Enzymes
| UniProtKB help_outline | 6,683 proteins |
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- Name help_outline β-L-arabinopyranose Identifier CHEBI:40886 (Beilstein: 1722190; CAS: 5328-37-0) help_outline Charge 0 Formula C5H10O5 InChIKeyhelp_outline SRBFZHDQGSBBOR-KLVWXMOXSA-N SMILEShelp_outline O[C@H]1CO[C@H](O)[C@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 2 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline L-ribulose Identifier CHEBI:16880 (CAS: 2042-27-5) help_outline Charge 0 Formula C5H10O5 InChIKeyhelp_outline ZAQJHHRNXZUBTE-UCORVYFPSA-N SMILEShelp_outline C(O)C(=O)[C@@H](O)[C@@H](O)CO 2D coordinates Mol file for the small molecule Search links Involved in 4 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:14821 | RHEA:14822 | RHEA:14823 | RHEA:14824 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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Anomeric specificity and mechanism of two pentose isomerases.
Schray K.J., Rose I.A.
Biochemistry 10:1058-1062(1971) [PubMed] [EuropePMC]
This publication is cited by 2 other entries.
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Crystal structure of Escherichia coli L-arabinose isomerase (ECAI), the putative target of biological tagatose production.
Manjasetty B.A., Chance M.R.
Escherichia coli L-arabinose isomerase (ECAI; EC 5.3.1.4) catalyzes the isomerization of L-arabinose to L-ribulose in vivo. This enzyme is also of commercial interest as it catalyzes the conversion of D-galactose to D-tagatose in vitro. The crystal structure of ECAI was solved and refined at 2.6 A ... >> More
Escherichia coli L-arabinose isomerase (ECAI; EC 5.3.1.4) catalyzes the isomerization of L-arabinose to L-ribulose in vivo. This enzyme is also of commercial interest as it catalyzes the conversion of D-galactose to D-tagatose in vitro. The crystal structure of ECAI was solved and refined at 2.6 A resolution. The subunit structure of ECAI is organised into three domains: an N-terminal, a central and a C-terminal domain. It forms a crystallographic trimeric architecture in the asymmetric unit. Packing within the crystal suggests the idea that ECAI can form a hexameric assembly. Previous electron microscopic and biochemical studies supports that ECAI is hexameric in solution. A comparison with other known structures reveals that ECAI adopts a protein fold most similar to E. coli fucose isomerase (ECFI) despite very low sequence identity 9.7%. The structural similarity between ECAI and ECFI with regard to number of domains, overall fold, biological assembly, and active site architecture strongly suggests that the enzymes have functional similarities. Further, the crystal structure of ECAI forms a basis for identifying molecular determinants responsible for isomerization of arabinose to ribulose in vivo and galactose to tagatose in vitro. << Less