Crystal Structure of the Haloalkane Dehalogenase fromSphingomonas paucimobilisUT26†,‡

Biochemistry ◽  
2000 ◽  
Vol 39 (46) ◽  
pp. 14082-14086 ◽  
Author(s):  
Jaromír Marek ◽  
Jitka Vévodová ◽  
Ivana Kutá Smatanová ◽  
Yuji Nagata ◽  
L. Anders Svensson ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Haloalkane Dehalogenase

X-ray crystal structure of Mycobacterium tuberculosis haloalkane dehalogenase Rv2579

2008 ◽  
Vol 1784 (2) ◽  
pp. 351-362 ◽  
Author(s):  
Pooja A. Mazumdar ◽  
Jordan C. Hulecki ◽  
Maia M. Cherney ◽  
Craig R. Garen ◽  
Michael N.G. James
Keyword(s):  
Crystal Structure ◽  
Mycobacterium Tuberculosis ◽  
Haloalkane Dehalogenase ◽  
X Ray

scholarly journals Reconstruction of Mycobacterial Dehalogenase Rv2579 by Cumulative Mutagenesis of Haloalkane Dehalogenase LinB

2003 ◽  
Vol 69 (4) ◽  
pp. 2349-2355 ◽  
Author(s):  
Yuji Nagata ◽  
Zbyněk Prokop ◽  
Soňa Marvanová ◽  
Jana Sýkorová ◽  
Marta Monincová ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Mycobacterium Tuberculosis ◽  
Amino Acid ◽  
Active Site ◽  
Homology Model ◽  
Protein Family ◽  
Sphingomonas Paucimobilis ◽  
Amino Acid Residues ◽  
Haloalkane Dehalogenase

ABSTRACT The homology model of protein Rv2579 from Mycobacterium tuberculosis H37Rv was compared with the crystal structure of haloalkane dehalogenase LinB from Sphingomonas paucimobilis UT26, and this analysis revealed that 6 of 19 amino acid residues which form an active site and entrance tunnel are different in LinB and Rv2579. To characterize the effect of replacement of these six amino acid residues, mutations were introduced cumulatively into the six amino acid residues of LinB. The sixfold mutant, which was supposed to have the active site of Rv2579, exhibited haloalkane dehalogenase activity with the haloalkanes tested, confirming that Rv2579 is a member of the haloalkane dehalogenase protein family.

scholarly journals Crystal structure of the haloalkane dehalogenase DbjA

2005 ◽  
Vol 61 (a1) ◽  
pp. c193-c193
Author(s):  
Y. Sato ◽  
R. Natsume ◽  
Z. Prokop ◽  
M. Senda ◽  
J. Damborsky ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Haloalkane Dehalogenase

Crystal Structure of Haloalkane Dehalogenase LinB fromSphingomonas paucimobilisUT26 at 0.95 Å Resolution:  Dynamics of Catalytic Residues†,‡

Biochemistry ◽  
2004 ◽  
Vol 43 (4) ◽  
pp. 870-878 ◽  
Author(s):  
Aaron J. Oakley ◽  
Martin Klvaňa ◽  
Michal Otyepka ◽  
Yuji Nagata ◽  
Matthew C. J. Wilce ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Haloalkane Dehalogenase ◽  
Catalytic Residues

scholarly journals Crystal Structure and Site-Directed Mutagenesis Analyses of Haloalkane Dehalogenase LinB from Sphingobium sp. Strain MI1205

2013 ◽  
Vol 195 (11) ◽  
pp. 2642-2651 ◽  
Author(s):  
M. Okai ◽  
J. Ohtsuka ◽  
L. F. Imai ◽  
T. Mase ◽  
R. Moriuchi ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Haloalkane Dehalogenase

scholarly journals Discovery of Novel Haloalkane Dehalogenase Inhibitors

2016 ◽  
Vol 82 (6) ◽  
pp. 1958-1965 ◽  
Author(s):  
Tomas Buryska ◽  
Lukas Daniel ◽  
Antonin Kunka ◽  
Jan Brezovsky ◽  
Jiri Damborsky ◽  
...  
Keyword(s):  
Crystal Structure ◽  
High Specificity ◽  
Molecular Probes ◽  
Molecular Architecture ◽  
Human Pathogen ◽  
Target Structure ◽  
Haloalkane Dehalogenase ◽  
Content Type ◽  
Potential Inhibitors ◽  
Number Of Bacteria

ABSTRACTHaloalkane dehalogenases (HLDs) have recently been discovered in a number of bacteria, including symbionts and pathogens of both plants and humans. However, the biological roles of HLDs in these organisms are unclear. The development of efficient HLD inhibitors serving as molecular probes to explore their function would represent an important step toward a better understanding of these interesting enzymes. Here we report the identification of inhibitors for this enzyme family using two different approaches. The first builds on the structures of the enzymes' known substrates and led to the discovery of less potent nonspecific HLD inhibitors. The second approach involved the virtual screening of 150,000 potential inhibitors against the crystal structure of an HLD from the human pathogenMycobacterium tuberculosisH37Rv. The best inhibitor exhibited high specificity for the target structure, with an inhibition constant of 3 μM and a molecular architecture that clearly differs from those of all known HLD substrates. The new inhibitors will be used to study the natural functions of HLDs in bacteria, to probe their mechanisms, and to achieve their stabilization.

scholarly journals Crystal structure of haloalkane dehalogenase DpcA from psychrophilicPsychrobacter cryohalolentisK5

2013 ◽  
Vol 69 (a1) ◽  
pp. s605-s606
Author(s):  
Katsiaryna Tratsiak ◽  
Oksana Degtjarik ◽  
Tatiana Prudnikova ◽  
Ivana Drienovska ◽  
Lukas Chrast ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Haloalkane Dehalogenase

scholarly journals Crystal structure of the cold-adapted haloalkane dehalogenase DpcA fromPsychrobacter cryohalolentisK5

2019 ◽  
Vol 75 (5) ◽  
pp. 324-331 ◽  
Author(s):  
Katsiaryna Tratsiak ◽  
Tatyana Prudnikova ◽  
Ivana Drienovska ◽  
Jiri Damborsky ◽  
Jiri Brynda ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Psychrophilic Bacterium ◽  
Haloalkane Dehalogenase ◽  
Temperature Optimum ◽  
Toxic Compounds ◽  
Cold Adapted ◽  
Subsurface Environment ◽  
Pure Compounds ◽  
Optically Pure ◽  
Hydrolytic Mechanism

Haloalkane dehalogenases (HLDs) convert halogenated aliphatic pollutants to less toxic compounds by a hydrolytic mechanism. Owing to their broad substrate specificity and high enantioselectivity, haloalkane dehalogenases can function as biosensors to detect toxic compounds in the environment or can be used for the production of optically pure compounds. Here, the structural analysis of the haloalkane dehalogenase DpcA isolated from the psychrophilic bacteriumPsychrobacter cryohalolentisK5 is presented at the atomic resolution of 1.05 Å. This enzyme exhibits a low temperature optimum, making it attractive for environmental applications such as biosensing at the subsurface environment, where the temperature typically does not exceed 25°C. The structure revealed that DpcA possesses the shortest access tunnel and one of the most widely open main tunnels among structural homologs of the HLD-I subfamily. Comparative analysis revealed major differences in the region of the α4 helix of the cap domain, which is one of the key determinants of the anatomy of the tunnels. The crystal structure of DpcA will contribute to better understanding of the structure–function relationships of cold-adapted enzymes.

Crystal structure of haloalkane dehalogenase: an enzyme to detoxify halogenated alkanes.

1991 ◽  
Vol 10 (6) ◽  
pp. 1297-1302 ◽  
Author(s):  
S.M. Franken ◽  
H.J. Rozeboom ◽  
K.H. Kalk ◽  
B.W. Dijkstra
Keyword(s):  
Crystal Structure ◽  
Haloalkane Dehalogenase ◽  
Halogenated Alkanes
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