4.2.2.16: levan fructotransferase (DFA-IV-forming)

This is an abbreviated version!
For detailed information about levan fructotransferase (DFA-IV-forming), go to the full flat file.

Reaction

Synonyms

2,6-beta-D-fructan D-fructosyl-D-fructosyltransferase (forming di-beta-D-fructofuranose 2,6':2',6-dianhydride), fructotransferase, levan, FTF, levan fructotransferase, levan fructotransferase (DFA-IV-forming), LFT, LFTase, LftM

ECTree

     4 Lyases

         4.2 Carbon-oxygen lyases

             4.2.2 Acting on polysaccharides

                4.2.2.16 levan fructotransferase (DFA-IV-forming)

Advanced search results

Do not include text mining results

Include results (more...)

Include results (more...)

Results	in table
2	AA Sequence
9	Application
1	CAS Registry Number
11	Cloned(Commentary)
1	Crystallization (Commentary)
2	General Stability
23	Inhibitors
1	KM Value [mM]
8	Localization
4	Metals/Ions
6	Molecular Weight [Da]
2	Natural Substrates/ Products (Substrates)
159	Organism
16	PDB ID
9	pH Optimum
2	pH Range
9	Protein Variants
8	Purification (Commentary)
1	Reaction
1	Reaction Type
34	Reference
2	Source Tissue
4	Specific Activity [micromol/min/mg]
43	Substrates and Products (Substrate)
8	Subunits
29	Synonyms
1	Systematic Name
8	Temperature Optimum [°C]
1	Temperature Range [°C]
5	Temperature Stability [°C]

Crystallization

print visible entries

print all entries

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

Crystallization on EC 4.2.2.16 - levan fructotransferase (DFA-IV-forming)

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

in apo form, as well as in complexes with sucrose and levanbiose. Enzyme contains an active site that accommodates a difructosaccharide using the -1 and -2 subsites. Binding is facilitated by small side chain residues in the loop region of a catalytic beta-propeller N-domain. An additional oligosaccharide-binding site is in the beta-sandwich C-domain, supporting its role in carbohydrate recognition

Paenarthrobacter ureafaciens

Q9KJD0

729994