4.1.2.19: rhamnulose-1-phosphate aldolase

This is an abbreviated version!
For detailed information about rhamnulose-1-phosphate aldolase, go to the full flat file.

Reaction

Synonyms

aldolase, rhamnulose phosphate, L-Rhamnulose-1-phosphate aldolase, L-rhamnulose-1-phosphate aldolase (class II), L-Rhamnulose-1-phosphate L-lactaldehyde-lyase, Rha-1PA, RhaD, Rhamn-1PA, rhamnulose 1-phosphate aldolase, Rhamnulose phosphate aldolase, rhamnulose-1-phosphate aldolase, RhuA, TM1072

ECTree

     4 Lyases

         4.1 Carbon-carbon lyases

             4.1.2 Aldehyde-lyases

                4.1.2.19 rhamnulose-1-phosphate aldolase

Advanced search results

Do not include text mining results

Include results (more...)

Include results (more...)

Results	in table
1	Activating Compound
3200	AA Sequence
2	Application
1	CAS Registry Number
10	Cloned(Commentary)
5	Crystallization (Commentary)
1	General Stability
1	IC50 Value
28	Inhibitors
1	kcat/KM [mM/s]
1	Ki Value [mM]
23	KM Value [mM]
36	Metals/Ions
9	Molecular Weight [Da]
11	Natural Substrates/ Products (Substrates)
1	Organic Solvent Stability
408	Organism
7	Pathway
49	PDB ID
5	pH Optimum
4	pH Range
1	pH Stability
18	Protein Variants
11	Purification (Commentary)
1	Reaction
9	Reaction Type
33	Reference
12	Specific Activity [micromol/min/mg]
5	Storage Stability
110	Substrates and Products (Substrate)
8	Subunits
33	Synonyms
1	Systematic Name
2	Temperature Optimum [°C]
1	Temperature Range [°C]
1	Temperature Stability [°C]
5	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 4.1.2.19 - rhamnulose-1-phosphate 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

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

-

Escherichia coli

-

5066, 5071

hanging drop method, crystallizes in space group P3(2)21

Escherichia coli

P32169

654067

mutant enzymes by hanging drop vapour diffusion method, with 100 mM sodium acetate pH 4.5, 50% (v/v) ethylene glycol and 5% (w/v) PEG1000

Escherichia coli

P32169

678345

structure established at 1.35 A resolution in a crystal form that is obtained by a surface mutation and has one subunit of the C4-symmetric tetramer in the asymmetric unit. Crystals of the wild-type enzyme with their 20 crystallographically asymmetric subunits diffract to only 2.7 A resolution are much too complex for a convenient analysis of structural modifications. For both reasons, a more suitable crystal form is obtained by producing the six point mutants W8T, Q51R, Q52E, D98Y, E192A and E254R at the protein surface far away from the active center

Escherichia coli

P32169

654673