KEGG   ENZYME: 5.3.1.3Help
Entry
EC 5.3.1.3                  Enzyme                                 

Name
D-arabinose isomerase;
D-arabinose(L-fucose) isomerase;
L-fucose isomerase;
D-arabinose ketol-isomerase;
arabinose isomerase (misleading)
Class
Isomerases;
Intramolecular oxidoreductases;
Interconverting aldoses and ketoses, and related compounds
BRITE hierarchy
Sysname
D-arabinose aldose-ketose-isomerase
Reaction(IUBMB)
D-arabinose = D-ribulose [RN:R01577]
Reaction(KEGG)
R01577;
(other) R03163
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Substrate
D-arabinose [CPD:C00216]
Product
D-ribulose [CPD:C00309]
Comment
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.
History
EC 5.3.1.3 created 1961, modified 2013
Reference
1  [PMID:13044776]
  Authors
COHEN S.
  Title
Studies on D-ribulose and its enzymatic conversion to D-arabinose.
  Journal
J. Biol. Chem. 201 (1953) 71-84.
  Organism
Escherichia coli
Reference
2  [PMID:13319278]
  Authors
GREEN M, COHEN SS.
  Title
Enzymatic conversion of L-fucose to L-fuculose.
  Journal
J. Biol. Chem. 219 (1956) 557-68.
  Organism
Escherichia coli
  Sequence
[up:P69922]
Reference
3  [PMID:9367760]
  Authors
Seemann JE, Schulz GE
  Title
Structure and mechanism of L-fucose isomerase from Escherichia coli.
  Journal
J. Mol. Biol. 273 (1997) 256-68.
  Organism
Escherichia coli
  Sequence
[up:P69922]
Reference
4  [PMID:20123133]
  Authors
Takeda K, Yoshida H, Izumori K, Kamitori S
  Title
X-ray structures of Bacillus pallidus d-arabinose isomerase and its complex with  l-fucitol.
  Journal
Biochim. Biophys. Acta. 1804 (2010) 1359-68.
  Organism
Bacillus pallidus
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
9023-81-8

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