Active Site

KDPG/KHG aldolase, active site 1 (IPR031337)

Short name: KDPG/KHG_AS_1

Description

4-Hydroxy-2-oxoglutarate aldolase (EC:4.1.3.16) (KHG-aldolase) catalyzes the interconversion of 4-hydroxy-2-oxoglutarate into pyruvate and glyoxylate. Phospho-2-dehydro-3-deoxygluconate aldolase (EC:4.1.2.14) (KDPG-aldolase) catalyzes the interconversion of 6-phospho-2-dehydro-3-deoxy-D-gluconate into pyruvate and glyceraldehyde 3-phosphate. These two enzymes are structurally and functionally related [PMID: 3136164]. They are both homotrimeric proteins of approximately 220 amino-acid residues. They are class I aldolases whose catalytic mechanism involves the formation of a Schiff-base intermediate between the substrate and the epsilon-amino group of a lysine residue. In both enzymes, an arginine is required for catalytic activity.

This site contains the active site arginine.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
PROSITE patterns