PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
23098192-0	2012	Structural and kinetic effects on changes in the CO(2) binding pocket of human carbonic anhydrase II.	co(2)	49-54	carbonic anhydrase 2	Homo sapiens	79-100	
23098192-1	2012	This work examines the effect of perturbing the position of bound CO(2) in the active site of human carbonic anhydrase II (HCA II) on catalysis.	co(2)	66-71	carbonic anhydrase 2	Homo sapiens	100-121	
21377369-2	2011	The new enzyme, denominated lwCA, has a catalytic activity for the physiologic CO(2) hydration to bicarbonate reaction, similar to that of the high activity human isoform hCA II, with a k(cat) of 1.1x10(6) s(-1), and a k(cat)/K(m) of 1.4x10(8) M(-1) s(-1).	co(2)	79-84	carbonic anhydrase 2	Homo sapiens	171-177	
22270627-6	2011	Similarly, CO(2) hydration occurs with an efficiency within ~500-fold of CAII.	co(2)	11-16	carbonic anhydrase 2	Homo sapiens	73-77	
20578724-1	2010	The catalysis of CO(2) hydration by human carbonic anhydrase II (HCA II) is limited in maximal velocity by proton transfer from a zinc-bound water molecule to the proton shuttle His64.	co(2)	17-22	carbonic anhydrase 2	Homo sapiens	42-63	
18343915-6	2008	In a CO(2) hydration assay, 3 behaved as a very weak, partial inhibitor of CA-II and CA-I.	co(2)	5-10	carbonic anhydrase 2	Homo sapiens	75-80	
19583303-1	2009	Human carbonic anhydrase II (HCA II) is a monomeric zinc-containing metalloenzyme that catalyzes the hydration of CO(2) to form bicarbonate and a proton.	co(2)	114-119	carbonic anhydrase 2	Homo sapiens	6-27	
19879980-1	2010	The soluble enzyme carbonic anhydrase II (CAII) plays an important role in CO(2) influx and efflux by red blood cells (RBCs), a process initiated by changes in the extracellular [CO(2)] (CO(2)-initiated CO(2) transport).	co(2)	75-80	carbonic anhydrase 2	Homo sapiens	42-46	
19879980-1	2010	The soluble enzyme carbonic anhydrase II (CAII) plays an important role in CO(2) influx and efflux by red blood cells (RBCs), a process initiated by changes in the extracellular [CO(2)] (CO(2)-initiated CO(2) transport).	co(2)	179-184	carbonic anhydrase 2	Homo sapiens	42-46	
19879980-1	2010	The soluble enzyme carbonic anhydrase II (CAII) plays an important role in CO(2) influx and efflux by red blood cells (RBCs), a process initiated by changes in the extracellular [CO(2)] (CO(2)-initiated CO(2) transport).	co(2)	179-184	carbonic anhydrase 2	Homo sapiens	42-46	
19879980-1	2010	The soluble enzyme carbonic anhydrase II (CAII) plays an important role in CO(2) influx and efflux by red blood cells (RBCs), a process initiated by changes in the extracellular [CO(2)] (CO(2)-initiated CO(2) transport).	co(2)	179-184	carbonic anhydrase 2	Homo sapiens	42-46	
19879980-5	2010	In this review, I assess the theoretical roles of CAs in the transport of CO(2) and HCO(3)(-)-related species, concluding that although the effect of bound CAII on CO(2)-initiated CO(2) transport is expected to be substantial, the effect of bound CAs on HCO(3)(-)-initiated HCO(3)(-) transport is expected to be modest at best.	co(2)	74-79	carbonic anhydrase 2	Homo sapiens	156-160	
19879980-5	2010	In this review, I assess the theoretical roles of CAs in the transport of CO(2) and HCO(3)(-)-related species, concluding that although the effect of bound CAII on CO(2)-initiated CO(2) transport is expected to be substantial, the effect of bound CAs on HCO(3)(-)-initiated HCO(3)(-) transport is expected to be modest at best.	co(2)	164-169	carbonic anhydrase 2	Homo sapiens	156-160	
19879980-5	2010	In this review, I assess the theoretical roles of CAs in the transport of CO(2) and HCO(3)(-)-related species, concluding that although the effect of bound CAII on CO(2)-initiated CO(2) transport is expected to be substantial, the effect of bound CAs on HCO(3)(-)-initiated HCO(3)(-) transport is expected to be modest at best.	co(2)	164-169	carbonic anhydrase 2	Homo sapiens	156-160	
17353189-6	2007	Mass spectrometric analysis and the rate of cytosolic H(+) change following addition of CO(2)/HCO(3)(-) confirmed the catalytic activity of injected and expressed CAII in oocytes.	co(2)	88-93	carbonic anhydrase 2	Homo sapiens	163-167	
14736710-2	2004	Cytosolic enzyme carbonic anhydrase II (CAII) catalyzes the reaction CO(2) + H(2)O left arrow over right arrow HCO(3)(-) + H(+) in many tissues.	co(2)	69-74	carbonic anhydrase 2	Homo sapiens	17-38	
15807537-3	2005	Human carbonic anhydrase II (hCAII) is an enzyme that evolved to catalyze the reversible hydration of CO(2) and performs this task at a remarkable rate (k(cat) approximately 10(6) s(-)(1)).	co(2)	102-107	carbonic anhydrase 2	Homo sapiens	6-27	
15807537-3	2005	Human carbonic anhydrase II (hCAII) is an enzyme that evolved to catalyze the reversible hydration of CO(2) and performs this task at a remarkable rate (k(cat) approximately 10(6) s(-)(1)).	co(2)	102-107	carbonic anhydrase 2	Homo sapiens	29-34	
14736710-2	2004	Cytosolic enzyme carbonic anhydrase II (CAII) catalyzes the reaction CO(2) + H(2)O left arrow over right arrow HCO(3)(-) + H(+) in many tissues.	co(2)	69-74	carbonic anhydrase 2	Homo sapiens	40-44	
11863462-1	2002	The maximal velocity of catalysis of CO(2) hydration by human carbonic anhydrase II (HCA II) requires proton transfer from zinc-bound water to solution assisted by His 64.	co(2)	37-42	carbonic anhydrase 2	Homo sapiens	62-83	
15070393-2	2004	CAII, through the Zn(2+)-bound hydroxide, catalyzes the deceptively simple reaction: CO(2) + H(2)O <==> HCO(3)(-) + H(+).	co(2)	85-90	carbonic anhydrase 2	Homo sapiens	0-4	
11414818-1	2001	Catalysis of (18)O exchange between CO(2) and water catalyzed by a Co(II)-substituted mutant of human carbonic anhydrase II is analyzed to show the rate of release of H(2)(18)O from the active site.	co(2)	36-41	carbonic anhydrase 2	Homo sapiens	102-123	
11327835-1	2001	Histidine 64 in human carbonic anhydrase II (HCA II) functions in the catalytic pathway of CO(2) hydration as a shuttle to transfer protons between the zinc-bound water and bulk water.	co(2)	91-96	carbonic anhydrase 2	Homo sapiens	22-43