Journal of the American Chemical Society, volume 128, issue 4, pages 1293-1303
Alkaline Phosphatase Mono- and Diesterase Reactions: Comparative Transition State Analysis
Publication type: Journal Article
Publication date: 2006-01-06
Quartile SCImago
Q1
Quartile WOS
Q1
Impact factor: 15
ISSN: 00027863, 15205126
General Chemistry
Catalysis
Biochemistry
Colloid and Surface Chemistry
Abstract
Enzyme-catalyzed phosphoryl transfer reactions have frequently been suggested to proceed through transition states that are altered from their solution counterparts. Previous work with Escherichia coli alkaline phosphatase (AP), however, suggests that this enzyme catalyzes the hydrolysis of phosphate monoesters through a loose, dissociative transition state, similar to that in solution. AP also exhibits catalytic promiscuity, with a low level of phosphodiesterase activity, despite the tighter, more associative transition state for phosphate diester hydrolysis in solution. Because AP is evolutionarily optimized for phosphate monoester hydrolysis, it is possible that the active site environment alters the transition state for diester hydrolysis to be looser in its bonding to the incoming and outgoing groups. To test this possibility, we have measured the nonenzymatic and AP-catalyzed rate of reaction for a series of substituted methyl phenyl phosphate diesters. The values of beta(lg) and additional data suggest that the transition state for AP-catalyzed phosphate diester hydrolysis is indistinguishable from that in solution. Instead of altering transition state structure, AP catalyzes phosphoryl transfer reactions by recognizing and stabilizing transition states similar to those in aqueous solution. The AP active site therefore has the ability to recognize different transition states, a property that could assist in the evolutionary optimization of promiscuous activities.
Top-30
Citations by journals
|
2
4
6
8
10
12
14
16
18
|
|
|
Biochemistry
17 publications, 12.32%
|
|
|
Journal of the American Chemical Society
16 publications, 11.59%
|
|
|
Journal of Physical Chemistry B
7 publications, 5.07%
|
|
|
Chemistry - A European Journal
6 publications, 4.35%
|
|
|
Journal of Organic Chemistry
6 publications, 4.35%
|
|
|
Inorganic Chemistry
5 publications, 3.62%
|
|
|
ChemPhysChem
4 publications, 2.9%
|
|
|
Theoretical Chemistry Accounts
3 publications, 2.17%
|
|
|
Organic and Biomolecular Chemistry
3 publications, 2.17%
|
|
|
Molecules
2 publications, 1.45%
|
|
|
Bulletin of the Korean Chemical Society
2 publications, 1.45%
|
|
|
Journal of Biological Chemistry
2 publications, 1.45%
|
|
|
Current Opinion in Structural Biology
2 publications, 1.45%
|
|
|
Journal of Computational Chemistry
2 publications, 1.45%
|
|
|
International Journal of Chemical Kinetics
2 publications, 1.45%
|
|
|
Journal of Chemical Theory and Computation
2 publications, 1.45%
|
|
|
Annual Reports Section B (Organic Chemistry)
2 publications, 1.45%
|
|
|
Physical Chemistry Chemical Physics
2 publications, 1.45%
|
|
|
RSC Advances
2 publications, 1.45%
|
|
|
Methods in Enzymology
2 publications, 1.45%
|
|
|
Pure and Applied Chemistry
2 publications, 1.45%
|
|
|
Proceedings of the National Academy of Sciences of the United States of America
2 publications, 1.45%
|
|
|
F1000Research
1 publication, 0.72%
|
|
|
Biochemical Journal
1 publication, 0.72%
|
|
|
European Journal of Medicinal Chemistry
1 publication, 0.72%
|
|
|
PLoS ONE
1 publication, 0.72%
|
|
|
PLoS Computational Biology
1 publication, 0.72%
|
|
|
Polyhedron
1 publication, 0.72%
|
|
|
Current Opinion in Chemical Biology
1 publication, 0.72%
|
|
|
2
4
6
8
10
12
14
16
18
|
Citations by publishers
|
10
20
30
40
50
60
|
|
|
American Chemical Society (ACS)
56 publications, 40.58%
|
|
|
Wiley
25 publications, 18.12%
|
|
|
Elsevier
15 publications, 10.87%
|
|
|
Royal Society of Chemistry (RSC)
15 publications, 10.87%
|
|
|
Springer Nature
3 publications, 2.17%
|
|
|
Multidisciplinary Digital Publishing Institute (MDPI)
2 publications, 1.45%
|
|
|
Public Library of Science (PLoS)
2 publications, 1.45%
|
|
|
American Society for Biochemistry and Molecular Biology
2 publications, 1.45%
|
|
|
Walter de Gruyter
2 publications, 1.45%
|
|
|
Proceedings of the National Academy of Sciences (PNAS)
2 publications, 1.45%
|
|
|
F1000 Research
1 publication, 0.72%
|
|
|
Portland Press
1 publication, 0.72%
|
|
|
Frontiers Media S.A.
1 publication, 0.72%
|
|
|
Taylor & Francis
1 publication, 0.72%
|
|
|
Oxford University Press
1 publication, 0.72%
|
|
|
Cambridge University Press
1 publication, 0.72%
|
|
|
10
20
30
40
50
60
|
- We do not take into account publications without a DOI.
- Statistics recalculated only for publications connected to researchers, organizations and labs registered on the platform.
- Statistics recalculated weekly.
{"yearsCitations":{"type":"bar","data":{"show":true,"labels":[2006,2007,2008,2009,2010,2011,2012,2013,2014,2015,2016,2017,2018,2019,2020,2021,2022,2023,2024],"ids":[0,0,0,0,0,0,0,0,0,0,0,0,0,0,0,0,0,0,0],"codes":[0,0,0,0,0,0,0,0,0,0,0,0,0,0,0,0,0,0,0],"imageUrls":["","","","","","","","","","","","","","","","","","",""],"datasets":[{"label":"Citations number","data":[3,10,13,11,10,9,8,9,6,9,12,7,11,2,4,4,3,4,3],"backgroundColor":["#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6"],"percentage":["2.17","7.25","9.42","7.97","7.25","6.52","5.8","6.52","4.35","6.52","8.7","5.07","7.97","1.45","2.9","2.9","2.17","2.9","2.17"],"barThickness":null}]},"options":{"indexAxis":"x","maintainAspectRatio":true,"scales":{"y":{"ticks":{"precision":0,"autoSkip":false,"font":{"family":"Montserrat"},"color":"#000000"},"stacked":false},"x":{"ticks":{"stepSize":1,"precision":0,"font":{"family":"Montserrat"},"color":"#000000"},"stacked":false}},"plugins":{"legend":{"position":"top","labels":{"font":{"family":"Montserrat"},"color":"#000000"}},"title":{"display":true,"text":"Citations per year","font":{"size":24,"family":"Montserrat","weight":600},"color":"#000000"}}}},"journals":{"type":"bar","data":{"show":true,"labels":["Biochemistry","Journal of the American Chemical Society","Journal of Physical Chemistry B","Chemistry - A European Journal","Journal of Organic Chemistry","Inorganic Chemistry","ChemPhysChem","Theoretical Chemistry Accounts","Organic and Biomolecular Chemistry","Molecules","Bulletin of the Korean Chemical Society","Journal of Biological Chemistry","Current Opinion in Structural Biology","Journal of Computational Chemistry","International Journal of Chemical Kinetics","Journal of Chemical Theory and Computation","Annual Reports Section B (Organic Chemistry)","Physical Chemistry Chemical Physics","RSC Advances","Methods in Enzymology","Pure and Applied Chemistry","Proceedings of the National Academy of Sciences of the United States of America","F1000Research","Biochemical Journal","European Journal of Medicinal Chemistry","PLoS ONE","PLoS Computational Biology","Polyhedron","Current Opinion in Chemical Biology"],"ids":[9964,4813,14990,24708,8697,24714,16306,19212,541,1770,7473,19451,13702,423,9472,58,25522,1773,3100,24566,11456,306,24267,15459,8171,24963,23198,21269,5052],"codes":[0,0,0,0,0,0,0,0,0,0,0,0,0,0,0,0,0,0,0,0,0,0,0,0,0,0,0,0,0],"imageUrls":["\/storage\/images\/resized\/iLiQsFqFaSEx6chlGQ5fbAwF6VYU3WWa08hkss0g_medium.webp","\/storage\/images\/resized\/iLiQsFqFaSEx6chlGQ5fbAwF6VYU3WWa08hkss0g_medium.webp","\/storage\/images\/resized\/iLiQsFqFaSEx6chlGQ5fbAwF6VYU3WWa08hkss0g_medium.webp","\/storage\/images\/resized\/bRyGpdm98BkAUYiK1YFNpl5Z7hPu6Gd87gbIeuG3_medium.webp","\/storage\/images\/resized\/iLiQsFqFaSEx6chlGQ5fbAwF6VYU3WWa08hkss0g_medium.webp","\/storage\/images\/resized\/iLiQsFqFaSEx6chlGQ5fbAwF6VYU3WWa08hkss0g_medium.webp","\/storage\/images\/resized\/bRyGpdm98BkAUYiK1YFNpl5Z7hPu6Gd87gbIeuG3_medium.webp","\/storage\/images\/resized\/voXLqlsvTwv5p3iMQ8Dhs95nqB4AXOG7Taj7G4ra_medium.webp","\/storage\/images\/resized\/leiAYcRDGTSl5B1eCnwpSGqmDEUEfDPPoYisFGhT_medium.webp","\/storage\/images\/resized\/MjH1ITP7lMYGxeqUZfkt2BnVLgjkk413jwBV97XX_medium.webp","\/storage\/images\/resized\/bRyGpdm98BkAUYiK1YFNpl5Z7hPu6Gd87gbIeuG3_medium.webp","\/storage\/images\/resized\/OuA6WPZekwEiUM99mP2pSqj4yHPxHezM6xgLhAjO_medium.webp","\/storage\/images\/resized\/GDnYOu1UpMMfMMRV6Aqle4H0YLLsraeD9IP9qScG_medium.webp","\/storage\/images\/resized\/bRyGpdm98BkAUYiK1YFNpl5Z7hPu6Gd87gbIeuG3_medium.webp","\/storage\/images\/resized\/bRyGpdm98BkAUYiK1YFNpl5Z7hPu6Gd87gbIeuG3_medium.webp","\/storage\/images\/resized\/iLiQsFqFaSEx6chlGQ5fbAwF6VYU3WWa08hkss0g_medium.webp","\/storage\/images\/resized\/leiAYcRDGTSl5B1eCnwpSGqmDEUEfDPPoYisFGhT_medium.webp","\/storage\/images\/resized\/leiAYcRDGTSl5B1eCnwpSGqmDEUEfDPPoYisFGhT_medium.webp","\/storage\/images\/resized\/leiAYcRDGTSl5B1eCnwpSGqmDEUEfDPPoYisFGhT_medium.webp","\/storage\/images\/resized\/GDnYOu1UpMMfMMRV6Aqle4H0YLLsraeD9IP9qScG_medium.webp","\/storage\/images\/resized\/3SpVxcYL33bOvPq4sHxJLH2NeKNeDloahSUpNiO4_medium.webp","\/storage\/images\/resized\/mxFdPe9qujsfvfYfcN0QOclAiYORFb0xrRlwV8gs_medium.webp","\/storage\/images\/resized\/WEXVM2IukNfkmwoqmPhtMKmAeERljKWAbbXmEX7m_medium.webp","\/storage\/images\/resized\/nUqNrP9GnM1t0BrAIXp1LBodjU8aIJ2Fk4pLfGhZ_medium.webp","\/storage\/images\/resized\/GDnYOu1UpMMfMMRV6Aqle4H0YLLsraeD9IP9qScG_medium.webp","\/storage\/images\/resized\/PRGhlgB4OKRltSNtT39eA6wlnOTGRap1QQ6FQHih_medium.webp","\/storage\/images\/resized\/PRGhlgB4OKRltSNtT39eA6wlnOTGRap1QQ6FQHih_medium.webp","\/storage\/images\/resized\/GDnYOu1UpMMfMMRV6Aqle4H0YLLsraeD9IP9qScG_medium.webp","\/storage\/images\/resized\/GDnYOu1UpMMfMMRV6Aqle4H0YLLsraeD9IP9qScG_medium.webp"],"datasets":[{"label":"","data":[17,16,7,6,6,5,4,3,3,2,2,2,2,2,2,2,2,2,2,2,2,2,1,1,1,1,1,1,1],"backgroundColor":["#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6"],"percentage":[12.32,11.59,5.07,4.35,4.35,3.62,2.9,2.17,2.17,1.45,1.45,1.45,1.45,1.45,1.45,1.45,1.45,1.45,1.45,1.45,1.45,1.45,0.72,0.72,0.72,0.72,0.72,0.72,0.72],"barThickness":13}]},"options":{"indexAxis":"y","maintainAspectRatio":false,"scales":{"y":{"ticks":{"precision":0,"autoSkip":false,"font":{"family":"Montserrat"},"color":"#000000"},"stacked":false},"x":{"ticks":{"stepSize":null,"precision":0,"font":{"family":"Montserrat"},"color":"#000000"},"stacked":false}},"plugins":{"legend":{"position":"top","labels":{"font":{"family":"Montserrat"},"color":"#000000"}},"title":{"display":true,"text":"Journals","font":{"size":24,"family":"Montserrat","weight":600},"color":"#000000"}}}},"publishers":{"type":"bar","data":{"show":true,"labels":["American Chemical Society (ACS)","Wiley","Elsevier","Royal Society of Chemistry (RSC)","Springer Nature","Multidisciplinary Digital Publishing Institute (MDPI)","Public Library of Science (PLoS)","American Society for Biochemistry and Molecular Biology","Walter de Gruyter","Proceedings of the National Academy of Sciences (PNAS)","F1000 Research","Portland Press","Frontiers Media S.A.","Taylor & Francis","Oxford University Press","Cambridge University Press"],"ids":[40,11,17,123,8,202,344,2090,4,162,7910,801,208,18,19,1],"codes":[0,0,0,0,0,0,0,0,0,0,0,0,0,0,0,0],"imageUrls":["\/storage\/images\/resized\/iLiQsFqFaSEx6chlGQ5fbAwF6VYU3WWa08hkss0g_medium.webp","\/storage\/images\/resized\/bRyGpdm98BkAUYiK1YFNpl5Z7hPu6Gd87gbIeuG3_medium.webp","\/storage\/images\/resized\/GDnYOu1UpMMfMMRV6Aqle4H0YLLsraeD9IP9qScG_medium.webp","\/storage\/images\/resized\/leiAYcRDGTSl5B1eCnwpSGqmDEUEfDPPoYisFGhT_medium.webp","\/storage\/images\/resized\/voXLqlsvTwv5p3iMQ8Dhs95nqB4AXOG7Taj7G4ra_medium.webp","\/storage\/images\/resized\/MjH1ITP7lMYGxeqUZfkt2BnVLgjkk413jwBV97XX_medium.webp","\/storage\/images\/resized\/PRGhlgB4OKRltSNtT39eA6wlnOTGRap1QQ6FQHih_medium.webp","\/storage\/images\/resized\/OuA6WPZekwEiUM99mP2pSqj4yHPxHezM6xgLhAjO_medium.webp","\/storage\/images\/resized\/3SpVxcYL33bOvPq4sHxJLH2NeKNeDloahSUpNiO4_medium.webp","\/storage\/images\/resized\/mxFdPe9qujsfvfYfcN0QOclAiYORFb0xrRlwV8gs_medium.webp","\/storage\/images\/resized\/WEXVM2IukNfkmwoqmPhtMKmAeERljKWAbbXmEX7m_medium.webp","\/storage\/images\/resized\/nUqNrP9GnM1t0BrAIXp1LBodjU8aIJ2Fk4pLfGhZ_medium.webp","\/storage\/images\/resized\/4QWA67eqfcfyOiA8Wk7YnqroHFqQbTsmDJUYTCTg_medium.webp","\/storage\/images\/resized\/5YZtvLvkPZuc2JHOaZsjCvGSHFCuC3drUwN3YAc5_medium.webp","\/storage\/images\/resized\/yNSijlgQghQF53VZuyFLA30CKDe4j3HK74Vtpnxa_medium.webp","\/storage\/images\/resized\/cF81zWlLdkmYekymGuDcSdvgBGNKaIDoMoeJtHS1_medium.webp"],"datasets":[{"label":"","data":[56,25,15,15,3,2,2,2,2,2,1,1,1,1,1,1],"backgroundColor":["#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6"],"percentage":[40.58,18.12,10.87,10.87,2.17,1.45,1.45,1.45,1.45,1.45,0.72,0.72,0.72,0.72,0.72,0.72],"barThickness":13}]},"options":{"indexAxis":"y","maintainAspectRatio":false,"scales":{"y":{"ticks":{"precision":0,"autoSkip":false,"font":{"family":"Montserrat"},"color":"#000000"},"stacked":false},"x":{"ticks":{"stepSize":null,"precision":0,"font":{"family":"Montserrat"},"color":"#000000"},"stacked":false}},"plugins":{"legend":{"position":"top","labels":{"font":{"family":"Montserrat"},"color":"#000000"}},"title":{"display":true,"text":"Publishers","font":{"size":24,"family":"Montserrat","weight":600},"color":"#000000"}}}},"yearsCitationsQuartiles":{"type":"bar","data":{"show":true,"labels":[2006,2007,2008,2009,2010,2011,2012,2013,2014,2015,2016,2017,2018,2019,2020,2021,2022,2023,2024],"ids":[],"codes":[],"imageUrls":[],"datasets":[{"label":"Q4","backgroundColor":"rgb(221,90,78)","data":[0,0,0,0,0,0,0,0,0,0,0,0,0,0,0,0,0,0,0],"percentage":["0","0","0","0","0","0","0","0","0","0","0","0","0","0","0","0","0","0","0"]},{"label":"Q3","backgroundColor":"rgb(251, 163,83)","data":[0,1,1,0,0,1,0,2,0,0,2,0,1,0,1,0,0,0,0],"percentage":["0","0.72","0.72","0","0","0.72","0","1.45","0","0","1.45","0","0.72","0","0.72","0","0","0","0"]},{"label":"Q2","backgroundColor":"rgb(232, 213, 89)","data":[0,0,0,2,0,0,1,0,1,3,1,2,0,0,0,0,0,0,2],"percentage":["0","0","0","1.45","0","0","0.72","0","0.72","2.17","0.72","1.45","0","0","0","0","0","0","1.45"]},{"label":"Q1","backgroundColor":"rgb(164, 207, 99)","data":[3,7,10,6,8,7,7,7,5,6,8,4,8,2,3,3,3,3,1],"percentage":["2.17","5.07","7.25","4.35","5.8","5.07","5.07","5.07","3.62","4.35","5.8","2.9","5.8","1.45","2.17","2.17","2.17","2.17","0.72"]},{"label":"Quartile not defined","backgroundColor":"#E5E7EB","data":[0,2,2,3,2,1,0,0,0,0,1,1,2,0,0,1,0,1,0],"percentage":["0","1.45","1.45","2.17","1.45","0.72","0","0","0","0","0.72","0.72","1.45","0","0","0.72","0","0.72","0"]}]},"options":{"indexAxis":"x","maintainAspectRatio":true,"scales":{"y":{"ticks":{"precision":0,"autoSkip":false,"font":{"family":"Montserrat"},"color":"#000000"},"stacked":true},"x":{"ticks":{"stepSize":1,"precision":0,"font":{"family":"Montserrat"},"color":"#000000"},"stacked":true}},"plugins":{"legend":{"position":"top","labels":{"font":{"family":"Montserrat"},"color":"#000000"}},"title":{"display":true,"text":"Citations quartiles by SCImago per year","font":{"size":24,"family":"Montserrat","weight":600},"color":"#000000"}}}},"yearsCitationsQuartilesWs":{"type":"bar","data":{"show":true,"labels":[2006,2007,2008,2009,2010,2011,2012,2013,2014,2015,2016,2017,2018,2019,2020,2021,2022,2023,2024],"ids":[],"codes":[],"imageUrls":[],"datasets":[{"label":"Q4","backgroundColor":"rgb(221,90,78)","data":[0,1,0,0,0,1,0,1,0,0,2,0,1,0,1,0,0,0,0],"percentage":["0","0.72","0","0","0","0.72","0","0.72","0","0","1.45","0","0.72","0","0.72","0","0","0","0"]},{"label":"Q3","backgroundColor":"rgb(251, 163,83)","data":[2,1,4,3,2,1,1,1,3,2,3,3,1,2,2,1,0,0,1],"percentage":["1.45","0.72","2.9","2.17","1.45","0.72","0.72","0.72","2.17","1.45","2.17","2.17","0.72","1.45","1.45","0.72","0","0","0.72"]},{"label":"Q2","backgroundColor":"rgb(232, 213, 89)","data":[0,4,0,1,2,2,4,3,1,5,2,2,1,0,0,1,1,2,2],"percentage":["0","2.9","0","0.72","1.45","1.45","2.9","2.17","0.72","3.62","1.45","1.45","0.72","0","0","0.72","0.72","1.45","1.45"]},{"label":"Q1","backgroundColor":"rgb(164, 207, 99)","data":[1,2,7,3,4,4,3,4,1,2,4,1,6,0,1,1,2,1,0],"percentage":["0.72","1.45","5.07","2.17","2.9","2.9","2.17","2.9","0.72","1.45","2.9","0.72","4.35","0","0.72","0.72","1.45","0.72","0"]},{"label":"Quartile not defined","backgroundColor":"#E5E7EB","data":[0,2,2,4,2,1,0,0,1,0,1,1,2,0,0,1,0,1,0],"percentage":["0","1.45","1.45","2.9","1.45","0.72","0","0","0.72","0","0.72","0.72","1.45","0","0","0.72","0","0.72","0"]}]},"options":{"indexAxis":"x","maintainAspectRatio":true,"scales":{"y":{"ticks":{"precision":0,"autoSkip":false,"font":{"family":"Montserrat"},"color":"#000000"},"stacked":true},"x":{"ticks":{"stepSize":1,"precision":0,"font":{"family":"Montserrat"},"color":"#000000"},"stacked":true}},"plugins":{"legend":{"position":"top","labels":{"font":{"family":"Montserrat"},"color":"#000000"}},"title":{"display":true,"text":"Citations quartiles by WoS per year","font":{"size":24,"family":"Montserrat","weight":600},"color":"#000000"}}}}}
Are you a researcher?
Create a profile to get free access to personal recommendations for colleagues and new articles.
Metrics
Cite this
GOST |
RIS |
BibTex |
MLA
Cite this
GOST
Copy
Zalatan J. G., Herschlag D. Alkaline Phosphatase Mono- and Diesterase Reactions: Comparative Transition State Analysis // Journal of the American Chemical Society. 2006. Vol. 128. No. 4. pp. 1293-1303.
GOST all authors (up to 50)
Copy
Zalatan J. G., Herschlag D. Alkaline Phosphatase Mono- and Diesterase Reactions: Comparative Transition State Analysis // Journal of the American Chemical Society. 2006. Vol. 128. No. 4. pp. 1293-1303.
Cite this
RIS
Copy
TY - JOUR
DO - 10.1021/ja056528r
UR - https://doi.org/10.1021/ja056528r
TI - Alkaline Phosphatase Mono- and Diesterase Reactions: Comparative Transition State Analysis
T2 - Journal of the American Chemical Society
AU - Zalatan, Jesse G
AU - Herschlag, Daniel
PY - 2006
DA - 2006/01/06 00:00:00
PB - American Chemical Society (ACS)
SP - 1293-1303
IS - 4
VL - 128
SN - 0002-7863
SN - 1520-5126
ER -
Cite this
BibTex
Copy
@article{2006_Zalatan,
author = {Jesse G Zalatan and Daniel Herschlag},
title = {Alkaline Phosphatase Mono- and Diesterase Reactions: Comparative Transition State Analysis},
journal = {Journal of the American Chemical Society},
year = {2006},
volume = {128},
publisher = {American Chemical Society (ACS)},
month = {jan},
url = {https://doi.org/10.1021/ja056528r},
number = {4},
pages = {1293--1303},
doi = {10.1021/ja056528r}
}
Cite this
MLA
Copy
Zalatan, Jesse G., and Daniel Herschlag. “Alkaline Phosphatase Mono- and Diesterase Reactions: Comparative Transition State Analysis.” Journal of the American Chemical Society, vol. 128, no. 4, Jan. 2006, pp. 1293-1303. https://doi.org/10.1021/ja056528r.