1.5.3.25: fructosyl amine oxidase (glucosone-forming)

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For detailed information about fructosyl amine oxidase (glucosone-forming), go to the full flat file.

Reaction

Synonyms

AgaE-like protein, amadoriase, amadoriase I, amadoriase II, FaoA, FAOAo1, FAOAo2, FAOD, FAOD-Ao1, FAOD-Ao2, FAOX, FAOX-C, FAOX-II, FrlB, fructosyl amine:oxygen oxidoreductase, fructosyl amino acid oxidase, GAOA

ECTree

     1 Oxidoreductases

         1.5 Acting on the CH-NH group of donors

             1.5.3 With oxygen as acceptor

                1.5.3.25 fructosyl amine oxidase (glucosone-forming)

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Results	in table
11	AA Sequence
2	Application
10	Cloned(Commentary)
6	Cofactor
6	Crystallization (Commentary)
2	Expression
4	General Information
7	Inhibitors
66	kcat/KM [mM/s]
100	KM Value [mM]
2	Localization
3	Metals/Ions
6	Molecular Weight [Da]
34	Organism
8	pH Optimum
3	pI Value
57	Protein Variants
2	Purification (Commentary)
3	Reaction
33	Reference
2	Specific Activity [micromol/min/mg]
78	Substrates and Products (Substrate)
11	Subunits
22	Synonyms
1	Systematic Name
5	Temperature Optimum [°C]
2	Temperature Range [°C]
6	Temperature Stability [°C]
75	Turnover Number [1/s]

Crystallization

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Crystallization on EC 1.5.3.25 - fructosyl amine oxidase (glucosone-forming)

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

mutant T60A/A188G/M244L/N257S/L261M, giving rhombic prismatic yellow crystals, space group C2 with unit-cell parameters a 101.08, b 63.36, c 83.07 A, beta 108.8°, to at least 1.8 A resolution, and additionally rod-like crystals, space group P4122 or P4322 with unitcell parameters a = b = 119.09, c 164.66 A and diffract to 2.7 A resolution

Arthrobacter sp. 2-4-1

Q7M0I4

763847

structure of FAOX-II shows an interaction between Lys53 and the isoalloxazine. The ammonium nitrogen of the lysine is in contact with and nearly centered over the aromatic ring of the flavin on the si-face. The positive charge of Lys53 is critical for flavin reduction, but plays very little role in the reaction with molecular oxygen

Aspergillus fumigatus

P78573

764132

structures in free form and in complex with the inhibitor fructosyl-thioacetate, at 1.75 and 1.6 A resolution, respectively. FAOX-II is a two domain FAD-enzyme with an overall topology similar to that of monomeric sarcosine oxidase. Active site residues Tyr-60, Arg-112 and Lys-368 bind the carboxylic portion of the fructosamine, whereas Glu-280 and Arg-411 bind the fructosyl portion

Aspergillus fumigatus

P78573

765037

structures of the free and the substrate-bound form of amadoriase I and comparison with isoform amadoriase II. While in Amadoriase II the loop 59-70 (amadoriase I numbering) is directed toward the core of the protein, in amadoriase I the loop is projected outward and is exposed to the solvent, contributing to the formation of a larger catalytic cavity

Aspergillus fumigatus

O42629

765733

homology modeling and docking of substrates fructosyl L-valine and Nepsilon-fructosyl-L-lysine. Residue Asn354 interacts closely with Nepsilon-fructosyl-L-lysine, but not with fructosyl L-valine

Pichia sp. N1-1

Q3L8U0

765700

homology modeling of structure. Asn354 plays an important role in substrate recognition and can be substituted in order to change substrate specificity while maintaining high catalytic activity

Pichia sp. N1-1

Q3L8U0

764360