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{PDOC00144}
{PS00159; ALDOLASE_KDPG_KHG_1}
{PS00160; ALDOLASE_KDPG_KHG_2}
{BEGIN}
*************************************************
* KDPG and KHG aldolases active site signatures *
*************************************************
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 [1]. 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.
We developed two signature patterns for these enzymes. The first one contains
the active site arginine and the second, the lysine involved in the Schiff-
base formation.
-Consensus pattern: G-[LIVM]-x(3)-E-[LIV]-T-[LF]-R
[R is the active site residue]
-Sequences known to belong to this class detected by the pattern: ALL, except
for Bacillus subtilis KDPG-aldolase which has Thr instead of Arg in the
active site.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Consensus pattern: G-x(3)-[LIVMF]-K-[LF]-F-P-[SA]-x(3)-G
[K is involved in Schiff-base formation]
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: November 1997 / Patterns and text revised.
[ 1] Vlahos C.J., Dekker E.E.
"The complete amino acid sequence and identification of the
active-site arginine peptide of Escherichia coli
2-keto-4-hydroxyglutarate aldolase."
J. Biol. Chem. 263:11683-11691(1988).
PubMed=3136164
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{END}
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