Intramolecular Inhibition by Enzyme of Site-Specific Modification Reactions can Mask pKa Values Characteristic of the Reaction Pathway: Do the Side Chains of Aspartic Acid-158 and Lysine-156 of Papain Form an Ion-Pair?

1978 ◽  
Vol 6 (1) ◽  
pp. 250-252 ◽  
Author(s):  
J. PAUL G. MALTHOUSE ◽  
KEITH BROCKLEHURST
Keyword(s):  
Aspartic Acid ◽  
Reaction Pathway ◽  
Ion Pair ◽  
Side Chains ◽  
Site Specific ◽  
Pka Values ◽  
Specific Modification

Site-specific modification of E. coli DNA polymerase I large fragment with pyridoxal 5'-phosphate

Biochemistry ◽  
1984 ◽  
Vol 23 (9) ◽  
pp. 2073-2078 ◽  
Author(s):  
Anup K. Hazra ◽  
Sevilla Detera-Wadleigh ◽  
Samuel H. Wilson
Keyword(s):  
Dna Polymerase ◽  
Large Fragment ◽  
Dna Polymerase I ◽  
Site Specific ◽  
E Coli ◽  
Specific Modification ◽  
Polymerase I

scholarly journals Studies on the role of actin's aspartic acid 3 and aspartic acid 11 using oligodeoxynucleotide-directed site-specific mutagenesis.

1988 ◽  
Vol 263 (36) ◽  
pp. 19662-19669
Author(s):  
T L Solomon ◽  
L R Solomon ◽  
L S Gay ◽  
P A Rubenstein
Keyword(s):  
Aspartic Acid ◽  
Site Specific

scholarly journals Dual, Site-Specific Modification of Antibodies by Using Solid-Phase Immobilized Microbial Transglutaminase

ChemBioChem ◽  
2017 ◽  
Vol 18 (19) ◽  
pp. 1923-1927 ◽  
Author(s):  
Philipp R. Spycher ◽  
Christian A. Amann ◽  
Jöri E. Wehrmüller ◽  
David R. Hurwitz ◽  
Olivier Kreis ◽  
...  
Keyword(s):  
Solid Phase ◽  
Microbial Transglutaminase ◽  
Site Specific ◽  
Specific Modification ◽  
Dual Site

scholarly journals Expression of ΔF508 CFTR in normal mouse lung after site-specific modification of CFTR sequences by SFHR

Gene Therapy ◽  
2001 ◽  
Vol 8 (12) ◽  
pp. 961-965 ◽  
Author(s):  
KK Goncz ◽  
A Colosimo ◽  
B Dallapiccola ◽  
L Gagné ◽  
K Hong ◽  
...  
Keyword(s):  
Normal Mouse ◽  
Mouse Lung ◽  
Site Specific ◽  
Specific Modification ◽  
Δf508 Cftr

Methyl acetyl phosphate: A novel acetylating agent Its site-specific modification of human hemoglobin A

1986 ◽  
Vol 359 ◽  
pp. 193-201 ◽  
Author(s):  
Hiroshi Ueno ◽  
Maria A. Pospischil ◽  
Ronald Kluger ◽  
James M. Manning
Keyword(s):  
Human Hemoglobin ◽  
Acetyl Phosphate ◽  
Site Specific ◽  
Specific Modification ◽  
Hemoglobin A

scholarly journals Site-specific modification of the lactose operator with acetylaminofluorene

1983 ◽  
Vol 11 (15) ◽  
pp. 5093-5102 ◽  
Author(s):  
Gerhard Stöhrer ◽  
Judith A. Osband ◽  
Gabriel Alvarado-Urbina
Keyword(s):  
Site Specific ◽  
Specific Modification

scholarly journals Site specific modification of the human plasma proteome by methylglyoxal

2015 ◽  
Vol 289 (2) ◽  
pp. 155-162 ◽  
Author(s):  
Michael J. Kimzey ◽  
Owen R. Kinsky ◽  
Hussein N. Yassine ◽  
George Tsaprailis ◽  
Craig S. Stump ◽  
...  
Keyword(s):  
Human Plasma ◽  
Plasma Proteome ◽  
Site Specific ◽  
Specific Modification ◽  
Human Plasma Proteome

Characterization of Holliday structures in FLP protein-promoted site-specific recombination

1990 ◽  
Vol 10 (1) ◽  
pp. 235-242
Author(s):  
L Meyer-Leon ◽  
R B Inman ◽  
M M Cox
Keyword(s):  
Reaction Rate ◽  
Reaction Pathway ◽  
Reaction Intermediates ◽  
Wild Type ◽  
Site Specific ◽  
Site Specific Recombination ◽  
Isomerization Process ◽  
Previous Demonstration ◽  
Rate Limiting

Holliday structures are formed in the course of FLP protein-promoted site-specific recombination. Here, we demonstrate that Holliday structures are formed in reactions involving wild-type substrates and that they are kinetically competent with respect to the overall reaction rate. Together with a previous demonstration of chemical competence (L. Meyer-Leon, L.-C. Huang, S. W. Umlauf, M. M. Cox, and R. B. Inman, Mol. Cell. Biol. 8:3784-3796, 1988), Holliday structures therefore meet all criteria necessary to establish that they are obligate reaction intermediates in FLP-mediated site-specific recombination. In addition, kinetic evidence suggests that two distinct forms of the Holliday intermediate are present in the reaction pathway, interconverted in an isomerization process that is rate limiting at 0 degree C.

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