4.1.3.16: 4-Hydroxy-2-oxoglutarate aldolase

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For detailed information about 4-Hydroxy-2-oxoglutarate aldolase, go to the full flat file.

Reaction

Synonyms

2-keto-4-hydroxybutyrate aldolase, 2-keto-4-hydroxyglutarate aldolase, 2-keto-4-hydroxyglutaric aldolase, 2-oxo-3-deoxy-6-phosphogluconate aldolase, 2-oxo-4-hydroxyglutarate aldolase, 2-oxo-4-hydroxyglutaric aldolase, 4-hydroxy-2-ketoglutarate aldolase, 4-hydroxy-2-ketoglutaric aldolase, 4-hydroxy-2-oxoglutarate aldolase, aldolase, 4-hydroxy-2-oxoglutarate, DHDPSL, dihydrodipicolinate synthase-like enzyme, DL-4-Hydroxy-2-ketoglutarate aldolase, EC 4.1.2.1, EC 4.1.2.31, eda, Entner-Doudoroff aldolase, hOGA, HOGA1, hydroxyketoglutarate aldolase, Hydroxyketoglutaric aldolase, KDPGlc aldolase, KHG-aldolase

ECTree

     4 Lyases

         4.1 Carbon-carbon lyases

             4.1.3 Oxo-acid-lyases

                4.1.3.16 4-Hydroxy-2-oxoglutarate aldolase

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Results	in table
4	Activating Compound
6473	AA Sequence
2	Application
1	CAS Registry Number
5	Cloned(Commentary)
2	Crystallization (Commentary)
80	Disease/ Diagnostics
4	General Information
1	General Stability
48	Inhibitors
10	kcat/KM [mM/s]
3	Ki Value [mM]
33	KM Value [mM]
4	Localization
12	Metals/Ions
16	Molecular Weight [Da]
8	Natural Substrates/ Products (Substrates)
21	Organism
6	Pathway
38	PDB ID
6	pH Optimum
5	pH Range
23	Protein Variants
10	Purification (Commentary)
1	Reaction
2	Reaction Type
20	Reference
13	Source Tissue
12	Specific Activity [micromol/min/mg]
4	Storage Stability
50	Substrates and Products (Substrate)
8	Subunits
26	Synonyms
1	Systematic Name
4	Temperature Optimum [°C]
2	Temperature Stability [°C]
11	Turnover Number [1/s]

Crystallization

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Crystallization on EC 4.1.3.16 - 4-Hydroxy-2-oxoglutarate aldolase

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

hamging drop vapor diffusion method, using 100 mM HEPES-NaOH pH 7.0, 200 mM Na2SO4, 22.5% (w/v) PEG 3350, and 20% (v/v) glycerol or 100 mM Tris-HCl pH 8.0 and 1.8 M ammonium sulfate

Bos taurus

Q0P5I5

746641

to 1.97 A resolution, crystal structure of enzyme bound to pyruvate. Modeling of the 4-hydroxy-2-oxoglutarate-Schiff base intermediate and kinetic analyses of site-directed mutants support the importance of Lys196 as the nucleophile, Tyr168 and Ser77 as components of a proton relay, and Asn78 and Ser198 as unique residues that facilitate substrate binding

Homo sapiens

Q86XE5

723542