The Enzyme Database

Your query returned 1 entry.    printer_iconPrintable version

EC 5.3.1.4     
Accepted name: L-arabinose isomerase
Reaction: β-L-arabinopyranose = L-ribulose
For diagram of L-Arabinose catabolism, click here
Other name(s): L-arabinose ketol-isomerase; araA (gene name)
Systematic name: β-L-arabinopyranose aldose-ketose-isomerase
Comments: Requires a divalent metal ion (the enzyme from the bacterium Escherichia coli prefers Mn2+) [2]. The enzyme binds β-L-arabinopyranose [4] and catalyses ring opening to generate a form of open-chain conformation that facilitates the isomerization reaction, which proceeds via an ene-diol mechanism [6]. The enzyme can also convert α-D-galactose to D-tagatose with lower efficiency [5].
Links to other databases: BRENDA, EXPASY, Gene, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9023-80-7
References:
1.  Heath, E.C., Horecker, B.L., Smyrniotis, P.Z. and Takagi, Y. Pentose formation by Lactobacillus plantarum. II. L-Arabinose isomerase. J. Biol. Chem. 231 (1958) 1031–1037. [PMID: 13539034]
2.  Patrick, J.W. and Lee, N. Purification and properties of an L-arabinose isomerase from Escherichia coli. J. Biol. Chem. 243 (1968) 4312–4318. [PMID: 4878429]
3.  Nakamatu, T. and Yamanaka, K. Crystallization and properties of L-arabinose isomerase from Lactobacillus gayonii. Biochim. Biophys. Acta 178 (1969) 156–165. [DOI] [PMID: 5773448]
4.  Schray, K.J. and Rose, I.A. Anomeric specificity and mechanism of two pentose isomerases. Biochemistry 10 (1971) 1058–1062. [DOI] [PMID: 5550812]
5.  Cheetham, P.S.J. and Wootton, A.N. Bioconversion of D-galactose into D-tagatose. Enzyme and Microbial Technology 15 (1993) 105–108.
6.  Banerjee, S., Anderson, F. and Farber, G.K. The evolution of sugar isomerases. Protein Eng. 8 (1995) 1189–1195. [DOI] [PMID: 8869631]
7.  Manjasetty, B.A. and Chance, M.R. Crystal structure of Escherichia coli L-arabinose isomerase (ECAI), the putative target of biological tagatose production. J. Mol. Biol. 360 (2006) 297–309. [DOI] [PMID: 16756997]
[EC 5.3.1.4 created 1961, modified 2022]
 
 


Data © 2001–2024 IUBMB
Web site © 2005–2024 Andrew McDonald