The Carbon Dioxide Hydration Activity of Carbonic Anhydrase I. STOP-FLOW KINETIC STUDIES ON THE NATIVE HUMAN ISOENZYMES B AND C
TLDR
The present kinetic results are interpreted as representing a great specificity of carbonic anhydrase for the binding of its substrate CO2, and it is proposed that the enzyme-catalyzed hydration of CO2 requires, not only water activation by a basic group, but also charge neutralization in the transition state by an electron acceptor function.About:
This article is published in Journal of Biological Chemistry.The article was published on 1971-04-25 and is currently open access. It has received 1654 citations till now. The article focuses on the topics: Carbonic anhydrase II & Carbonic Anhydrase I.read more
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PatentDOI
Carbonic anhydrase inhibitors
Peter Ebbesen,Claudlu T. Supuran,Andrea Scozzafava,Erik Olai Pettersen,Kaye Williams,L.J. Dubois,Philippe Lambin +6 more
TL;DR: A carbonic anhydrase IX (CA IX) inhibitor is a compound of general formula: R-NH-CX-NH-(CH 2 ) n -Ar-Q-SO 2 -NH 2 or a pharmaceutically acceptable salt, derivative or prodrug thereof.
Journal ArticleDOI
Structure and mechanism of carbonic anhydrase.
TL;DR: Carbonic anhydrase (CA; carbonate hydro-lyase, EC 4.2.1.1) is a zinc-containing enzyme that catalyzes the reversible hydration of carbon dioxide: CO2+ H2O<-->HCO3(-)+H+.
Journal ArticleDOI
The 'evolvability' of promiscuous protein functions.
Amir Aharoni,Leonid Gaidukov,Olga Khersonsky,Stephen McQ Gould,Cintia Roodveldt,Dan S. Tawfik +5 more
TL;DR: Results from directed laboratory evolution experiments indicate that the evolution of a new function is driven by mutations that have little effect on the native function but large effects on the promiscuous functions that serve as starting point.
Journal ArticleDOI
The catalytic mechanism of carbonic anhydrase: implications of a rate-limiting protolysis of water
David N. Silverman,Sven Lindskog +1 more
Journal ArticleDOI
Voltage-Gated Proton Channels and Other Proton Transfer Pathways
TL;DR: Voltage-gated proton channels represent a specific subset of proton channel that have voltage- and time-dependent gating like other ion channels, but differ from most ion channels in their extraordinarily high selectivity, tiny conductance, strong temperature and deuterium isotope effects on conductance and gating kinetics, and insensitivity to block by steric occlusion.
References
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Book
The solubility of non-electrolytes
TL;DR: Hildebrand's book is an exception as mentioned in this paper, since the reviewer has taken the opportunity to renew his acquaintance with the earlier as well as the later text, and has found this to be a most interesting experience, since the book is full of matter which is not dealt with adequately in the ordinary text-books of physical chemistry.
Journal ArticleDOI
A comparison of estimates of michaelis-menten kinetic constants from various linear transformations.
John E. Dowd,Douglas S. Riggs +1 more
TL;DR: The parameters which characterize this equation, and which must ordinarily be estimated from the observed data, are v,,,, the maximum initial velocity which is theoretically attained when the enzyme has been “saturated” by an infinite concentration of substrate, and K,, the Michaelis constant which is numerically equal to the concentration of substrates for half-maximal initial velocity.
Journal ArticleDOI
Esterase Activities of Human Carbonic Anhydrases B and C
TL;DR: The data gave no evidence for the presence of an acyl intermediate; if such an intermediate exists it must be very rapidly hydrolyzed, and the pH dependence curves appear to reflect the catalytic center activity.
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