Literature DB >> 20124718

Expression, purification and X-ray analysis of 1,3-propanediol dehydrogenase (Aq_1145) from Aquifex aeolicus VF5.

Jeyaraman Jeyakanthan1, Subbiah Thamotharan, Santosh Panjikar, Yoshiaki Kitamura, Noriko Nakagawa, Akeo Shinkai, Seiki Kuramitsu, Shigeyuki Yokoyama.   

Abstract

1,3-Propanediol dehydrogenase is an enzyme that catalyzes the oxidation of 1,3-propanediol to 3-hydroxypropanal with the simultaneous reduction of NADP(+) to NADPH. SeMet-labelled 1,3-propanediol dehydrogenase protein from the hyperthermophilic bacterium Aquifex aeolicus VF5 was overexpressed in Escherichia coli and purified to homogeneity. Crystals of this protein were grown from an acidic buffer with ammonium sulfate as the precipitant. Single-wavelength data were collected at the selenium peak to a resolution of 2.4 A. The crystal belonged to space group P3(2), with unit-cell parameters a = b = 142.19, c = 123.34 A. The structure contained two dimers in the asymmetric unit and was solved by the MR-SAD approach.

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Year:  2010        PMID: 20124718      PMCID: PMC2815688          DOI: 10.1107/S1744309109052403

Source DB:  PubMed          Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun        ISSN: 1744-3091


  21 in total

1.  Crystal structure of an iron-containing 1,3-propanediol dehydrogenase (TM0920) from Thermotoga maritima at 1.3 A resolution.

Authors:  Robert Schwarzenbacher; Frank von Delft; Jaume M Canaves; Linda S Brinen; Xiaoping Dai; Ashley M Deacon; Marc A Elsliger; Said Eshaghi; Ross Floyd; Adam Godzik; Carina Grittini; Slawomir K Grzechnik; Chittibabu Guda; Lukasz Jaroszewski; Cathy Karlak; Heath E Klock; Eric Koesema; John S Kovarik; Andreas Kreusch; Peter Kuhn; Scott A Lesley; Daniel McMullan; Timothy M McPhillips; Mark A Miller; Mitchell D Miller; Andrew Morse; Kin Moy; Jie Ouyang; Rebecca Page; Alyssa Robb; Kevin Rodrigues; Thomas L Selby; Glen Spraggon; Raymond C Stevens; Henry van den Bedem; Jeff Velasquez; Juli Vincent; Xianhong Wang; Bill West; Guenter Wolf; Keith O Hodgson; John Wooley; Ian A Wilson
Journal:  Proteins       Date:  2004-01-01

2.  Production of 1,3-propanediol by Klebsiella pneumoniae from glycerol broth.

Authors:  Ke-Ke Cheng; Jian-An Zhang; De-Hua Liu; Yan Sun; Ming-De Yang; Jing-Ming Xu
Journal:  Biotechnol Lett       Date:  2006-08-16       Impact factor: 2.461

3.  Solvent content of protein crystals.

Authors:  B W Matthews
Journal:  J Mol Biol       Date:  1968-04-28       Impact factor: 5.469

4.  Kinetic, dynamic, and pathway studies of glycerol metabolism by Klebsiella pneumoniae in anaerobic continuous culture: III. Enzymes and fluxes of glycerol dissimilation and 1,3-propanediol formation.

Authors:  K Ahrens; K Menzel; A Zeng; W Deckwer
Journal:  Biotechnol Bioeng       Date:  1998-09-05       Impact factor: 4.530

5.  Taxonomic diversity of anaerobic glycerol dissimilation in the Enterobacteriaceae.

Authors:  O M Bouvet; P Lenormand; E Ageron; P A Grimont
Journal:  Res Microbiol       Date:  1995-05       Impact factor: 3.992

Review 6.  Metabolic engineering of propanediol pathways.

Authors:  D C Cameron; N E Altaras; M L Hoffman; A J Shaw
Journal:  Biotechnol Prog       Date:  1998 Jan-Feb

7.  1,3-Propanediol:NAD+ oxidoreductases of Lactobacillus brevis and Lactobacillus buchneri.

Authors:  M Veiga-da-Cunha; M A Foster
Journal:  Appl Environ Microbiol       Date:  1992-06       Impact factor: 4.792

8.  Sugar-glycerol cofermentations in lactobacilli: the fate of lactate.

Authors:  M Veiga da Cunha; M A Foster
Journal:  J Bacteriol       Date:  1992-02       Impact factor: 3.490

9.  Phylogenetic position of the genus Hydrogenobacter.

Authors:  C Pitulle; Y Yang; M Marchiani; E R Moore; J L Siefert; M Aragno; P Jurtshuk; G E Fox
Journal:  Int J Syst Bacteriol       Date:  1994-10

10.  1H-15N heteronuclear NMR studies of Escherichia coli thioredoxin in samples isotopically labeled by residue type.

Authors:  D M LeMaster; F M Richards
Journal:  Biochemistry       Date:  1985-12-03       Impact factor: 3.162

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