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  • 1
    Electronic Resource
    Electronic Resource
    Structure of dehydroquinate synthase reveals an active site capable of multistep catalysis (1998)
    [s.l.] : Macmillan Magazines Ltd.
    Nature 394 (1998), S. 299-302 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Dehydroquinate synthase (DHQS) has long been regarded as a catalytic marvel because of its ability to perform several consecutive chemical reactions in one active site. There has been considerable debate as to whether DHQS is actively involved in all these steps,, or whether several steps occur ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/28431
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  • 2
    Electronic Resource
    Electronic Resource
    The two types of 3-dehydroquinase have distinct structures but catalyze the same overall reaction (1999)
    [s.l.] : Nature America Inc.
    Nature structural biology 6 (1999), S. 521-525 
    Details
    ISSN: 1072-8368
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Medicine
    Notes: [Auszug] The structures of enzymes catalyzing the reactions in central metabolic pathways are generally well conserved as are their catalytic mechanisms. The two types of 3-dehydroquinate dehydratase (DHQase) are therefore most unusual since they are unrelated at the sequence level and they utilize ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/9287
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  • 3
    Electronic Resource
    Electronic Resource
    Isolation and identification of the Aspergillus nidulans gdhA gene encoding NADP-linked glutamate dehydrogenase (1986)
    Springer
    Current genetics 10 (1986), S. 761-766 
    Details
    ISSN: 1432-0983
    Keywords: Aspergillus nidulans ; Glutamate dehydrogenase ; Ammonium assimilation ; Fungal genes
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The Neurospora crassa am gene was used as a heterologous probe to identify clones from two independently constructed Aspergillus nidulans gene libraries. These clones have a common HindIII 1.85 kb fragment. This A. nidulans nucleotide stretch hybridises to a N. crassa 2.7 kb BamHI fragment of wild type DNA but not to a co-migrating fragment from the DNA of the N. crassa am132 deletion mutant. One A. nidulans clone was shown to complement the N. crasse am132 deletion strain. The N. crassa transformants show low levels (∼5%) of heterologous glutamate dehydrogenase activity. The A. nidulans gdhA gene was found to locate in N. crassa at both the “homologous” (i.e. am) site as well as non-nomologous sites. Partial nucleotide analysis of the fragment has revealed the 5′ end of the locus and considerable homology with the N. crassa am gene. We concluded that we have cloned the A. nidulans gdhA gene.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00405099
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  • 4
    Electronic Resource
    Electronic Resource
    Identification and isolation of a putative permease gene in the quinic acid utilization (QUT) gene cluster of Aspergillus nidulans (1987)
    Springer
    Current genetics 12 (1987), S. 135-139 
    Details
    ISSN: 1432-0983
    Keywords: Aspergillus ; Quinic acid utilization ; Noninducible mutants ; pH sensitivity ; Permease
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Mutations in the qutD gene of Aspergillus nidulans cause the loss of ability to grow upon quinic acid as sole carbon source in media at normal pH 6.5 and failure to induce three enzyme activities specifically required for metabolism to protochatechuic acid. All 9 qutD mutants recovered are recessive and have been found to be pH sensitive, growing strongly on quinic acid media at pH 3.5 and producing significant induced enzyme acitivities. These properties are consistent with the hypothesis that the QUTD gene encodes an essential component of a permease required for transport of quinate ion into mycelium at pH 6.5. The QUTD gene has been located within the cloned QUT gene cluster of A. nidulans by transformation of qutD mutants with fragments of cloned sequences from phage λ-Q1. The QUTD locus is in a region distinct from other QUT genes and which contains sequences homologous to the QA-Y gene in the corresponding QA gene cluster of Neurospora crassa.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00434668
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  • 5
    Electronic Resource
    Electronic Resource
    Cloning and characterization of the three enzyme structural genes QUTB, QUTC and QUTE from the quinic acid utilization gene cluster in Aspergillus nidulans (1985)
    Springer
    Current genetics 9 (1985), S. 305-311 
    Details
    ISSN: 1432-0983
    Keywords: Aspergillus ; Quinic acid utilisation ; Gene cluster ; Cloning
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Heterologous DNA probes from the quinic acid gene cluster (QA) in Neurospora crassa (Schweizer 1981) have been used to isolate the corresponding gene cluster (QUT) from Aspergillus nidulans cloned in a phage λ vector. N. crassa probes for each of the three enzyme structural genes in the cluster have been used to identify the corresponding genes within the A. nidulans cloned DNA. The three genes are in the same relative sequence [dehydrogenase (1), QA-3 ≡ QUTB; dehydratase (3), QA-4 ≡ QUTC; dehydroquinase (2), QA-2 = QUTE] though contained within a 3.4 kb DNA sequence in Aspergillus compared to a 5.4 kb sequence in Neurospora. The A. nidulans dehydroquinase (2) gene QUTE has been shown to complement an auxotrophic mutantaro D6 of Escherichia coli lacking biosynthetic dehydroquinase when tested for growth at 30 °C. A mutant of A. nidulans lacking catabolic dehydroquinase (2) and designated qutE208 has been isolated and shown to be tightly linked to the gene cluster, which maps between the ornB and fwA loci in linkage group VIII.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00419960
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  • 6
    Electronic Resource
    Electronic Resource
    Genetical and biochemical aspects of quinate breakdown in the filamentous fungus Aspergillus nidulans (1982)
    Springer
    Biochemical genetics 20 (1982), S. 271-286 
    Details
    ISSN: 1573-4927
    Keywords: Aspergillus nidulans ; gene cluster ; dehydroquinase ; quinate
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract In the ascomycetous fungus Aspergillus nidulans, the expression of two inducible, contiguous or closely linked genes (qutB and qutC) which encode enzymes for quinate breakdown to protocatechuate, appears to be controlled by the product of a tightly linked third gene (qutA). The qut gene cluster locates on chromosome VIII. The catalytic steps required for this conversion are dehydrogenase, dehydroquinase, and dehydratase, and these activities are induced by the presence of quinate in a similar manner. The dehydroquinase enzyme has been purified and shown to be multimeric, consisting of 20–22 identical subunits of approximately 10,000 MW. The enzyme has a pI value of 5.84, a K m of 5×10−4 m, and an amino acid composition that lacks tryptophan and cysteine. The enzyme also cross-reacts with rabbit antibodies raised against Neurospora crassa catabolic dehydroquinase.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00484424
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  • 7
    Electronic Resource
    Electronic Resource
    In vivo overproduction of the pentafunctional arom polypeptide in Aspergillus nidulans affects metabolic flux in the quinate pathway (1991)
    Springer
    Molecular genetics and genomics 227 (1991), S. 187-196 
    Details
    ISSN: 1617-4623
    Keywords: Shikimate pathway ; QUT pathway ; Channelling ; Metabolic flux
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The shikimate pathway and the quinic acid utilisation (QUT) pathway of Aspergillus nidulans and other fungi share the two common metabolic intermediates, 3-dehydroquinic acid (DHQ) and dehydroshikimic acid (DHS), which are interconverted by two isoenzymes, catabolic 3-dehydroquinase, (cDHQase) and biosynthetic dehydroquinase (bDHQase). bDHQase is one of five consecutive enzymatic activities associated with the pentafunctional arom protein encoded by the complex AROM locus, whereas cDHQase is encoded by the single-function QUTE gene, one of seven genes comprising the QUT gene cluster in A. nidulans, which is required for the catabolism of quinate to protocatechuate. We addressed the question of how much (if any) leakage there is of the two common substrates between the two pathways, by increasing the concentration of the arom protein in vivo by means of recombinant DNA technology. We demonstrated that constitutive overproduction of the arom protein by 12-fold in the presence of quinate inhibits germination of conidiospores, but showed that 12-fold quinate-inducible overproduction of arom protein does not have this effect. In addition we showed that a qutE mutant (lacking cDHQase) can grow with quinic acid as sole carbon source when the arom protein is overproduced fivefold. The data are most simply interpreted as simple competition for common substrates by the enzymes of the two pathways and demonstrate that any channelling function of the arom protein in vivo is relatively leaky.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00259670
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  • 8
    Electronic Resource
    Electronic Resource
    Sequence of the Phytophthora infestans glyceraldehyde-3-phosphate dehydrogenase-encoding gene (gpdA) (1992)
    Springer
    Plant molecular biology 18 (1992), S. 1209-1211 
    Details
    ISSN: 1573-5028
    Keywords: gpdA ; P. infestans ; fungal pathogens
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00047730
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  • 9
    Electronic Resource
    Electronic Resource
    Molecular organisation of the quinic acid utilization (QUT) gene cluster in Aspergillus nidulans (1988)
    Springer
    Molecular genetics and genomics 214 (1988), S. 224-231 
    Details
    ISSN: 1617-4623
    Keywords: Quinic acid utilization ; DNA sequence ; Divergent transcription ; Permease ; Upstream activator
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The functional integrity of the QUTB gene (encoding quinate dehydrogenase) has been confirmed by transformation of a qutB mutant strain. The DNA sequence of the contiguous genes QUTD (quinate permease), QUTB and QUTG (function unknown) has been determined and analysed, together with that of QUTE (catabolic 3-dehydroquinase). The QUTB sequence shows significant homology with the shikimate dehydrogenase function of the complex AROM locus of Aspergillus nidulans, and with the QA-3 quinate dehydrogenase and QA-1S (repressor) genes of Neurospora crassa. The QUTD gene shows strong homology with the N. crassa QA-Y gene and QUTG with the QA-X gene. QUTD, QUTB, and QUTG, QUTE form two pairs of divergently transcribed genes, and conserved sequence motifs identified in the two common 5′ non-coding regions show significant homology with UAS GAL and UAS QA sequences of the Saccharomyces cerevisiae and N. crassa Gal and QA systems. In addition, conserved 5′ sequences homologous to the mammalian CAAT box are noted and a previously unreported conserved 22 nucleotide motif is presented.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00337715
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  • 10
    Electronic Resource
    Electronic Resource
    Nucleotide sequence and regulation of expression of the Aspergillus nidulans gdhA gene encoding NADP dependent glutamate dehydrogenase (1989)
    Springer
    Molecular genetics and genomics 218 (1989), S. 105-111 
    Details
    ISSN: 1617-4623
    Keywords: Aspergillus nidulans ; Glutamate dehydrogenase ; Gene structure ; Transcription initiation sites ; Intervening sequences
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The nucleotide sequence of the Aspergillus nidulans gdhA gene encoding NADP linked glutamate dehydrogenase has been determined and Northern blot analysis used to study the regulation of expression of this gene. The gdhA gene is 1485 nucleotides long and, by comparison with the corresponding Neurospora crassa am gene, has two putative introns of 53 nucleotides and a protein encoding region of 1380 nucleotides that codes for an inferred protein of 49.63 kDa which shows regions of homology with glutamate dehydrogenase proteins from a range of organisms. mRNA analysis of wild-type mycelium grown under a variety of conditions shows that: (a) the highest levels are seen with glucose as the carbon source with inorganic nitrogen; and (b) no gdhA mRNA is detectable when cells are transferred to amino acids as sole carbon source, closely matching the observed glutamate dehydrogenase activity levels under identical conditions. The results presented strongly suggest that a good carbon source is a prerequisite for transcription, but the molecular mechanism responsible is unclear.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00330572
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