X-ray Structures of the Proprotein Convertase Furin Bound with Substrate Analogue Inhibitors Reveal Substrate Specificity Determinants beyond the S4 Pocket

Biochemistry ◽  
2018 ◽  
Vol 57 (6) ◽  
pp. 925-934 ◽  
Author(s):  
Sven O. Dahms ◽  
Kornelia Hardes ◽  
Torsten Steinmetzer ◽  
Manuel E. Than
Keyword(s):  
Substrate Specificity ◽  
Proprotein Convertase ◽  
X Ray ◽  
Substrate Analogue ◽  
Specificity Determinants

scholarly journals Substrate specificity of three new intradiol dioxygenases: an X-ray characterization

2005 ◽  
Vol 61 (a1) ◽  
pp. c209-c209 ◽  
Author(s):  
M. Ferraroni ◽  
V. M. Travkin ◽  
M. P. Kolomytseva ◽  
A. Scozzafava ◽  
L. Golovleva ◽  
...  
Keyword(s):  
Substrate Specificity ◽  
X Ray

A Family 10 Thermoascus aurantiacus Xylanase Utilizes Arabinose Decorations of Xylan as Significant Substrate Specificity Determinants

2005 ◽  
Vol 352 (5) ◽  
pp. 1060-1067 ◽  
Author(s):  
Maria Vardakou ◽  
James Flint ◽  
Paul Christakopoulos ◽  
Richard J. Lewis ◽  
Harry J. Gilbert ◽  
...  
Keyword(s):  
Substrate Specificity ◽  
Thermoascus Aurantiacus ◽  
Specificity Determinants

X-ray Structure, Bioinformatics Analysis, and Substrate Specificity of a 6-Phospho-β-glucosidase Glycoside Hydrolase 1 Enzyme from Bacillus licheniformis

2020 ◽  
Vol 60 (12) ◽  
pp. 6392-6407
Author(s):  
Wayde Veldman ◽  
Marcelo Vizona Liberato ◽  
Vitor M. Almeida ◽  
Valquiria P. Souza ◽  
Maira A. Frutuoso ◽  
...  
Keyword(s):  
Substrate Specificity ◽  
Bacillus Licheniformis ◽  
Glycoside Hydrolase ◽  
Bioinformatics Analysis ◽  
X Ray

Chemo-enzymatic Synthesis of 3′-azido/-amino-C-4′-spirooxetano-xylo nucleosides

2020 ◽  
Vol 7 (1) ◽  
pp. 120-127 ◽  
Author(s):  
Manish Kumar ◽  
Rajesh Kumar ◽  
Neha Rana ◽  
Ashok K. Prasad
Keyword(s):  
Substrate Specificity ◽  
Ethyl Acetate ◽  
Enzymatic Synthesis ◽  
Environmentally Friendly ◽  
Modified Nucleosides ◽  
Quantitative Yield ◽  
Hydroxymethyl Group ◽  
Crucial Step ◽  
X Ray ◽  
Sugar Derivative

Conformationally locked 3'-azido-C-4'-spirooxetano-xylonucleosides T, U, C and A have been synthesized by following chemo-enzymatic convergent route. One of the 3'-azido-C-4'- spirooxetano-xylonucleosides, i.e. T was converted into 3'-amino-C-4'-spirooxetano-xylothymidine by reduction of azide to amine with H2/Pd-C in ethyl acetate in quantitative yield. The crucial step in the synthesis of spirooxetano-xylonucleosides is the Lipozyme® TL IM-mediated exclusive diastereoselective acetylation of 4-C-hydroxymethyl group in dihydroxysugar derivative, 3-azido-3-deoxy-4-Chydroxymethyl- 1,2-O-isopropylidene-α-D-xylofuranose in quantitative yield. The diastereoselective monoacetylation of 4-C-hydroxymethyl in dihydroxysugar derivative was unambiguously confirmed by X-ray crystal study on the tosylated compound obtained by the tosylation of Lipozyme® TL IM - mediated monoacetylated sugar derivative. The broader substrate specificity and exclusive selective nature of Lipozyme® TL IM can be utilised for the development of environmentally friendly methodologies for the synthesis of different sugar-modified nucleosides of importance.

scholarly journals Structure and substrate specificity determinants of the taurine biosynthetic enzyme cysteine sulphinic acid decarboxylase

2021 ◽  
Vol 213 (1) ◽  
pp. 107674
Author(s):  
Elaheh Mahootchi ◽  
Arne Raasakka ◽  
Weisha Luan ◽  
Gopinath Muruganandam ◽  
Remy Loris ◽  
...  
Keyword(s):  
Substrate Specificity ◽  
Acid Decarboxylase ◽  
Biosynthetic Enzyme ◽  
Specificity Determinants

scholarly journals X-ray Analysis of the NMC-A β-Lactamase at 1.64-Å Resolution, a Class A Carbapenemase with Broad Substrate Specificity

1998 ◽  
Vol 273 (41) ◽  
pp. 26714-26721 ◽  
Author(s):  
Peter Swarén ◽  
Laurent Maveyraud ◽  
Xavier Raquet ◽  
Stéphanie Cabantous ◽  
Colette Duez ◽  
...  
Keyword(s):  
Substrate Specificity ◽  
Broad Substrate Specificity ◽  
X Ray ◽  
Class A

scholarly journals Use of the transport specificity ratio and cysteine-scanning mutagenesis to detect multiple substrate specificity determinants in the consensus amphipathic region of the Escherichia coli GABA (γ-aminobutyric acid) transporter encoded by gabP

2003 ◽  
Vol 376 (3) ◽  
pp. 633-644 ◽  
Author(s):  
Steven C. KING ◽  
Lisa BROWN-ISTVAN
Keyword(s):  
Escherichia Coli ◽  
Substrate Specificity ◽  
Chemical Potential ◽  
Hydrophobic Surface ◽  
Structural Features ◽  
Aminobutyric Acid ◽  
Cysteine Scanning ◽  
Cysteine Scanning Mutagenesis ◽  
Specificity Determinants ◽  
Substrate Discrimination

The Escherichia coli GABA (γ-aminobutyric acid) permease, GabP, and other members of the APC (amine/polyamine/choline) transporter superfamily share a CAR (consensus amphipathic region) that probably contributes to solute translocation. If true, then the CAR should contain structural features that act as determinants of substrate specificity (kcat/Km). In order to address this question, we have developed a novel, expression-independent TSR (transport specificity ratio) analysis, and applied it to a series of 69 cysteine-scanning (single-cysteine) variants. The results indicate that GabP has multiple specificity determinants (i.e. residues at which an amino acid substitution substantially perturbs the TSR). Specificity determinants were found: (i) on a hydrophobic surface of the CAR (from Leu-267 to Ala-285), (ii) on a hydrophilic surface of the CAR (from Ser-299 to Arg-318), and (iii) in a cytoplasmic loop (His-233) between transmembrane segments 6 and 7. Overall, these observations show that (i) structural features within the CAR have a role in substrate discrimination (as might be anticipated for a transport conduit) and, interestingly, (ii) the substrate discrimination task is shared among specificity determinants that appear too widely dispersed across the GabP molecule to be in simultaneous contact with the substrates. We conclude that GabP exhibits behaviour consistent with a broadly applicable specificity delocalization principle, which is demonstrated to follow naturally from the classical notion that translocation occurs synchronously with conformational transitions that change the chemical potential of the bound ligand [Tanford (1982) Proc. Natl. Acad. Sci. U.S.A. 79, 2882–2884].

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