1.2.3.3: pyruvate oxidase

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

Reaction

Synonyms

acetyl phosphate-producing pyruvate oxidase, phosphate-dependent pyruvate oxidase, POD, POX, POX-2, poxB, PoxF, PyOD, PyrOx, pyruvate oxidase, pyruvate:oxygen-2-oxidoreductase (phosphorylating), pyruvic oxidase, SpxB, SpxB protein

ECTree

     1 Oxidoreductases

         1.2 Acting on the aldehyde or oxo group of donors

             1.2.3 With oxygen as acceptor

                1.2.3.3 pyruvate oxidase

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Results	in table
7	Activating Compound
1477	AA Sequence
19	Application
1	CAS Registry Number
11	Cloned(Commentary)
38	Cofactor
7	Crystallization (Commentary)
4	Expression
18	General Information
1	General Stability
6	Inhibitors
4	Ki Value [mM]
13	KM Value [mM]
9	Metals/Ions
5	Molecular Weight [Da]
55	Natural Substrates/ Products (Substrates)
124	Organism
2	Pathway
20	PDB ID
4	pH Optimum
1	pH Range
2	pH Stability
11	Protein Variants
6	Purification (Commentary)
2	Reaction
6	Reaction Type
78	Reference
20	Source Tissue
1	Specific Activity [micromol/min/mg]
1	Storage Stability
84	Substrates and Products (Substrate)
9	Subunits
70	Synonyms
1	Systematic Name
4	Temperature Optimum [°C]
1	Temperature Stability [°C]
9	Turnover Number [1/s]

Crystallization

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Crystallization on EC 1.2.3.3 - pyruvate oxidase

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

by the hanging-drop vapour-diffusion method. POX complexed with FAD, with FAD and thiamine diphosphate, and with FAD and the 2-acetyl-thiamine diphosphate intermediate at 1.6, 1.8 and 1.9 A resolution, respectively. Each subunit of the homotetrameric POX enzyme consists of three domains. FAD is bound within one subunit in the elongated conformation and with the flavin moiety being planar in the oxidized form, while thiamine diphosphate is bound in a conserved V-conformation at the subunit-subunit interface. The structures reveal flexible regions in the active-site tunnel which may undergo conformational changes to allow the entrance of the substrates and the exit of the reaction products. Lys478, the side chain of which may be bent or extended depending on the stage of catalysis

Aerococcus viridans

A9X9K8

684189

the full-length form and a proteolytically activated C-terminal truncation variant which lacks the last 23 amino acids, by the hanging-drop vapour-diffusion method using either protamine sulfate (fulllength POX) or 2-methyl-2,4-pentanediol (DELTA23 POX) as precipitants. To 2.9 A resolution. Fulllength POX crystallizes in the tetragonal space group P43212 with two monomers per asymmetric unit, the crystals of DELTA23 POX belong to the orthorhombic space group P212121 and contain 12 monomers per asymmetric unit

Escherichia coli

-

684193

in complex with the thiamin diphosphate carbanion-enamine and two-electron reduced FAD, hanging drop vapor diffusion method

Lactiplantibacillus plantarum

-

726382

mutant V265A

Lactiplantibacillus plantarum

-

654686

triple mutant at 2.1 A resolution

Lactiplantibacillus plantarum

-

114312

V265A mutant

Lactiplantibacillus plantarum

P37063

672023

wild-type at 2.5 A resolution, triple mutant at 2.1 A resolution, hanging drop vapour diffusion technique

Lactiplantibacillus plantarum

-

390433