3.2.1.7: inulinase

This is an abbreviated version!
For detailed information about inulinase, go to the full flat file.

Reaction

Synonyms

2,1-beta-D-fructanfructanohydrolase, AARAC_000847, An11g03200, AUD_0597, beta-2,1-D-fructan fructanohydrolase, beta-D-fructan fructanohydrolase, Endo I, Endo-I, Endo-II, endo-inulinase, endoinulinase, EnIA, extracellular endo-inulinase, fructofuranosyl hydrolase, Fructozyme L, Insulinase, inu1, Inu2, InuA, inuB, inuC, inuE, inulase, inulinase, P-III, PENSUB_1400, PENSUB_5768, PENSUB_5772, TCE0_044r16122, TSTA_051680, Xcp KM 24

ECTree

     3 Hydrolases

         3.2 Glycosylases

             3.2.1 Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds

                3.2.1.7 inulinase

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Results	in table
10	Activating Compound
27	AA Sequence
92	Application
1	CAS Registry Number
14	Cloned(Commentary)
2	Crystallization (Commentary)
2	Expression
73	General Information
72	Inhibitors
5	kcat/KM [mM/s]
44	KM Value [mM]
44	Localization
29	Metals/Ions
29	Molecular Weight [Da]
48	Natural Substrates/ Products (Substrates)
153	Organism
2	PDB ID
43	pH Optimum
7	pH Range
22	pH Stability
2	pI Value
14	Posttranslational Modification
36	Protein Variants
22	Purification (Commentary)
1	Reaction
1	Reaction Type
132	Reference
14	Source Tissue
21	Specific Activity [micromol/min/mg]
1	Storage Stability
179	Substrates and Products (Substrate)
56	Subunits
158	Synonyms
1	Systematic Name
41	Temperature Optimum [°C]
5	Temperature Range [°C]
44	Temperature Stability [°C]
20	Turnover Number [1/s]

Crystallization

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Crystallization on EC 3.2.1.7 - inulinase

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

to 1.5 A resolution. Structural arrangement shows a N-terminal 5fold beta-propeller catalytic domain with four beta-sheets and a C-terminal beta-sandwich domain organized in two beta-sheets with five beta-strands. Comparison with other GH32 enzymes reveals the presence of an extra pocket in the isoform INU2 catalytic site, formed by two loops and the conserved motif W-M(I)-N-D(E)-P-N-G. This cavity explains the endo-activity of the enzyme, the critical role of residue Trp40 and particularly the cleavage at the third unit of the inulin(-like) substrates

Aspergillus ficuum

O94220

729331

homology modeling, docking and molecular simulations using structure of Aspergillus awamori as a template. The thermodynamic equilibrium is reached after a few picoseconds, the enzyme toggles between two states during the entire equilibrium phase of the dynamics. The first conformation of the funnel domain corresponds to the closed/inactive state whereas the second conformation corresponds to the open/active conformation

Aspergillus niger

O74641

707832