1.20.99.1: arsenate reductase (donor)

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For detailed information about arsenate reductase (donor), go to the full flat file.

Reaction

Synonyms

Acr2, ACR2.1, ACR2.2, AR, Arr, ArrA, ArsC, arsenate reductase, arsenite oxidase, As(V) reductase, ATQ1, Cdc25B, Cdc25C, EC 1.97.1.6, gene arsC proteins, HAC1, More, proteins (specific proteins and subclasses), genearsC, reductase, arsenate, respiratory arsenate reductase

ECTree

     1 Oxidoreductases

         1.20 Acting on phosphorus or arsenic in donors

             1.20.99 With unknown physiological acceptors

                1.20.99.1 arsenate reductase (donor)

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Results	in table
17	Activating Compound
9	AA Sequence
1	CAS Registry Number
6	Cloned(Commentary)
6	Cofactor
9	Crystallization (Commentary)
3	Expression
5	General Information
4	kcat/KM [mM/s]
14	KM Value [mM]
3	Localization
17	Metals/Ions
13	Molecular Weight [Da]
33	Natural Substrates/ Products (Substrates)
50	Organism
2	Pathway
4	pH Optimum
1	pH Range
6	Protein Variants
6	Purification (Commentary)
7	Reaction
1	Reaction Type
47	Reference
11	Source Tissue
5	Specific Activity [micromol/min/mg]
67	Substrates and Products (Substrate)
9	Subunits
57	Synonyms
1	Systematic Name
3	Temperature Optimum [°C]
12	Turnover Number [1/s]

Crystallization

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Crystallization on EC 1.20.99.1 - arsenate reductase (donor)

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

X-ray diffraction structure determination and analysis of 2 different crystal forms at 1.64-2.03 A using multiple isomorphous replacement with anomalous scattering and multiple-wavelength anomalous dispersion methods

Alcaligenes faecalis

-

287858

purified recombinant wild-type and SeMet-labeled enzyme, 4°C, PEG or PEG methyl ether is utilized as main precipitant, 2 crystal forms, X-ray diffraction structure determination and analysis at 2.2 A, flash-annealing technique

Bacillus subtilis

-

657473

purified wild-type and selenomethionine-labeled enzyme, hanging drop vapour diffusion method, enzyme in 0.1 M sodium acetate, pH 4.4-4.6, 0.2 M ammonium sulfate, in presence of 30-35% PEG methyl ether, and 5 mM DTT, crystal structure in reduced form, X-ray diffraction structure determination and analysis at 1.6-2.4 A resolution

Bacillus subtilis

-

660404

solution structure and backbone dynamics of both the reduced and oxidized forms of enzyme. Reduced from undergoes millisecond conformational changes in the functional P-loop and C82-C89. In the oxidized form, C82-C89 shows motional flexibility on both picosecond-to-nanosecond and possibly millisecond scales

Bacillus subtilis

-

674507

solution structure of enzyme in complex with thioarsenate represents the transiently formed intermediate during the intermolecualr thiol-disulfide exchange reaction. Substantial conformational changes are coupled to the reaction process

Bacillus subtilis

-

674785

free enzyme or enzyme complexed with arsenate and arsenite, X-ray diffraction structure determination and analysis at 1.65 A and 1.26 A, respecively

Escherichia coli

-

660525

in complex with arsenitate and arsenite and enzyme alone. Native structure shows sulfate and sulfite ions binding in the active site as analogs of arsenate and arsenite. Arsenate forms a covlaent adduct with C12 in the active site, showing tetrahedral geometry. The corresponding adduct with arsenite binds as thiarsahydroxy adduct. High number of 385 water molecules bound to crystal structure

Escherichia coli

-

660525

wild-type and mutant R60K and R60A enzymes in complex with product arsenite, X-ray diffraction structure determination and analysis at 1.3-1.8 A resolution

Escherichia coli

-

660461

recombinant protein, space group P321

Leishmania major

-

671156