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You searched for: Author "Isupov, Michail N." Remove constraint Author: "Isupov, Michail N." Subject crystal structure Remove constraint Subject: crystal structure Subject active sites Remove constraint Subject: active sites
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1. Structural studies of a thermophilic esterase from a new Planctomycetes species, Thermogutta terrifontis

Author:
Isupov, Michail N.,   et al.   ; Sayer, Christopher; Bonch‐Osmolovskaya, Elizaveta; Littlechild, Jennifer A.;     Show all 4 Authors
Source:
The FEBS journal 2015 v.282 no.15 pp. 2846-2857
ISSN:
1742-464X
Subject:
Escherichia coli; acetates; active sites; alcohols; amino acids; butyrates; catalytic activity; crystal structure; esterases; genetic databases; ligands; malates; mutants; propionic acid; thermophilic bacteria
Abstract:
... Thermogutta terrifontis esterase (TtEst), a carboxyl esterase identified in the novel thermophilic bacterium T. terrifontis from the phylum Planctomycetes, has been cloned and over‐expressed in Escherichia coli. The enzyme has been characterized biochemically and shown to have activity towards small p‐nitrophenyl (pNP) carboxylic esters, with optimal activity for pNP‐propionate. The enzyme retaine ...
DOI:
10.1111/febs.13326

2. Biochemical and structural characterisation of a haloalkane dehalogenase from a marine Rhodobacteraceae

Author:
Isupov, Michail N.,   et al.   ; Novak, Halina R.; Sayer, Christopher; Gotz, Dorothee; Spragg, Andrew Mearns; Littlechild, Jennifer A.;     Show all 6 Authors
Source:
FEBS letters 2014 v.588 pp. 1616-1622
ISSN:
0014-5793
Subject:
Escherichia coli; Rhodobacteraceae; active sites; carbon; crystal structure; hydrophobicity
Abstract:
... A putative haloalkane dehalogenase has been identified in a marine Rhodobacteraceae and subsequently cloned and over-expressed in Escherichia coli. The enzyme has highest activity towards the substrates 1,6-dichlorohexane, 1-bromooctane, 1,3-dibromopropane and 1-bromohexane. The crystal structures of the enzyme in the native and product bound forms reveal a large hydrophobic active site cavity. A ...
DOI:
10.1016/j.febslet.2014.02.056

3. The Fasciola hepatica thioredoxin: High resolution structure reveals two oxidation states

Author:
Isupov, Michail N.,   et al.   ; Line, Kirsty; Garcia-Rodriguez, Esther; Maggioli, Gabriela; Parra, Francisco; Littlechild, Jennifer A.;     Show all 6 Authors
Source:
Molecular and biochemical parasitology 2008 v.161 no.1 pp. 44-48
ISSN:
0166-6851
Subject:
Fasciola hepatica; active sites; crystal structure; cysteine; disulfide bonds; hosts; humans; oxidation; protein structure
Abstract:
... The Fasciola hepatica thioredoxin protein structure has been determined to 1.45Å resolution. This is the first example of a single crystal structure to show the active site cysteine residues in both the reduced and disulfide oxidised form. Consistent with this observation the process of oxidation appears to require very little rearrangement of the surrounding protein structure. The F. hepatica thi ...
DOI:
10.1016/j.molbiopara.2008.06.009

4. Crystal structure of D-serine dehydratase from Escherichia coli Proteins and proteomics

Author:
Isupov, Michail N.,   et al.   ; Urusova, Darya V.; Antonyuk, Svetlana; Kachalova, Galina S.; Obmolova, Galina; Vagin, Alexei A.; Lebedev, Andrey A.; Burenkov, Gleb P.; Dauter, Zbigniew; Bartunik, Hans D.; Lamzin, Victor S.; Melik-Adamyan, William R.; Mueller, Thomas D.; Schnackerz, Klaus D.;     Show all 14 Authors
Source:
Biochimica et biophysica acta 2012 v.1824 no.3 pp. 422-432
ISSN:
1878-1454
Subject:
Escherichia coli; active sites; ammonia; catalytic activity; crystal structure; data collection; hydrogen bonding; models; oxygen; pyridoxal; pyruvic acid; schiff bases; serine dehydratase
Abstract:
... D-Serine dehydratase from Escherichia coli is a member of the β-family (fold-type II) of the pyridoxal 5′-phosphate-dependent enzymes, catalyzing the conversion of D-serine to pyruvate and ammonia. The crystal structure of monomeric D-serine dehydratase has been solved to 1.97Å-resolution for an orthorhombic data set by molecular replacement. In addition, the structure was refined in a monoclinic ...
DOI:
10.1016/j.bbapap.2011.10.017