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

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.

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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