L-arabinose isomerase

L-arabinose isomerase
L-arabinose isomerase hexamer, Geobacillus kaustophilus
Identifiers
EC no.	5.3.1.4
CAS no.	9023-80-7
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
Gene Ontology	AmiGO / QuickGO
Search PMC articles PubMed articles NCBI proteins

Arabinose isomerase
crystal structure of l-arabinose isomerase from e.coli
Identifiers
Symbol	Arabinose_Isome
Pfam	PF02610
InterPro	IPR003762
Available protein structures: Pfam   structures / ECOD   PDB RCSB PDB; PDBe; PDBj PDBsum structure summary

In enzymology, a L-arabinose isomerase (EC 5.3.1.4) is an enzyme that catalyzes the chemical reaction

L-arabinose ${\displaystyle \rightleftharpoons }$ L-ribulose

Hence, this enzyme has one substrate, L-arabinose, and one product, L-ribulose.

This enzyme belongs to the family of isomerases, specifically those intramolecular oxidoreductases interconverting aldoses and ketoses. The systematic name of this enzyme class is L-arabinose aldose-ketose-isomerase. This enzyme participates in pentose and glucuronate interconversions.

This enzyme catalyses the conversion of L-arabinose to L-ribulose as the first step in the pathway of L-arabinose utilization as a carbon source.^[1]

Structural studies

As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 2AJT and 2HXG.

References

1. Sa-Nogueira I, Nogueira TV, Soares S, de Lencastre H (March 1997). "The Bacillus subtilis L-arabinose (ara) operon: nucleotide sequence, genetic organization and expression". Microbiology. 143 (3): 957–69. doi:10.1099/00221287-143-3-957. PMID 9084180.

Further reading

• HEATH EC, HORECKER BL, SMYRNIOTIS PZ, TAKAGI Y (1958). "Pentose fermentation by Lactobacillus plantarum. II. L-arabinose isomerase". J. Biol. Chem. 231 (2): 1031–7. doi:10.1016/S0021-9258(18)70464-X. PMID 13539034.
• Nakamatu T, Yamanaka K (1969). "Crystallization and properties of L-arabinose isomerase from Lactobacillus gayonii". Biochim. Biophys. Acta. 178 (1): 156–65. doi:10.1016/0005-2744(69)90142-9. PMID 5773448.

This article incorporates text from the public domain Pfam and InterPro: IPR003762