4.1.2.52: 4-hydroxy-2-oxoheptanedioate aldolase

This is an abbreviated version!
For detailed information about 4-hydroxy-2-oxoheptanedioate aldolase, go to the full flat file.

Reaction

Synonyms

4-hydroxy-2-oxo-heptane-1,7-dioate aldolase, HpaI, HpcH

ECTree

4 Lyases

4.1 Carbon-carbon lyases

4.1.2 Aldehyde-lyases

4.1.2.52 4-hydroxy-2-oxoheptanedioate aldolase

Advanced search results

Do not include text mining results

Include

results (more...)

Include

results (more...)

Results	in table
2354	AA Sequence
3	Cloned(Commentary)
4	Crystallization (Commentary)
2	General Information
1	General Stability
7	Inhibitors
18	kcat/KM [mM/s]
8	Ki Value [mM]
24	KM Value [mM]
12	Metals/Ions
3	Molecular Weight [Da]
4	Natural Substrates/ Products (Substrates)
5	Organism
6	Pathway
6	PDB ID
1	pH Range
8	Protein Variants
3	Purification (Commentary)
2	Reaction
5	Reference
19	Substrates and Products (Substrate)
2	Subunits
7	Synonyms
1	Systematic Name
19	Turnover Number [1/s]

Crystallization

print visible entries

print all entries

Go back to the abbreviated version
of the Enzyme Summary Page.

Crystallization on EC 4.1.2.52 - 4-hydroxy-2-oxoheptanedioate aldolase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.

top print hide

Go to Crystallization (commentary) Search

crystallization of apo-HpcH, because divalent metal ion is lost during the purification process, resulting in preparation of the inactive apo form of the enzyme, crystals grown using the hanging-drop vapour diffusion method

Escherichia coli

722955

HpcHMg2+oxamate crystals grown with the addition of 10 mM magnesium chloride and sodium oxamate (substrate analogue), elucidation of active site architecture

Escherichia coli

722955

in complex with substrate or products, hanging drop vapor diffusion method, using

Escherichia coli

B1IS70

725493

the active site of HpaI is formed by approx. 30 residues from adjacent dimers and consists of an approx. 15 A deep bell-shaped cleft with an approx. 12 A wide mouth. This broad entrance to the active site is predominantly lined with noncharged residues and a few positively charged residues

Escherichia coli

702377