To improve security and privacy, we are moving our web pages and services from HTTP to HTTPS.
To give users of web services time to transition to HTTPS, we will support separate HTTP and HTTPS services until the end of 2017.
From January 2018 most HTTP traffic will be automatically redirected to HTTPS. [more...]
View this page in https

ENZYME entry: EC 5.3.1.3

Accepted Name
D-arabinose isomerase.
Alternative Name(s)
Arabinose isomerase.
L-fucose isomerase.
Reaction catalysed
D-arabinose <=> D-ribulose
Cofactor(s)
Mn(2+).
Comment(s)
  • The enzyme binds the closed form of the sugar and catalyzes ring opening to generate a form of open-chain conformation that facilitates the isomerization reaction, which proceeds via an ene- diol mechanism.
  • The enzyme catalyzes the aldose-ketose isomerization of several sugars.
  • Most enzymes also catalyze the reaction of EC 5.3.1.25.
  • The enzyme from the bacterium Falsibacillus pallidus also converts D-altrose to D-psicose.
  • Cf. EC 5.3.1.4.
Cross-references
BRENDA5.3.1.3
EC2PDB5.3.1.3
ExplorEnz5.3.1.3
PRIAM enzyme-specific profiles5.3.1.3
KEGG Ligand Database for Enzyme Nomenclature5.3.1.3
IUBMB Enzyme Nomenclature5.3.1.3
IntEnz5.3.1.3
MEDLINEFind literature relating to 5.3.1.3
MetaCyc5.3.1.3
UniProtKB/Swiss-Prot
P69922, FUCI_ECOLI

View entry in original ENZYME format
View entry in raw text format (no links)

All UniProtKB/Swiss-Prot entries referenced in this entry, with possibility to download in different formats, align etc.
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 5.3.1.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 5.3.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 5.-.-.-