scholarly journals Predicting active site residue annotations in the Pfam database

2007 ◽  
Vol 8 (1) ◽  
Author(s):  
Jaina Mistry ◽  
Alex Bateman ◽  
Robert D Finn
Keyword(s):  
Active Site ◽  
Active Site Residue ◽  
Pfam Database

Active-site residue, domain and module swaps in modular polyketide synthases

2003 ◽  
Vol 30 (8) ◽  
pp. 489-494 ◽  
Author(s):  
Francesca Del Vecchio ◽  
Hrvoje Petkovic ◽  
Steven G. Kendrew ◽  
Lindsey Low ◽  
Barrie Wilkinson ◽  
...  
Keyword(s):  
Active Site ◽  
Polyketide Synthases ◽  
Active Site Residue

Active site residue involvement in monoamine or diamine oxidation catalysed by pea seedling amine oxidase

FEBS Journal ◽  
2011 ◽  
Vol 278 (8) ◽  
pp. 1232-1243 ◽  
Author(s):  
Maria Luisa Di Paolo ◽  
Michele Lunelli ◽  
Monika Fuxreiter ◽  
Adelio Rigo ◽  
Istvan Simon ◽  
...  
Keyword(s):  
Active Site ◽  
Amine Oxidase ◽  
Active Site Residue ◽  
Pea Seedling

scholarly journals The active-site residue Cys-29 is responsible for the neutral-pH inactivation and the refolding barrier of human cathepsin B

FEBS Letters ◽  
2000 ◽  
Vol 475 (3) ◽  
pp. 157-162 ◽  
Author(s):  
Jianxing Song ◽  
Ping Xu ◽  
Hui Xiang ◽  
Zhengding Su ◽  
Andrew C. Storer ◽  
...  
Keyword(s):  
Active Site ◽  
Cathepsin B ◽  
Active Site Residue ◽  
Neutral Ph ◽  
Ph Inactivation ◽  
Human Cathepsin

scholarly journals Phospholipase A2 Engineering. Structural and Functional Roles of the Highly Conserved Active Site Residue Aspartate-49

Biochemistry ◽  
1994 ◽  
Vol 33 (49) ◽  
pp. 14714-14722 ◽  
Author(s):  
Yishan Li ◽  
Bao-Zhu Yu ◽  
Hongxin Zhu ◽  
Mahendra K. Jain ◽  
Ming-Daw Tsai
Keyword(s):  
Phospholipase A2 ◽  
Active Site ◽  
Active Site Residue ◽  
Functional Roles

Identification of Glutamic Acid 381 as a Candidate Active Site Residue ofPseudomonas aeruginosaExoenzyme S†

Biochemistry ◽  
1996 ◽  
Vol 35 (8) ◽  
pp. 2754-2758 ◽  
Author(s):  
Suyan Liu ◽  
Scott M. Kulich ◽  
Joseph T. Barbieri
Keyword(s):  
Glutamic Acid ◽  
Active Site ◽  
Active Site Residue

scholarly journals Charge Reversal of a Critical Active-Site Residue of Cytochrome-c Peroxidase. Characterization of the Arg48Glu Variant

1997 ◽  
Vol 243 (1-2) ◽  
pp. 72-84 ◽  
Author(s):  
Jordi Bujons ◽  
Alexander Dikiy ◽  
Juan C. Ferrer ◽  
Lucia Banci ◽  
A. Grant Mauk
Keyword(s):  
Cytochrome C ◽  
Active Site ◽  
Cytochrome C Peroxidase ◽  
Active Site Residue ◽  
Charge Reversal

scholarly journals Identification of an essential active-site residue in the α-d-phosphohexomutase enzyme superfamily

FEBS Journal ◽  
2013 ◽  
Vol 280 (11) ◽  
pp. 2622-2632 ◽  
Author(s):  
Yingying Lee ◽  
Ritcha Mehra-Chaudhary ◽  
Cristina Furdui ◽  
Lesa J. Beamer
Keyword(s):  
Active Site ◽  
Active Site Residue ◽  
Enzyme Superfamily

Structure analysis of endosialidase NF at 0.98 Å resolution

2010 ◽  
Vol 66 (2) ◽  
pp. 176-180 ◽  
Author(s):  
Eike C. Schulz ◽  
Piotr Neumann ◽  
Rita Gerardy-Schahn ◽  
George M. Sheldrick ◽  
Ralf Ficner
Keyword(s):  
Sialic Acid ◽  
Structure Analysis ◽  
Active Site ◽  
Polysialic Acid ◽  
Crystal Form ◽  
Atomic Resolution ◽  
Active Site Residue ◽  
Catalytic Function ◽  
Multiple Conformations ◽  
A Minor

Endosialidase NF (endoNF) is a bacteriophage-derived endosialidase that specifically degrades α-2,8-linked polysialic acid. The structure of a new crystal form of endoNF in complex with sialic acid has been refined at 0.98 Å resolution. The 210 kDa homotrimeric multi-domain enzyme displays outstanding stability and resistance to SDS. Even at atomic resolution, only a minor fraction of side chains possess alternative conformations. However, multiple conformations of an active-site residue imply that it has an important catalytic function in the cleavage mechanism of polysialic acid.

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