97 research outputs found
Escherichia coli inorganic pyrophosphatase : site-directed mutagenesis of the metal binding sites
AbstractAspartic acids 65, 67, 70, 97 and 102 in the inorganic pyrophosphatase of Escherichia coli, identified as evolutionarily conserved residues of the active site, have been replaced by asparagine. Each mutation was found to decrease the ΞΊapp value by approx. 2β3 orders of magnitude. At the same time, the Km values changed only slightly. Only minor changes take place in the pK values of the residues essential for both substrate binding and catalysis. All mutant variants have practically the same affinity to Mg2+ as the wild-type pyrophosphatase
Mg2+ activation of Escherichia coli inorganic pyrophosphatase
AbstractFurther refinement of X-ray data on Escherichia coli inorganic pyrophosphatase [Oganessyan et al. (1994) FEBS Lett. 348, 301β304] to 2.2 Γ
reveals a system of noncovalent interactions involving Tyr55 and Tyr141 in the active site. The pKa for one of the eight Tyr residues in wild-type pyrophosphatase is as low as 9.1 and further decreases to 8.1 upon Mg2+ binding, generating characteristic changes in the absorption spectrum. These effects are lost in a Y55F but not in a Y141F variant. It is suggested that the lower-affinity site for Mg2+ in the enzyme is formed by Tyr55 and Asp70, which are in close proximity in the apo-enzyme structure
Π€ΠΈΠ·ΠΈΠΊΠΎ-Ρ ΠΈΠΌΠΈΡΠ΅ΡΠΊΠΈΠ΅ ΠΎΡΠ½ΠΎΠ²Ρ Ρ ΠΈΠΌΠΈΠΈ ΠΈ ΡΠ΅Ρ Π½ΠΎΠ»ΠΎΠ³ΠΈΠΈ ΠΏΠ»Π°ΡΠΈΠ½ΠΎΠ²ΡΡ ΠΌΠ΅ΡΠ°Π»Π»ΠΎΠ² ΠΈ ΠΈΡ ΡΠΎΠ΅Π΄ΠΈΠ½Π΅Π½ΠΈΠΉ
The date of investigation on chemistry and technology of platinum metals in the large years are presented. The complexes of palladium(II) with macroheterocyclyc compounds are syntesited. The application of electrochemical processes for selection of platinum metals from solutions and applyed of concentrate of platinum metals is shownΠΡΠ°ΡΠΊΠΎ ΡΠ°ΡΡΠΌΠΎΡΡΠ΅Π½Ρ ΡΠ΅Π·ΡΠ»ΡΡΠ°ΡΡ Π²ΡΠΏΠΎΠ»Π½Π΅Π½Π½ΡΡ
Π² ΠΏΠΎΡΠ»Π΅Π΄Π½ΠΈΠ΅ Π³ΠΎΠ΄Ρ ΡΠ°Π±ΠΎΡ Π² ΠΎΠ±Π»Π°ΡΡΠΈ Ρ
ΠΈΠΌΠΈΠΈ ΠΈ ΡΠ΅Ρ
Π½ΠΎΠ»ΠΎΠ³ΠΈΠΈ ΠΏΠ»Π°ΡΠΈΠ½ΠΎΠ²ΡΡ
ΠΌΠ΅ΡΠ°Π»Π»ΠΎΠ². ΠΡΠΏΠΎΠ»Π½Π΅Π½ ΡΠΈΠ½ΡΠ΅Π· ΠΊΠΎΠΌΠΏΠ»Π΅ΠΊΡΠΎΠ² ΠΏΠ°Π»Π»Π°Π΄ΠΈΡ(II) Ρ ΠΌΠ°ΠΊΡΠΎΠ³Π΅ΡΠ΅ΡΠΎΡΠΈΠΊΠ»ΠΈΡΠ΅ΡΠΊΠΈΠΌΠΈ ΡΠΎΠ΅Π΄ΠΈΠ½Π΅-Π½ΠΈΡΠΌΠΈ. ΠΠΎΠΊΠ°Π·Π°Π½Π° Π²ΠΎΠ·ΠΌΠΎΠΆΠ½ΠΎΡΡΡ ΠΏΡΠΈΠΌΠ΅Π½Π΅Π½ΠΈΡ ΡΠ»Π΅ΠΊΡΡΠΎΡ
ΠΈΠΌΠΈΡΠ΅ΡΠΊΠΎΠ³ΠΎ ΠΌΠ΅ΡΠΎΠ΄Π° Π΄Π»Ρ ΠΈΠ·Π²Π»Π΅ΡΠ΅Π½ΠΈΡ ΠΏΠ»Π°ΡΠΈΠ½ΠΎΠ²ΡΡ
ΠΌΠ΅ΡΠ°Π»Π»ΠΎΠ² ΠΈΠ· ΡΠ°ΡΡΠ²ΠΎΡΠΎΠ² ΠΈ ΠΏΠΎΠ»ΡΡΠ΅Π½ΠΈΡ ΠΊΠΎΠ½ΡΠ΅Π½ΡΡΠ°ΡΠΎΠ²
The action of the acid phosphomonoesterase of wheat bran on the methylamide of N-bensoyl-O-pyrophosphoserine
Hydrolysis of the pyrophosphate bond of seryl pyrophosphates by the alkaline phosphatase ofEscherichia coli
Fluoride inhibition of inorganic pyrophosphatase II. Isolation and characterization of a covalent intermediate between enzyme and entire substrate molecule
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