EC 5.3.1.3 - D-arabinose isomerase

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IntEnz Enzyme Nomenclature
EC 5.3.1.3

Names

Accepted name:
D-arabinose isomerase
Other names:
arabinose isomerase [ambiguous]
D-arabinose ketol-isomerase
D-arabinose(L-fucose) isomerase
L-fucose isomerase
Systematic name:
D-arabinose aldose-ketose-isomerase

Reaction

Cofactor

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

Enzymes and pathways: NC-IUBMB , BRENDA , ERGO , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , NIST 74 , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0008790
CAS Registry Number: 9023-81-8
UniProtKB/Swiss-Prot:

References

  1. Cohen, S.S.
    Studies on D-ribulose and its enzymatic conversion to D-arabinose.
    J. Biol. Chem. 201: 71-84 (1953). [PMID: 13044776]
  2. Green, M. and Cohen, S.S.
    Enzymatic conversion of L-fucose to L-fuculose.
    J. Biol. Chem. 219: 557-568 (1956). [PMID: 13319278]
  3. Seemann, J. E., Schulz, G. E.
    Structure and mechanism of L-fucose isomerase from Escherichia coli.
    J. Mol. Biol. 273: 256-268 (1997). [PMID: 9367760]
  4. Takeda, K., Yoshida, H., Izumori, K., Kamitori, S.
    X-ray structures of Bacillus pallidus d-arabinose isomerase and its complex with l-fucitol.
    Biochim. Biophys. Acta 1804: 1359-1368 (2010). [PMID: 20123133]

[EC 5.3.1.3 created 1961, modified 2013]