Reaction participants Show >> << Hide
- Name help_outline 2-dehydro-3-deoxy-6-phospho-D-galactonate Identifier CHEBI:58298 Charge -3 Formula C6H8O9P InChIKeyhelp_outline OVPRPPOVAXRCED-NQXXGFSBSA-K SMILEShelp_outline O[C@H](COP([O-])([O-])=O)[C@H](O)CC(=O)C([O-])=O 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 D-glyceraldehyde 3-phosphate Identifier CHEBI:59776 (Beilstein: 6139851) help_outline Charge -2 Formula C3H5O6P InChIKeyhelp_outline LXJXRIRHZLFYRP-VKHMYHEASA-L SMILEShelp_outline [H]C(=O)[C@H](O)COP([O-])([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 33 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline pyruvate Identifier CHEBI:15361 (Beilstein: 3587721; CAS: 57-60-3) help_outline Charge -1 Formula C3H3O3 InChIKeyhelp_outline LCTONWCANYUPML-UHFFFAOYSA-M SMILEShelp_outline CC(=O)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 215 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:24464 | RHEA:24465 | RHEA:24466 | RHEA:24467 | |
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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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Characterization and crystal structure of Escherichia coli KDPGal aldolase.
Walters M.J., Srikannathasan V., McEwan A.R., Naismith J.H., Fierke C.A., Toone E.J.
2-Keto-3-deoxy-6-phosphogluconate (KDPG) and 2-keto-3-deoxy-6-phosphogalactonate (KDPGal) aldolases catalyze an identical reaction differing in substrate specificity in only the configuration of a single stereocenter. However, the proteins show little sequence homology at the amino acid level. Her ... >> More
2-Keto-3-deoxy-6-phosphogluconate (KDPG) and 2-keto-3-deoxy-6-phosphogalactonate (KDPGal) aldolases catalyze an identical reaction differing in substrate specificity in only the configuration of a single stereocenter. However, the proteins show little sequence homology at the amino acid level. Here we investigate the determinants of substrate selectivity of these enzymes. The Escherichia coli KDPGal aldolase gene, cloned into a T7 expression vector and overexpressed in E. coli, catalyzes retro-aldol cleavage of the natural substrate, KDPGal, with values of k(cat)/K(M) and k(cat) of 1.9x10(4)M(-1)s(-1) and 4s(-1), respectively. In the synthetic direction, KDPGal aldolase efficiently catalyzes an aldol addition using a limited number of aldehyde substrates, including d-glyceraldehyde-3-phosphate (natural substrate), d-glyceraldehyde, glycolaldehyde, and 2-pyridinecarboxaldehyde. A preparative scale reaction between 2-pyridinecarboxaldehyde and pyruvate catalyzed by KDPGal aldolase produced the aldol adduct of the R stereochemistry in >99.7% ee, a result complementary to that observed using the related KDPG aldolase. The native crystal structure has been solved to a resolution of 2.4A and displays the same (alpha/beta)(8) topology, as KDPG aldolase. We have also determined a 2.1A structure of a Schiff base complex between the enzyme and its substrate. This model predicts that a single amino acid change, T161 in KDPG aldolase to V154 in KDPGal aldolase, plays an important role in determining the stereochemical course of enzyme catalysis and this prediction was borne out by site-directed mutagenesis studies. However, additional changes in the enzyme sequence are required to prepare an enzyme with both high catalytic efficiency and altered stereochemistry. << Less
Bioorg. Med. Chem. 16:710-720(2008) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.