81-8
References:
1.  Cohen, S.S. Studies on D-ribulose and its enzymatic conversion to D-arabinose. J. Biol. Chem. 201 (1953) 71–84. [PMID: 13044776]
2.  Green, M. and Cohen, S.S. Enzymatic conversion of L-fucose to L-fuculose. J. Biol. Chem. 219 (1956) 557–568. [PMID: 13319278]
3.  Seemann, J.E. and Schulz, G.E. Structure and mechanism of L-fucose isomerase from Escherichia coli. J. Mol. Biol. 273 (1997) 256–268. [PMID: 9367760]
4.  Takeda, K., Yoshida, H., Izumori, K. and Kamitori, S. X-ray structures of Bacillus pallidus D-arabinose isomerase and its complex with L-fucitol. Biochim. Biophys. Acta 1804 (2010) 1359–1368. [PMID: 20123133]
[EC 5.3.1.3 created 1961, modified 2013]
 
 


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