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The Acid/Base Catalyst in the Exoglucanase/Xylanase from Cellulomonas fimi Is Glutamic Acid 127: Evidence from Detailed Kinetic Studies of Mutants

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Alasdair M. MacLeod, Thisbe Lindhorst, Stephen G. Withers, R. Antony J. Warren

Biochemistry, 1994, 33 (20), pp 6371–6376

DOI: 10.1021/bi00186a042

Publication Date: May 1994

Note: In lieu of an abstract, this is the article's first page.

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Citing Articles

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This article has been cited by 7 ACS Journal articles (5 most recent appear below).

NMR Spectroscopic Characterization of the Sialyltransferase CstII from Campylobacter jejuni: Histidine 188 Is the General Base
Patrick H. W. Chan, Luke L. Lairson, Ho Jun Lee, Warren W. Wakarchuk, Natalie C. J. Strynadka, Stephen G. Withers and Lawrence P. McIntosh
Biochemistry2009 48 (47), 11220-11230
- NMR Spectroscopic Characterization of the Sialyltransferase CstII from Campylobacter jejuni: Histidine 188 Is the General Base
  Patrick H. W. Chan, Luke L. Lairson, Ho Jun Lee, Warren W. Wakarchuk, Natalie C. J. Strynadka, Stephen G. Withers and Lawrence P. McIntosh
  Biochemistry2009 48 (47), 11220-11230
  Cell surface glycans are often terminated by sialic acid, which is incorporated onto sugar acceptors by sialyltransferases. The crystal structure of the GT family 42 Campylobacter jejuni α-2,3/2,8-sialyltransferase (CstII) provides key insights into the ...
  Abstract | Full Text HTML | Hi-Res PDF | PDF w/ Links
Kinetic and Mechanistic Analysis of Trypanosoma cruzi Trans-Sialidase Reveals a Classical Ping-Pong Mechanism with Acid/Base Catalysis
Iben Damager, Sabrina Buchini, Maria F. Amaya, Alejandro Buschiazzo, Pedro Alzari, Alberto C. Frasch, Andrew Watts and Stephen G. Withers
Biochemistry2008 47 (11), 3507-3512
- Kinetic and Mechanistic Analysis of Trypanosoma cruzi Trans-Sialidase Reveals a Classical Ping-Pong Mechanism with Acid/Base Catalysis
  Iben Damager, Sabrina Buchini, Maria F. Amaya, Alejandro Buschiazzo, Pedro Alzari, Alberto C. Frasch, Andrew Watts and Stephen G. Withers
  Biochemistry2008 47 (11), 3507-3512
  The trans-sialidase from Trypanosoma cruzi catalyzes the transfer of a sialic acid moiety from sialylated donor substrates to the terminal galactose moiety of lactose and lactoside acceptors to yield α-(2,3)-sialyllactose or its derivatives with net ...
  Abstract | Full Text HTML | Hi-Res PDF | PDF w/ Links
Recruitment of Both Uniform and Differential Binding Energy in Enzymatic Catalysis: Xylanases from Families 10 and 11
Jacqueline Wicki, Johann Schloegl, Chris A. Tarling, and Stephen G. Withers
Biochemistry2007 46 (23), 6996-7005
- Recruitment of Both Uniform and Differential Binding Energy in Enzymatic Catalysis: Xylanases from Families 10 and 11
  Jacqueline Wicki, Johann Schloegl, Chris A. Tarling, and Stephen G. Withers
  Biochemistry2007 46 (23), 6996-7005
  The contributions of enzymesubstrate hydrogen-binding interactions to catalysis by two different families of xylanases were evaluated through kinetic studies with two representative wild-type enzymes, Cellulomonas fimi xylanase (Cex) and Bacillus ...
  Abstract | Full Text HTML | Hi-Res PDF
Identification of Asp¹⁷⁴ and Asp¹⁷⁵ as the Key Catalytic Residues of Human O-GlcNAcase by Functional Analysis of Site-Directed Mutants
Naniye Çetinbaş, Matthew S. Macauley, Keith A. Stubbs, Robert Drapala, and David J. Vocadlo
Biochemistry2006 45 (11), 3835-3844
- Identification of Asp¹⁷⁴ and Asp¹⁷⁵ as the Key Catalytic Residues of Human O-GlcNAcase by Functional Analysis of Site-Directed Mutants
  Naniye Çetinbaş, Matthew S. Macauley, Keith A. Stubbs, Robert Drapala, and David J. Vocadlo
  Biochemistry2006 45 (11), 3835-3844
  O-GlcNAcase is a family 84 -N-acetylglucosaminidase catalyzing the hydrolytic cleavage of -O-linked 2-acetamido-2-deoxy-d-glycopyranose (O-GlcNAc) from serine and threonine residues of posttranslationally modified proteins. O-GlcNAcases use a double-...
  Abstract | Full Text HTML | Hi-Res PDF
Structures of Purine 2‘-Deoxyribosyltransferase, Substrate Complexes, and the Ribosylated Enzyme Intermediate at 2.0 Å Resolution^,
Ruchi Anand, Pierre Alexandre Kaminski, and Steven E. Ealick
Biochemistry2004 43 (9), 2384-2393
- Structures of Purine 2‘-Deoxyribosyltransferase, Substrate Complexes, and the Ribosylated Enzyme Intermediate at 2.0 Å Resolution^,
  Ruchi Anand, Pierre Alexandre Kaminski, and Steven E. Ealick
  Biochemistry2004 43 (9), 2384-2393
  The structure of class I N-deoxyribosyltransferase from Lactobacillus helveticus was determined by X-ray crystallography. Unlike class II N-deoxyribosyltransferases, which accept either purine or pyrimidine deoxynucleosides, class I enzymes are specific ...
  Abstract | Full Text HTML | Hi-Res PDF

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Research Article

The Acid/Base Catalyst in the Exoglucanase/Xylanase from Cellulomonas fimi Is Glutamic Acid 127: Evidence from Detailed Kinetic Studies of Mutants

Citing Articles

NMR Spectroscopic Characterization of the Sialyltransferase CstII from Campylobacter jejuni: Histidine 188 Is the General Base

NMR Spectroscopic Characterization of the Sialyltransferase CstII from Campylobacter jejuni: Histidine 188 Is the General Base

Kinetic and Mechanistic Analysis of Trypanosoma cruzi Trans-Sialidase Reveals a Classical Ping-Pong Mechanism with Acid/Base Catalysis

Kinetic and Mechanistic Analysis of Trypanosoma cruzi Trans-Sialidase Reveals a Classical Ping-Pong Mechanism with Acid/Base Catalysis

Recruitment of Both Uniform and Differential Binding Energy in Enzymatic Catalysis: Xylanases from Families 10 and 11

Recruitment of Both Uniform and Differential Binding Energy in Enzymatic Catalysis: Xylanases from Families 10 and 11

Identification of Asp¹⁷⁴ and Asp¹⁷⁵ as the Key Catalytic Residues of Human O-GlcNAcase by Functional Analysis of Site-Directed Mutants

Identification of Asp¹⁷⁴ and Asp¹⁷⁵ as the Key Catalytic Residues of Human O-GlcNAcase by Functional Analysis of Site-Directed Mutants

Structures of Purine 2‘-Deoxyribosyltransferase, Substrate Complexes, and the Ribosylated Enzyme Intermediate at 2.0 Å Resolution^,