Transition-state analysis of nucleoside hydrolase from Crithidia fasciculata

Benjamin A. Horenstein; David W. Parkin; Bernardo Estupinan; Vern L. Schramm

doi:10.1021/bi00108a026

Transition-state analysis of nucleoside hydrolase from Crithidia fasciculata

Biochemistry ◽

10.1021/bi00108a026 ◽

1991 ◽

Vol 30 (44) ◽

pp. 10788-10795 ◽

Cited By ~ 83

Author(s):

Benjamin A. Horenstein ◽

David W. Parkin ◽

Bernardo Estupinan ◽

Vern L. Schramm

Keyword(s):

Transition State ◽

Crithidia Fasciculata ◽

Nucleoside Hydrolase ◽

State Analysis

Nucleoside hydrolase from Crithidia fasciculata. Metabolic role, purification, specificity, and kinetic mechanism.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(18)54759-1 ◽

1991 ◽

Vol 266 (31) ◽

pp. 20658-20665

Author(s):

D.W. Parkin ◽

B.A. Horenstein ◽

D.R. Abdulah ◽

B. Estupiñán ◽

V.L. Schramm

Keyword(s):

Kinetic Mechanism ◽

Crithidia Fasciculata ◽

Nucleoside Hydrolase ◽

Metabolic Role

Transition State Analysis of Thymidine Hydrolysis by Human Thymidine Phosphorylase

Journal of the American Chemical Society ◽

10.1021/ja105041j ◽

2010 ◽

Vol 132 (38) ◽

pp. 13425-13433 ◽

Cited By ~ 18

Author(s):

Phillip A. Schwartz ◽

Mathew J. Vetticatt ◽

Vern L. Schramm

Keyword(s):

Transition State ◽

Thymidine Phosphorylase ◽

State Analysis

Kinetic investigation of hydroxide ion attack at high spin Fe(II) bromosalicylidine chelates with amino acids in binary aqueous solvents: Initial and transition state analysis

Russian Journal of General Chemistry ◽

10.1134/s1070363213120499 ◽

2013 ◽

Vol 83 (12) ◽

pp. 2510-2518 ◽

Cited By ~ 5

Author(s):

Laila H. Abdel-Rahman ◽

Rafat M. El-Khatib ◽

Lobna A. E. Nassr ◽

Ahmed M. Abu-Dief

Keyword(s):

Amino Acids ◽

Transition State ◽

High Spin ◽

Kinetic Investigation ◽

Hydroxide Ion ◽

State Analysis

A new class of C-nucleoside analogues. 1-(S)-aryl-1,4-dideoxy-1,4-imino-D-ribitols, transition state analogue inhibitors of nucleoside hydrolase

Tetrahedron Letters ◽

10.1016/s0040-4039(00)79290-2 ◽

1993 ◽

Vol 34 (45) ◽

pp. 7213-7216 ◽

Cited By ~ 51

Author(s):

Benjamin A. Horenstein ◽

Roger F. Zabinski ◽

Vern L. Schramm

Keyword(s):

Transition State ◽

Nucleoside Analogues ◽

New Class ◽

Nucleoside Hydrolase ◽

Transition State Analogue ◽

Transition State Analogue Inhibitors

Transient [3,3] Cope rearrangement of 3,3-dicyano-1,5-dienes: computational analysis and 2-step synthesis of arylcycloheptanes

Chemical Science ◽

10.1039/c8sc03057j ◽

2018 ◽

Vol 9 (46) ◽

pp. 8760-8764 ◽

Cited By ~ 8

Author(s):

Ehsan Fereyduni ◽

Jacob N. Sanders ◽

Gabriel Gonzalez ◽

K. N. Houk ◽

Alexander J. Grenning

Keyword(s):

Transition State ◽

Computational Analysis ◽

Cope Rearrangement ◽

State Analysis

Unexpectedly mild [3,3] rearrangement computed transition state analysis, regio- and diastereoselecitve transformations multicomponent couplings, convergent 2-step arylcycloheptene synthesis.

Transition State Analysis Using Multiple Kinetic Isotope Effects: Mechanisms of Enzymatic and Non-enzymatic Glycoside Hydrolysis and Transfer

Advances in Physical Organic Chemistry ◽

10.1016/s0065-3160(02)37004-7 ◽

2002 ◽

pp. 239-314 ◽

Cited By ~ 34

Author(s):

Paul J. Berti ◽

Kelly S.E. Tanaka

Keyword(s):

Transition State ◽

Isotope Effects ◽

Kinetic Isotope Effects ◽

Kinetic Isotope ◽

Glycoside Hydrolysis ◽

State Analysis

Purine nucleoside phosphorylase. Catalytic mechanism and transition-state analysis of the arsenolysis reaction

Biochemistry ◽

10.1021/bi00211a033 ◽

1993 ◽

Vol 32 (48) ◽

pp. 13212-13219 ◽

Cited By ~ 112

Author(s):

Paul C. Kline ◽

Vern L. Schramm

Keyword(s):

Transition State ◽

Purine Nucleoside Phosphorylase ◽

Catalytic Mechanism ◽

Purine Nucleoside ◽

Nucleoside Phosphorylase ◽

State Analysis

[13] Enzymatic transition-state analysis and transition-state analogs

Methods in Enzymology - Enzyme kinetics and mechanism Part E: Energetics of Enzyme Catalysis ◽

10.1016/s0076-6879(99)08015-5 ◽

1999 ◽

pp. 301-355 ◽

Cited By ~ 53

Author(s):

Vern L. Schramm

Keyword(s):

Transition State ◽

Transition State Analogs ◽

State Analysis

Hydrophobicity, reactivity trends of base catalyzed hydrolysis of some novel high spin Fe(II) Schiff base amino acid chelates in some binary aqueous solvent mixtures: Initial-transition state analysis

Journal of Saudi Chemical Society ◽

10.1016/j.jscs.2013.11.004 ◽

2017 ◽

Vol 21 ◽

pp. S128-S135 ◽

Cited By ~ 1

Author(s):

Laila H. Abdel-Rahman ◽

Rafat M. El-Khatib ◽

Lobna A.E. Nassr ◽

Ahmed M. Abu-Dief

Keyword(s):

Schiff Base ◽

Amino Acid ◽

Transition State ◽

High Spin ◽

Solvent Mixtures ◽

Aqueous Solvent Mixtures ◽

Aqueous Solvent ◽

Hydrolysis Of ◽

State Analysis

Binding modes for substrate and a proposed transition-state analog of protozoan nucleoside hydrolase

Biochemistry ◽

10.1021/bi00042a030 ◽

1995 ◽

Vol 34 (42) ◽

pp. 13961-13966 ◽

Cited By ~ 23

Author(s):

David W. Parkin ◽

Vern L. Schramm

Keyword(s):

Transition State ◽

Binding Modes ◽

Transition State Analog ◽

Nucleoside Hydrolase