4.1.2.17: L-fuculose-phosphate aldolase

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

Word Map on EC 4.1.2.17

4.1.2.17

dihydroxyacetone

aldolases

dhap

l-rhamnulose-1-phosphate

l-lactaldehyde

l-ribulose-5-phosphate

epimerase

fucose

dhap-dependent

iminocyclitols

epimer

epimerization

l-1,2-propanediol

propanediol

polyhydroxylated

synthesis

Reaction

Synonyms

aldolase, L-fuculose phosphate, F-1PA, Fuc-1PA, FucA, fuculose aldolase, fuculose-1-phosphate aldolase, L-Fuc1P aldolase, L-Fuculose 1-phosphate aldolase, L-Fuculose phosphate aldolase, L-Fuculose-1-P aldolase, L-fuculose-1-phosphate aldolase, L-fuculose-phosphate aldolase

ECTree

4 Lyases

4.1 Carbon-carbon lyases

4.1.2 Aldehyde-lyases

4.1.2.17 L-fuculose-phosphate aldolase

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Results	in table
5244	AA Sequence
2	Application
1	CAS Registry Number
12	Cloned(Commentary)
9	Crystallization (Commentary)
4	General Stability
17	Inhibitors
2	Ki Value [mM]
30	KM Value [mM]
20	Metals/Ions
4	Molecular Weight [Da]
14	Natural Substrates/ Products (Substrates)
129	Organism
11	Pathway
39	PDB ID
5	pH Optimum
4	pH Range
1	pI Value
23	Protein Variants
13	Purification (Commentary)
2	Reaction
4	Reaction Type
38	Reference
13	Specific Activity [micromol/min/mg]
1	Storage Stability
111	Substrates and Products (Substrate)
10	Subunits
44	Synonyms
1	Systematic Name
2	Temperature Optimum [°C]
1	Temperature Stability [°C]
15	Turnover Number [1/s]

Crystallization

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Crystallization on EC 4.1.2.17 - L-fuculose-phosphate aldolase

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2 entries

cocrystallized with phosphoglycolohydroxamate

Escherichia coli

650038

hanging drop vapor diffusion method

Escherichia coli

P0AB87

652834

hanging drop vapor diffusion method, using 0.1 M Tris pH 8.0, 25% PEG 8000, 0.25 M MgCl2

Glaciozyma antarctica

746666

sitting-drop vapour-diffusion and microbatch techniques. Crystals belong to space group P4, with unit-cell parameters a = b = 100.94 A, c = 45.87 A

Thermus thermophilus

663524

to 1.9 A resolution. The enzyme possesses only a single core domain that catalyzes the biological function. No zinc atom is trapped in the active site of the apo structure. Instead, the FucA dimer possesses one sulfate ion per subunit. In chain A the sulfur oxygen atoms are positioned by Asn28, Ser42, Lys46 and Ser68, while in chain B only Asn28, Ser42 and Ser68 take part in the coordination

Thermus thermophilus

Q5SHB9

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