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.

scholarly journals Molecular architectures of benzoic acid-specific type III polyketide synthases

2017 ◽  
Vol 73 (12) ◽  
pp. 1007-1019 ◽  
Author(s):  
Charles Stewart ◽  
Kate Woods ◽  
Greg Macias ◽  
Andrew C. Allan ◽  
Roger P. Hellens ◽  
...  
Keyword(s):  
Benzoic Acid ◽  
Active Site ◽  
Polyketide Synthases ◽  
Chain Elongation ◽  
Cyclization Reactions ◽  
Functional Diversification ◽  
Structural Determinants ◽  
Type Iii ◽  
Endogenous Substrate ◽  
Small Hydrophobic

Biphenyl synthase and benzophenone synthase constitute an evolutionarily distinct clade of type III polyketide synthases (PKSs) that use benzoic acid-derived substrates to produce defense metabolites in plants. The use of benzoyl-CoA as an endogenous substrate is unusual for type III PKSs. Moreover, sequence analyses indicate that the residues responsible for the functional diversification of type III PKSs are mutated in benzoic acid-specific type III PKSs. In order to gain a better understanding of structure–function relationships within the type III PKS family, the crystal structures of biphenyl synthase fromMalus×domesticaand benzophenone synthase fromHypericum androsaemumwere compared with the structure of an archetypal type III PKS: chalcone synthase fromMalus×domestica. Both biphenyl synthase and benzophenone synthase contain mutations that reshape their active-site cavities to prevent the binding of 4-coumaroyl-CoA and to favor the binding of small hydrophobic substrates. The active-site cavities of biphenyl synthase and benzophenone synthase also contain a novel pocket associated with their chain-elongation and cyclization reactions. Collectively, these results illuminate structural determinants of benzoic acid-specific type III PKSs and expand the understanding of the evolution of specialized metabolic pathways in plants.

Sign in / Sign up

Export Citation Format

Share Document