Probing the active site of L-aspartate oxidase by site-directed mutagenesis: Role of basic residues in fumarate reduction

Tedeschi, G.; Ronchi, S.; Simonic, T.; Treu, C.; Mattevi, A.; Negri, A.; Biochemistry 40, 4738-4744 (2001)

 show all sequences of 1.4.3.16

Data extracted from this reference:

Engineering
Amino acid exchange Commentary Organism
H244A binds substrate analogues with higher dissociation constants and presents lower kcat/Km values in the reduction of fumarate Escherichia coli
H244S binds substrate analogues with higher dissociation constants and presents lower kcat/Km values in the reduction of fumarate Escherichia coli
H351A binds substrate analogues with higher dissociation constants and presents lower kcat/Km values in the reduction of fumarate Escherichia coli
H351S binds substrate analogues with higher dissociation constants and presents lower kcat/Km values in the reduction of fumarate Escherichia coli
R386L binds substrate analogues with higher dissociation constants and presens lower kcat/Km values in the reduction of fumarate Escherichia coli
Organism
Organism Primary Accession No. (UniProt) Commentary Textmining
Escherichia coli
-
 fumarate reductase in anaerobic conditions
-
Purification (Commentary)
Commentary Organism
overexpression in Escherichia coli Escherichia coli
Substrates and Products (Substrate)
Substrates Commentary Substrates Literature (Substrates) Organism Products Commentary (Products) Literature (Products) Organism (Products) Reversibility
L-aspartate + H2O + O2 fumarate or succinate can be electron acceptor instead of O2 391762 Escherichia coli oxaloacetate + NH3 + H2O2
-
-
-
 ?
Cofactor
Cofactor Commentary Organism Structure
FAD
-
 Escherichia coli
Cofactor (protein specific)
Cofactor Commentary Organism Structure
FAD
-
 Escherichia coli
Engineering (protein specific)
Amino acid exchange Commentary Organism
H244A binds substrate analogues with higher dissociation constants and presents lower kcat/Km values in the reduction of fumarate Escherichia coli
H244S binds substrate analogues with higher dissociation constants and presents lower kcat/Km values in the reduction of fumarate Escherichia coli
H351A binds substrate analogues with higher dissociation constants and presents lower kcat/Km values in the reduction of fumarate Escherichia coli
H351S binds substrate analogues with higher dissociation constants and presents lower kcat/Km values in the reduction of fumarate Escherichia coli
R386L binds substrate analogues with higher dissociation constants and presens lower kcat/Km values in the reduction of fumarate Escherichia coli
Purification (Commentary) (protein specific)
Commentary Organism
overexpression in Escherichia coli Escherichia coli
Substrates and Products (Substrate) (protein specific)
Substrates Commentary Substrates Literature (Substrates) Organism Products Commentary (Products) Literature (Products) Organism (Products) Reversibility
L-aspartate + H2O + O2 fumarate or succinate can be electron acceptor instead of O2 391762 Escherichia coli oxaloacetate + NH3 + H2O2
-
-
-
 ?

See also following references to EC number 1.4.3.16 (sorted by year of publication):
No.1st authorPub
Med		titleorganimsjournalvolumepagesyearActivating CompoundApplicationCloned(Commentary)Crystallization (Commentary)EngineeringGeneral StabilityInhibitorsKM Value [mM]LocalizationMetals/IonsMolecular Weight [Da]Natural Substrates/ Products (Substrates)Organic Solvent StabilityOrganismOxidation StabilityPosttranslational ModificationPurification (Commentary)ReactionRenatured (Commentary)Source TissueSpecific Activity [micromol/min/mg]Storage StabilitySubstrates and Products (Substrate)SubunitsTemperature Optimum [°C]Temperature Range [°C]Temperature Stability [°C]Turnover Number [1/s]pH OptimumpH RangepH StabilityCofactorKi Value [mM]pI ValueIC50 ValueActivating Compound (protein specific)Application (protein specific)Cloned(Commentary) (protein specific)Cofactor (protein specific)Crystallization (Commentary) (protein specific)Engineering (protein specific)General Stability (protein specific)IC50 Value (protein specific)Inhibitors (protein specific)Ki Value [mM] (protein specific)KM Value [mM] (protein specific)Localization (protein specific)Metals/Ions (protein specific)Molecular Weight [Da] (protein specific)Natural Substrates/ Products (Substrates) (protein specific)Organic Solvent Stability (protein specific)Oxidation Stability (protein specific)Posttranslational Modification (protein specific)Purification (Commentary) (protein specific)Renatured (Commentary) (protein specific)Source Tissue (protein specific)Specific Activity [micromol/min/mg] (protein specific)Storage Stability (protein specific)Substrates and Products (Substrate) (protein specific)Subunits (protein specific)Temperature Optimum [°C] (protein specific)Temperature Range [°C] (protein specific)Temperature Stability [°C] (protein specific)Turnover Number [1/s] (protein specific)pH Optimum (protein specific)pH Range (protein specific)pH Stability (protein specific)pI Value (protein specific)ExpressionGeneral InformationGeneral Information (protein specific)Expression (protein specific)KCat/KM [mM/s]KCat/KM [mM/s] (protein specific)
711324TedeschiOn the catalytic role of the a ...Escherichia coliBiochimie921335-13422010--1-4-110---3-3--------711--101--1-----11-4--1-10---3--------711--101----22-1010
685396SakurabaStructure of L-aspartate oxida ...Sulfolobus tokodaiiBiochim. Biophys. Acta1784563-5712008--11---1--3--4--1---1-11--1-1-11-----111-----1--3----1--1-11--1-1-1-------
686712MarinoniCharacterization of L-aspartat ...Bacillus subtilisFEBS J.2755090-51072008--1----2--2--4--1-----221--21--1-----11------2--2----1----221--21----11-22
676612KatohEarly steps in the biosynthesi ...Arabidopsis thalianaPlant Physiol.141851-8572006-11-1---1----4-----1--1-------------11--1-----1--------1--1---------------
391763BossiStructure of FAD-bound L-aspar ...Escherichia coliBiochemistry413018-30242002---1---------2--------1--------1------11------------------1---------------
391765SakurabaL-Aspartate oxidase is present ...Pyrococcus horikoshiiExtremophiles6275-2812002-----1----1--7--1---1-111---1------------1------1----1--1-111---1---------
656090MessnerMechanism of superoxide and hy ...Escherichia coliJ. Biol. Chem.27742563-425712002-----------1-1--------3--------1------1----------1--------3---------------
391762TedeschiProbing the active site of L-a ...Escherichia coliBiochemistry404738-47442001----5--------5--1-----1--------1------1-5------------1----1---------------
391761TedeschiL-Aspartate oxidase from Esche ...Escherichia coliEur. J. Biochem.239427-4331996-------------4--1-----1----2---1------1--------------1----1----2----------
391764MortarinoL-aspartate oxidase from Esche ...Escherichia coliEur. J. Biochem.239418-4261996----1--------3--1-----1--------1------1-1------------1----1---------------
391756SeifertExpression of the E. coli nadB ...Escherichia coliBiol. Chem. Hoppe-Seyler371239-2481990-----162---1-3--1---1-211--1---1------1--1-6-2---1---1--1-211--1----------
391757FlachmannMolecular biology of pyridine ...Escherichia coliEur. J. Biochem.175221-2291988--1-------11-3--1-----2-----1--------1----------11---1----2-----1---------
391759WilderThe L-aspartate oxidase report ...Gossypium hirsutumBiochem. Biophys. Res. Commun.123836-84119841------------3--------1------------1----------------------1---------------
391758HosokawaHigher plants contain L-aspara ...Gossypium hirsutumBiochem. Biophys. Res. Commun.111188-1931983------11--1--4--1--2--1--------------------1-1--1----1-2--1---------------
391760NasuL-Aspartate oxidase, a newly d ...Escherichia coliJ. Biol. Chem.257626-63219821-----1----1-3--1---1-2--------1---1--1----1-----1---1--1-2---------------