scholarly journals Open reading frame 176 in the photosynthesis gene cluster of Rhodobacter capsulatus encodes idi, a gene for isopentenyl diphosphate isomerase.

1996 ◽  
Vol 178 (3) ◽  
pp. 619-624 ◽  
Author(s):  
F M Hahn ◽  
J A Baker ◽  
C D Poulter
Keyword(s):  
Gene Cluster ◽  
Rhodobacter Capsulatus ◽  
Open Reading Frame ◽  
Isopentenyl Diphosphate ◽  
Isopentenyl Diphosphate Isomerase ◽  
Reading Frame ◽  
Photosynthesis Gene

scholarly journals Type II Isopentenyl Diphosphate Isomerase from Synechocystis sp. Strain PCC 6803

2004 ◽  
Vol 186 (23) ◽  
pp. 8156-8158 ◽  
Author(s):  
Sam J. Barkley ◽  
Shrivallabh B. Desai ◽  
C. Dale Poulter
Keyword(s):  
Escherichia Coli ◽  
Open Reading Frame ◽  
Flavin Mononucleotide ◽  
Isopentenyl Diphosphate ◽  
Type Ii ◽  
Isopentenyl Diphosphate Isomerase ◽  
Reading Frame ◽  
Synechocystis Sp ◽  
Pcc 6803

ABSTRACT Open reading frame sll1556 in the cyanobacterium Synechocystis sp. strain 6803 encodes a putative type II isopentenyl diphosphate (IPP) isomerase. The His6-tagged protein was produced in Escherichia coli and purified by Ni2+ chromatography. The homotetrameric enzyme required NADPH, flavin mononucleotide, and Mg2+ for activity; K m IPP was 52 μM, and k cat IPP was 0.23 s−1.

scholarly journals Escherichia coli Open Reading Frame 696 Is idi, a Nonessential Gene Encoding Isopentenyl Diphosphate Isomerase

1999 ◽  
Vol 181 (15) ◽  
pp. 4499-4504 ◽  
Author(s):  
Frederick M. Hahn ◽  
Anthony P. Hurlburt ◽  
C. Dale Poulter
Keyword(s):  
Escherichia Coli ◽  
Mevalonate Pathway ◽  
Open Reading Frame ◽  
Restrictive Temperature ◽  
Isopentenyl Diphosphate ◽  
Isopentenyl Diphosphate Isomerase ◽  
Reading Frame ◽  
E Coli ◽  
Isoprene Unit ◽  
Nonessential Gene

ABSTRACT Isopentenyl diphosphate isomerase catalyzes the interconversion of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). In eukaryotes, archaebacteria, and some bacteria, IPP is synthesized from acetyl coenzyme A by the mevalonate pathway. The subsequent isomerization of IPP to DMAPP activates the five-carbon isoprene unit for subsequent prenyl transfer reactions. In Escherichia coli, the isoprene unit is synthesized from pyruvate and glyceraldehyde-3-phosphate by the recently discovered nonmevalonate pathway. An open reading frame (ORF696) encoding a putative IPP isomerase was identified in the E. coli chromosome at 65.3 min. ORF696 was cloned into an expression vector; the 20.5 kDa recombinant protein was purified in three steps, and its identity as an IPP isomerase was established biochemically. The gene for IPP isomerase, idi, is not clustered with other known genes for enzymes in the isoprenoid pathway. E. coli FH12 was constructed by disruption of the chromosomal idi gene with the aminoglycoside 3′-phosphotransferase gene and complemented by the wild-type idi gene on plasmid pFMH33 with a temperature-sensitive origin of replication. FH12/pFMH33 was able to grow at the restrictive temperature of 44°C and FH12 lacking the plasmid grew on minimal medium, thereby establishing thatidi is a nonessential gene. Although theV max of the bacterial protein was 20-fold lower than that of its yeast counterpart, the catalytic efficiencies of the two enzymes were similar through a counterbalance inKm s. The E. coli protein requires Mg2+ or Mn2+ for activity. The enzyme contains conserved cysteine and glutamate active-site residues found in other IPP isomerases.

scholarly journals Enhancement of the Diversity of Polyoxins by a Thymine-7-Hydroxylase Homolog outside the Polyoxin Biosynthesis Gene Cluster

2010 ◽  
Vol 76 (21) ◽  
pp. 7343-7347 ◽  
Author(s):  
Changming Zhao ◽  
Tingting Huang ◽  
Wenqing Chen ◽  
Zixin Deng
Keyword(s):  
Gene Cluster ◽  
Carbon Skeleton ◽  
Open Reading Frame ◽  
Streptomyces Avermitilis ◽  
Biosynthesis Gene Cluster ◽  
Reading Frame ◽  
Biosynthesis Gene ◽  
Pyrimidine Moiety

ABSTRACT Polyoxins consist of 14 structurally variable components which differentiate at three branch sites of the carbon skeleton. Open reading frame (ORF) SAV_4805 of Streptomyces avermitilis, showing similarity to thymine-7-hydroxylase, was proved to enhance the diversity of polyoxins at the C-5 site of the 1-(5′-amino-5′-deoxy-β-d-allofuranuronosyl) pyrimidine moiety.

scholarly journals Isolation and Characterization of Canthaxanthin Biosynthesis Genes from the Photosynthetic Bacterium Bradyrhizobiumsp. Strain ORS278

2000 ◽  
Vol 182 (13) ◽  
pp. 3850-3853 ◽  
Author(s):  
Laure Hannibal ◽  
Jean Lorquin ◽  
Nicolas Angles D'Ortoli ◽  
Nelly Garcia ◽  
Clemence Chaintreuil ◽  
...  
Keyword(s):  
Gene Cluster ◽  
Photosynthetic Bacterium ◽  
Carotenoid Biosynthesis ◽  
Open Reading Frame ◽  
Biosynthesis Gene Cluster ◽  
Reading Frame ◽  
Functional Assignment ◽  
Isolation And Characterization ◽  
Biosynthesis Gene

ABSTRACT A carotenoid biosynthesis gene cluster involved in canthaxanthin production was isolated from the photosyntheticBradyrhizobium sp. strain ORS278. This cluster includes five genes identified as crtE, crtY,crtI, crtB, and crtW that are organized in at least two operons. The functional assignment of each open reading frame was confirmed by complementation studies.

Cloning and characterization of theddsAgene encoding decaprenyl diphosphate synthase fromRhodobacter capsulatusB10

2006 ◽  
Vol 52 (12) ◽  
pp. 1141-1147 ◽  
Author(s):  
Xinyi Liu ◽  
Haizhen Wu ◽  
Jiang Ye ◽  
Qinsheng Yuan ◽  
Huizhan Zhang
Keyword(s):  
Gene Expression ◽  
Escherichia Coli ◽  
Rhodobacter Capsulatus ◽  
Open Reading Frame ◽  
High Similarity ◽  
Reading Frame ◽  
Endogenous Production ◽  
Genome Library

A decaprenyl diphosphate synthase gene (ddsA, GenBank accession No. DQ191802) was cloned from Rhodobacter capsulatus B10 by constructing and screening the genome library. An open reading frame of 1002 bp was revealed from sequence analysis. The deduced polypeptide consisted of 333 amino acids residues with an molecular mass of about 37 kDa. The DdsA protein contained the conserved amino acid sequence (DDXXD) of E-type polyprenyl diphosphate synthase and showed high similarity to others. In contrast, DdsA showed only 39% identity to a solanesyl diphosphate synthase cloned from R. capsulatus SB1003. DdsA was expressed successfully in Escherichia coli. Assaying the enzyme in vivo found it made E.coli synthesize UQ-10 in addition to the endogenous production UQ-8.Key words: ubiquinone, polyprenyl diphosphate synthase, gene expression, Rhodobacter capsulatus.

scholarly journals MrpB Functions as the Terminator for Assembly of Proteus mirabilis Mannose-Resistant Proteus-Like Fimbriae

1998 ◽  
Vol 66 (4) ◽  
pp. 1759-1763 ◽  
Author(s):  
Xin Li ◽  
Harry L. T. Mobley
Keyword(s):  
Gene Cluster ◽  
Proteus Mirabilis ◽  
Insertional Mutagenesis ◽  
Open Reading Frame ◽  
Reading Frame

ABSTRACT Insertional mutagenesis studies of mrpB, a putative pilin-encoding open reading frame of the mrp gene cluster, which encodes mannose-resistant Proteus-like (MR/P) fimbriae of Proteus mirabilis, indicate that MrpB functions as the terminator for fimbrial assembly.

scholarly journals Eubacterial Diterpene Cyclase Genes Essential for Production of the Isoprenoid Antibiotic Terpentecin

2001 ◽  
Vol 183 (20) ◽  
pp. 6085-6094 ◽  
Author(s):  
Tohru Dairi ◽  
Yoshimitsu Hamano ◽  
Tomohisa Kuzuyama ◽  
Nobuya Itoh ◽  
Kazuo Furihata ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Sequence Analysis ◽  
Mevalonate Pathway ◽  
Open Reading Frame ◽  
Upstream Region ◽  
Constitutive Promoter ◽  
Isopentenyl Diphosphate ◽  
Geranylgeranyl Diphosphate ◽  
Reading Frame ◽  
Open Reading Frame 2

ABSTRACT A gene cluster containing the mevalonate pathway genes (open reading frame 2 [ORF2] to ORF7) for the formation of isopentenyl diphosphate and a geranylgeranyl diphosphate (GGDP) synthase gene (ORF1) had previously been cloned from Streptomyces griseolosporeus strain MF730-N6, a diterpenoid antibiotic, terpentecin (TP) producer (Y. Hamano, T. Dairi, M. Yamamoto, T. Kawasaki, K Kaneda, T. Kuzuyama, N. Itoh, and H. Seto, Biosci. Biotech. Biochem. 65:1627–1635, 2001). Sequence analysis in the upstream region of the cluster revealed seven new ORFs, ORF8 to ORF14, which were suggested to encode TP biosynthetic genes. We constructed two mutants, in which ORF11 and ORF12, which encode a protein showing similarities to eukaryotic diterpene cyclases (DCs) and a eubacterial pentalenene synthase, respectively, were inactivated by gene disruptions. The mutants produced no TP, confirming that these cyclase genes are essential for the production of TP. The two cyclase genes were also expressed in Streptomyces lividans together with the GGDP synthase gene under the control of theermE* constitutive promoter. The transformant produced a novel cyclic diterpenoid, ent-clerod-3,13(16),14-triene (terpentetriene), which has the same basic skeleton as TP. The two enzymes, each of which was overproduced in Escherichia coli and purified to homogeneity, converted GGDP into terpentetriene. To the best of our knowledge, this is the first report of a eubacterial DC.

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