scholarly journals Characterization of a Bifunctional PutA Homologue fromBradyrhizobium japonicumand Identification of an Active Site Residue that Modulates Proline Reduction of the Flavin Adenine Dinucleotide Cofactor†

Biochemistry ◽  
2005 ◽  
Vol 44 (25) ◽  
pp. 9130-9139 ◽  
Author(s):  
Navasona Krishnan ◽  
Donald F. Becker
Keyword(s):  
Active Site ◽  
Flavin Adenine Dinucleotide ◽  
Active Site Residue

scholarly journals Charge Reversal of a Critical Active-Site Residue of Cytochrome-c Peroxidase. Characterization of the Arg48Glu Variant

1997 ◽  
Vol 243 (1-2) ◽  
pp. 72-84 ◽  
Author(s):  
Jordi Bujons ◽  
Alexander Dikiy ◽  
Juan C. Ferrer ◽  
Lucia Banci ◽  
A. Grant Mauk
Keyword(s):  
Cytochrome C ◽  
Active Site ◽  
Cytochrome C Peroxidase ◽  
Active Site Residue ◽  
Charge Reversal

Characterization of the 1-phosphohistidinyl residue in the phosphocarrier protein HPr of the phosphoenolpyruvate:sugar phosphotransferase system of Streptococcus faecalis

1988 ◽  
Vol 66 (1) ◽  
pp. 76-80 ◽  
Author(s):  
E. B. Waygood ◽  
K. Pasloske ◽  
L. T. J. Delbaere ◽  
J. Deutscher ◽  
W. Hengstenberg
Keyword(s):  
Escherichia Coli ◽  
Active Site ◽  
Carboxyl Group ◽  
Active Site Residue ◽  
Phosphotransferase System ◽  
Temperature Dependent ◽  
Streptococcus Faecalis ◽  
Terminal Residue ◽  
Hydrolysis Of

The phosphocarrier protein HPr of the bacterial phosphoenolpyruvate:sugar phosphotransferase system contains 1- phosphohistidine at residue 15. This residue and the active site residue Arg-17 are conserved in HPrs isolated from both Gram-positive and -negative bacteria. The pH- and temperature-dependent hydrolysis of the 1-phosphohistidinyl residue in P-HPr from Streptococcus faecalis has been investigated. The results show that the hydrolysis properties are very similar to those previously reported for P-HPr from Escherichia coli. It was postulated that the unusual hydrolysis properties were due to the presence of a carboxyl group at the active site, and it is now known that in HPr from Escherichia coli the C-terminal residue Glu-85 is present. The results in this paper suggest that a similar carboxyl group is present at the active site in HPr from Streptococcus faecalis.

PHYSIOLOGY OF SELENITE REDUCTION BY ENTEROCOCCI: II. CHARACTERIZATION OF SELENITE INHIBITION AND ITS REVERSAL BY ASCORBATE

1967 ◽  
Vol 13 (9) ◽  
pp. 1183-1193 ◽  
Author(s):  
Richard C. Tilton ◽  
Haim B. Gunner ◽  
Warren Litsky
Keyword(s):  
Active Site ◽  
Flavin Adenine Dinucleotide ◽  
Inhibitory Effect ◽  
Inhibitory Effects ◽  
Selenite Reduction ◽  
Heat Stable ◽  
Oxygen Sensitive ◽  
Test Organisms ◽  
Reduced Nicotinamide Adenine Dinucleotide

Cell-free extracts of Streptococcus faecalis N83 and Streptococcus faecium K6A were shown to possess comparable enzyme systems for the reduction of selenite to metallic selenium. The enzymatic complement of each of the organisms was oxygen sensitive, heat stable, and required flavin adenine dinucleotide (FAD) for maximum stimulation. Potent reduced nicotinamide adenine dinucleotide (NADH2) oxidase activity was demonstrated in extracts of both organisms. Although the NADH2 oxidase of S. faecium was sensitive to sulfhydryl inhibitors, the enzyme in S. faecalis was unaffected. The addition of ascorbate to the medium reversed the inhibitory effects of selenite and enhanced selenite reduction by S. faecium. Radioisotope studies, utilizing selenium75, demonstrated that selenite was taken up by both test organisms. The addition of ascorbate increased the rate and extent of selenium75 incorporation. It was concluded that the inhibitory effect of selenite and the inability of S. faecium to reduce the ion is a reflection of the oxidation by selenite of sulfhydryl groups on the active site.

Identification of an Active Site Residue of the R1 Subunit of Ribonucleotide Reductase fromEscherichia coli:  Characterization of Substrate-Induced Polypeptide Cleavage by C225SR1†

Biochemistry ◽  
1996 ◽  
Vol 35 (31) ◽  
pp. 10058-10067 ◽  
Author(s):  
Wilfred A. van der Donk ◽  
Chenhui Zeng ◽  
Klaus Biemann ◽  
JoAnne Stubbe ◽  
AnneMarie Hanlon ◽  
...  
Keyword(s):  
Ribonucleotide Reductase ◽  
Active Site ◽  
Active Site Residue ◽  
Fromescherichia Coli

Characterization of an Abnormal Antithrombin (Milano 2) with Defective Thrombin Binding

1986 ◽  
Vol 56 (03) ◽  
pp. 349-352 ◽  
Author(s):  
A Tripodi ◽  
A Krachmalnicoff ◽  
P M Mannucci
Keyword(s):  
Venous Thromboembolism ◽  
Active Site ◽  
Inhibitory Activity ◽  
Antithrombin Iii ◽  
Factor Xa ◽  
Molecular Defect ◽  
Affinity Adsorption ◽  
Italian Family ◽  
Crossed Immunoelectrophoresis

SummaryFour members of an Italian family (two with histories of venous thromboembolism) had a qualitative defect of antithrombin III reflected by normal antigen concentrations and halfnormal antithrombin activity with or without heparin. Anti-factor Xa activities were consistently borderline low (about 70% of normal). For the propositus’ plasma and serum the patterns of antithrombin III in crossed-immunoelectrophoresis with or without heparin were indistinguishable from those of normal plasma or serum. A normal affinity of antithrombin III for heparin was documented by heparin-sepharose chromatography. Affinity adsorption of the propositus’ plasma to human α-thrombin immobilized on sepharose beads revealed defective binding of the anti thrombin III to thrombin-sepharose. Hence the molecular defect of this variant appears to be at the active site responsible for binding and neutralizing thrombin, thus accounting for the low thrombin inhibitory activity.

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