4.1.2.40: tagatose-bisphosphate aldolase

This is an abbreviated version!
For detailed information about tagatose-bisphosphate aldolase, go to the full flat file.

Reaction

Synonyms

aldolase, tagatose 1,6-diphosphate, D-Tagatose 1,6-diphosphate aldolase, D-tagatose-1,6-bisphosphate aldolase, D-Tagatose-1,6-bisphosphate aldolase (class I), D-Tagatose-1,6-bisphosphate aldolase (class II), GatY, LacD, LacD.1, Tagatose 1,6-bisphosphate aldolase, Tagatose bisphosphate aldolase, tagatose-1,6-biphosphate aldolase 2, tagatose-1,6-bisphosphate aldolase, Tagatose-1,6-diphosphate aldolase, Tagatose-bisphosphate aldolase, TBA, TBP aldolase, TDP aldolase

ECTree

     4 Lyases

         4.1 Carbon-carbon lyases

             4.1.2 Aldehyde-lyases

                4.1.2.40 tagatose-bisphosphate aldolase

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Results	in table
6549	AA Sequence
2	Application
1	CAS Registry Number
5	Cloned(Commentary)
5	Crystallization (Commentary)
1	General Stability
6	Inhibitors
6	kcat/KM [mM/s]
11	KM Value [mM]
8	Metals/Ions
8	Molecular Weight [Da]
9	Natural Substrates/ Products (Substrates)
25	Organism
11	Pathway
54	PDB ID
4	pH Optimum
1	pH Range
7	Protein Variants
7	Purification (Commentary)
3	Reaction
1	Reaction Type
21	Reference
3	Specific Activity [micromol/min/mg]
2	Storage Stability
41	Substrates and Products (Substrate)
9	Subunits
25	Synonyms
1	Systematic Name
6	Turnover Number [1/s]

Crystallization

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Crystallization on EC 4.1.2.40 - tagatose-bisphosphate aldolase

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

in complex with phosphoglycolohydroxamate

Escherichia coli

-

652267

sitting drop vapor diffusion method

Staphylococcus aureus

Q5HE13

715040

sitting drop vapor diffusion method, using

Staphylococcus aureus

Q5HE13

715040

native enzyme and native enzyme in complex with dihydroxyacetone-P, by the hanging drop method. Native free TBP aldolase crystallized in the P212121 space group with four protomers in the asymmetric unit and diffracted to 1.87 A resolution. Folding of the polypeptide chain of TBP aldolase corresponds to a (alpha/beta)8 or TIM barrel fold. The liganded crystal structure is isomorphous with the crystal structure of the native aldolase and diffracted to 1.92 A resolution

Streptococcus pyogenes

-

704712

recombinant, orthorhombic crystals suitable for structural analysis are obtained by the hanging-drop vapour-diffusion method for the native enzyme and the selenomethionine derivative. The crystals belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 63.7, b = 108.1, c = 238.7 A for the native form and a = 64.1, b = 108.3, c = 239.8 A for the selenomethionine derivative. The asymmetric unit contains four protomers

Streptococcus pyogenes

-

663519