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Article: Expression of fungal genes involved in penicllin biosynthesis.

Peñalva, M A / Espeso, E / Pérez-Esteban, B / Orejas, M / Fernández-Cañón, J M / Martínez-Blanco, H

World journal of microbiology & biotechnology

2014 Volume 9, Issue 4, Page(s) 461–467

Abstract: Carbon catabolite repression and pH regulation are regulatory circuits with a wide domain of action in the Plectomycetes. Penicillin biosynthesis is one of the pathways which are under their control. The conclusions obtained so far, which are based on ... ...

Abstract	Carbon catabolite repression and pH regulation are regulatory circuits with a wide domain of action in the Plectomycetes. Penicillin biosynthesis is one of the pathways which are under their control. The conclusions obtained so far, which are based on studies of the genetic and molecular regulation of the penicillin pathway of Aspergillus nidulans, would have been much harder to produce using an organism such as Penicillium chrysogenum (the industrial penicillin producer). However, A. nidulans and P. chrysogenum are close in terms of their phylogeny and one can reasonably predict that the conclusions about A. nidulans, which are summarized in this review and which are of unquestionable biotechnological relevance, will be extrapolable to the industrial organism.
Language	English
Publishing date	2014-01-14
Publishing country	Germany
Document type	Journal Article
ZDB-ID	1499109-3
ISSN	1573-0972 ; 0959-3993
ISSN (online)	1573-0972
ISSN	0959-3993
DOI	10.1007/BF00328034
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Article: Characterization of a fungal maleylacetoacetate isomerase gene and identification of its human homologue.

Fernández-Cañón, J M / Peñalva, M A

The Journal of biological chemistry

1998 Volume 273, Issue 1, Page(s) 329–337

Abstract: We have previously used Aspergillus nidulans as a fungal model for human phenylalanine catabolism. This model was crucial for our characterization of the human gene involved in alcaptonuria. We use here an identical approach to characterize at the cDNA ... ...

Abstract	We have previously used Aspergillus nidulans as a fungal model for human phenylalanine catabolism. This model was crucial for our characterization of the human gene involved in alcaptonuria. We use here an identical approach to characterize at the cDNA level the human gene for maleylacetoacetate isomerase (MAAI, EC 5.2.1.2), the only as yet unidentified structural gene of the phenylalanine catabolic pathway. We report here the first characterization of a gene encoding a MAAI enzyme from any organism, the A. nidulans maiA gene. maiA disruption prevents growth on phenylalanine (Phe) and phenylacetate and results in the absence of MAAI activity in vitro and Phe toxicity. The MaiA protein shows strong amino acid sequence identity to glutathione S-transferases and has MAAI activity when expressed in Escherichia coli. maiA is clustered with fahA and hmgA, the genes encoding the two other enzymes of the common part of the Phe/phenylacetate pathways. Based on the high amino acid sequence conservation existing between other homologous A. nidulans and human enzymes of this pathway, we used the MaiA sequence in data base searches to identify human expressed sequence tags encoding its putative homologues. Four such cDNAs were sequenced and shown to be encoded by the same gene. They encode a protein with 45% sequence identity to MaiA, which showed MAAI activity when expressed in E. coli. Human MAAI deficiency would presumably cause tyrosinemia that would be characterized by the absence of succinylacetone, the diagnostic compound resulting from fumarylacetoacetate hydrolase deficiency in humans and fungi. Culture supernatants of an A. nidulans strain disrupted for maiA are succinylacetone-negative but specifically contain cis and/or trans isomers of 2, 4-dioxohept-2-enoic acid. We suggest that this compound(s) might be diagnostic for human MAAI deficiency.
MeSH term(s)	Amino Acid Sequence ; Aspergillus nidulans/enzymology ; Base Sequence ; DNA, Complementary ; Gas Chromatography-Mass Spectrometry ; Humans ; Molecular Sequence Data ; Multigene Family ; Sequence Homology, Amino Acid ; cis-trans-Isomerases/genetics
Chemical Substances	DNA, Complementary ; cis-trans-Isomerases (EC 5.2.-) ; maleylacetoacetate isomerase (EC 5.2.1.2)
Language	English
Publishing date	1998-01-02
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.273.1.329
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Article: Characterization of a fungal maleylacetoacetate isomerase gene and identification of its human homologue

Fernandez-Canon, J.M / Penalva, M.A

Journal of biological chemistry. Jan 2, 1998. v. 273 (1)

1998

Keywords	humans ; Aspergillus nidulellus ; complementary DNA ; isomerases ; nucleotide sequences ; amino acid sequences ; structural genes ; enzyme activity ; recombinant proteins ; amino acid metabolism ; phenylalanine ; phenylacetic acid ; metabolism ; mutants ; monocarboxylic acids
Language	English
Dates of publication	1998-0102
Size	p. 329-337.
Document type	Article
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
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Article: The phenylacetic acid uptake system of Aspergillus nidulans is under a creA-independent model of catabolic repression which seems to be mediated by acetyl-CoA.

Fernández-Cañón, J M / Luengo, J M

The Journal of antibiotics

1997 Volume 50, Issue 1, Page(s) 45–52

Abstract: The filamentous fungus Aspergillus nidulans is able to grow on phenylacetic acid (PhAc) as the sole carbon source and has a highly specific phenylacetic acid transport system mediating the uptake of this aromatic compound. This transport system is also ... ...

Abstract	The filamentous fungus Aspergillus nidulans is able to grow on phenylacetic acid (PhAc) as the sole carbon source and has a highly specific phenylacetic acid transport system mediating the uptake of this aromatic compound. This transport system is also able to transport some phenoxyacetic acid (PhOAc), although less efficiently. Maximal uptake rates were observed at 37 degrees C in 50 mM phosphate buffer (pH 7.0). Under these conditions, uptake was linear for at least 1 minute, with K(m) values for PhAc and PhOAc of 74 and 425 microM, respectively. The PhAc transport system is strongly induced by PhAc and, to a lesser extent by PhOAc and other phenyl derivatives. The utilization of glucose (and other sugars), glycerol or acetate results in a substantially reduced uptake. This negative effect caused by certain carbon sources is independent of the creA gene, the regulatory gene mediating carbon catabolite repression. Negative regulation by acetate is prevented by a loss-of-function mutation in the gene encoding acetyl-CoA synthetase, strongly suggesting that this regulation is mediated by the intracellular pool of acetyl-CoA.
MeSH term(s)	Acetic Acid/pharmacology ; Acetyl Coenzyme A/physiology ; Aspergillus nidulans/metabolism ; Biological Transport ; Fungal Proteins/physiology ; Phenylacetates/metabolism ; Repressor Proteins/physiology
Chemical Substances	Fungal Proteins ; Phenylacetates ; Repressor Proteins ; CreA protein, Aspergillus nidulans (144516-87-0) ; Acetyl Coenzyme A (72-89-9) ; phenylacetic acid (ER5I1W795A) ; Acetic Acid (Q40Q9N063P)
Language	English
Publishing date	1997-01
Publishing country	Japan
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	390800-8
ISSN	1881-1469 ; 0021-8820 ; 0368-3532
ISSN (online)	1881-1469
ISSN	0021-8820 ; 0368-3532
DOI	10.7164/antibiotics.50.45
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Article: Spectrophotometric determination of homogentisate using Aspergillus nidulans homogentisate dioxygenase.

Fernández-Cañón, J M / Peñalva, M A

Analytical biochemistry

1997 Volume 245, Issue 2, Page(s) 218–221

Abstract: The presence of homogentisic acid (HGA) in urine is diagnostic for alkaptonuria, a classical example of a biochemical lesion resulting from a single gene trait. We describe here simple culture conditions which induce the synthesis of high levels of ... ...

Abstract	The presence of homogentisic acid (HGA) in urine is diagnostic for alkaptonuria, a classical example of a biochemical lesion resulting from a single gene trait. We describe here simple culture conditions which induce the synthesis of high levels of homogentisate dioxygenase activity in mycelia from the filamentous ascomycete Aspergillus nidulans. Crude enzyme preparations, showing an apparent Km of 9 microM for homogentisate and an optimal pH of 6.5-7.0 are rather stable and highly specific for homogentisate. Thus, the reaction is not competed by a large molar excess of a number of substrate structural analogues, including phenylacetate and its 2-, 3-, and 4-hydroxy derivatives, phenylalanine, tyrosine, phenylpyruvate, and gentisate. We demonstrate how this enzyme preparation can be used in sensitive, spectrophotometric enzymatic determination of this compound. The accuracy is almost indistinguishable from that obtained by HPLC. The method can be applied to routine determination of homogentisate in human urine. A 1-liter culture of the mold provides sufficient enzyme activity for 1500 enzymatic assays.
MeSH term(s)	Alkaptonuria/metabolism ; Aspergillus nidulans/drug effects ; Aspergillus nidulans/enzymology ; Aspergillus nidulans/metabolism ; Chromatography, High Pressure Liquid ; Dioxygenases ; Female ; Homogentisate 1,2-Dioxygenase ; Homogentisic Acid/analysis ; Homogentisic Acid/metabolism ; Homogentisic Acid/urine ; Humans ; Male ; Oxygenases/genetics ; Oxygenases/metabolism ; Phenylacetates/metabolism ; Phenylacetates/pharmacology ; Sensitivity and Specificity ; Spectrophotometry/methods
Chemical Substances	Phenylacetates ; Oxygenases (EC 1.13.-) ; Dioxygenases (EC 1.13.11.-) ; Homogentisate 1,2-Dioxygenase (EC 1.13.11.5) ; phenylacetic acid (ER5I1W795A) ; Homogentisic Acid (NP8UE6VF08)
Language	English
Publishing date	1997-02-15
Publishing country	United States
Document type	Journal Article
ZDB-ID	1110-1
ISSN	1096-0309 ; 0003-2697
ISSN (online)	1096-0309
ISSN	0003-2697
DOI	10.1006/abio.1996.9957
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Article: Molecular characterization of a gene encoding a homogentisate dioxygenase from Aspergillus nidulans and identification of its human and plant homologues.

Fernández-Cañón, J M / Peñalva, M A

The Journal of biological chemistry

1995 Volume 270, Issue 36, Page(s) 21199–21205

Abstract: We report here the first characterization of a gene encoding a homogentisate dioxygenase, the Aspergillus nidulans hmgA gene. The HmgA protein catalyzes an essential step in phenylalanine catabolism, and disruption of the gene results in accumulation of ... ...

Abstract	We report here the first characterization of a gene encoding a homogentisate dioxygenase, the Aspergillus nidulans hmgA gene. The HmgA protein catalyzes an essential step in phenylalanine catabolism, and disruption of the gene results in accumulation of homogentisate in broths containing phenylalanine. hmgA putatively encodes a 448-residue polypeptide (Mr = 50,168) containing 21 histidine and 23 tyrosine residues. This polypeptide has been expressed in Escherichia coli as a fusion to glutathione S-transferase, and the affinity-purified protein has homogentisate dioxygenase activity. A. nidulans, an ascomycete amenable to classical and reverse genetic analysis, is a good metabolic model to study inborn errors in human Phe catabolism. One such disease, alkaptonuria, was the first human inborn error recognized (Garrod, A. E. (1902) Lancet 2, 1616-1620) and results from loss of homogentisate dioxygenase. Here we take advantage of the high degree of conservation between the amino acid sequences of the fungal and higher eukaryote enzymes of this pathway to identify expressed sequence tags encoding human and plant homologues of HmgA. This is a significant advance in characterizing the genetic defect(s) of alkaptonuria and illustrates the usefulness of our fungal model.
MeSH term(s)	Amino Acid Sequence ; Aspergillus nidulans/genetics ; Aspergillus nidulans/growth & development ; Aspergillus nidulans/metabolism ; Base Sequence ; Cloning, Molecular ; DNA, Complementary ; Dioxygenases ; Genes, Fungal ; Genes, Plant ; Homogentisate 1,2-Dioxygenase ; Homogentisic Acid/metabolism ; Humans ; Molecular Sequence Data ; Oxygenases/genetics ; Pigments, Biological/metabolism ; Sequence Homology, Amino Acid
Chemical Substances	DNA, Complementary ; Pigments, Biological ; Oxygenases (EC 1.13.-) ; Dioxygenases (EC 1.13.11.-) ; Homogentisate 1,2-Dioxygenase (EC 1.13.11.5) ; Homogentisic Acid (NP8UE6VF08)
Language	English
Publishing date	1995-09-08
Publishing country	United States
Document type	Journal Article
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.270.36.21199
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Article: Fungal metabolic model for human type I hereditary tyrosinaemia.

Fernández-Cañón, J M / Peñalva, M A

Proceedings of the National Academy of Sciences of the United States of America

1995 Volume 92, Issue 20, Page(s) 9132–9136

Abstract: Type I hereditary tyrosinaemia (HT1) is a severe human inborn disease resulting from loss of fumaryl-acetoacetate hydrolase (Fah). Homozygous disruption of the gene encoding Fah in mice causes neonatal lethality, seriously limiting use of this animal as ... ...

Abstract	Type I hereditary tyrosinaemia (HT1) is a severe human inborn disease resulting from loss of fumaryl-acetoacetate hydrolase (Fah). Homozygous disruption of the gene encoding Fah in mice causes neonatal lethality, seriously limiting use of this animal as a model. We report here that fahA, the gene encoding Fah in the fungus Aspergillus nidulans, encodes a polypeptide showing 47.1% identity to its human homologue, fahA disruption results in secretion of succinylacetone (a diagnostic compound for human type I tyrosinaemia) and phenylalanine toxicity. We have isolated spontaneous suppressor mutations preventing this toxicity, presumably representing loss-of-function mutations in genes acting upstream of fahA in the phenylalanine catabolic pathway. Analysis of a class of these mutations demonstrates that loss of homogentisate dioxygenase (leading to alkaptonuria in humans) prevents the effects of a Fah deficiency. Our results strongly suggest human homogentisate dioxygenase as a target for HT1 therapy and illustrate the usefulness of this fungus as an alternative to animal models for certain aspects of human metabolic diseases.
MeSH term(s)	Amino Acid Metabolism, Inborn Errors/genetics ; Amino Acid Sequence ; Aspergillus nidulans/genetics ; Aspergillus nidulans/metabolism ; Chromatography, High Pressure Liquid ; Dioxygenases ; Enzyme Inhibitors/analysis ; Gas Chromatography-Mass Spectrometry ; Genes, Fungal ; Heptanoates/analysis ; Heptanoates/metabolism ; Homogentisate 1,2-Dioxygenase ; Humans ; Hydrolases/biosynthesis ; Hydrolases/genetics ; Models, Genetic ; Molecular Sequence Data ; Mutation ; Open Reading Frames ; Oxygenases/analysis ; Oxygenases/genetics ; Oxygenases/metabolism ; Phenylalanine/metabolism ; Restriction Mapping ; Sequence Homology, Amino Acid ; Tyrosine/metabolism
Chemical Substances	Enzyme Inhibitors ; Heptanoates ; Tyrosine (42HK56048U) ; Phenylalanine (47E5O17Y3R) ; succinylacetone (51568-18-4) ; Oxygenases (EC 1.13.-) ; Dioxygenases (EC 1.13.11.-) ; Homogentisate 1,2-Dioxygenase (EC 1.13.11.5) ; Hydrolases (EC 3.-) ; fumarylacetoacetase (EC 3.7.1.2)
Language	English
Publishing date	1995-09-26
Publishing country	United States
Document type	Comparative Study ; Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	209104-5
ISSN	1091-6490 ; 0027-8424
ISSN (online)	1091-6490
ISSN	0027-8424
DOI	10.1073/pnas.92.20.9132
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Article: Overexpression of two penicillin structural genes in Aspergillus nidulans.

Fernández-Cañón, J M / Peñalva, M A

Molecular & general genetics : MGG

1995 Volume 246, Issue 1, Page(s) 110–118

Abstract: We have placed two different penicillin structural genes from Aspergillus nidulans, ipnA (encoding isopenicillin N synthetase, IPNS) and acyA (encoding acyl-CoA:6-aminopenicillanic acid acyltransferase, AAT), under the control of the strong alcA promoter ...

Abstract	We have placed two different penicillin structural genes from Aspergillus nidulans, ipnA (encoding isopenicillin N synthetase, IPNS) and acyA (encoding acyl-CoA:6-aminopenicillanic acid acyltransferase, AAT), under the control of the strong alcA promoter [alcA(p)]. Single copies of these transcriptional fusions were targeted to the same chromosomal location and conditions have been worked out which simultaneously allow induction of the alcA(p) and support penicillin biosynthesis. Transcriptional induction of the chimeric genes alcA(p)::ipnA or alcA(p)::acyA(cdna) in the relevant recombinant strains results in 10-fold higher levels of the ipnA or acyA transcripts than those resulting from transcription of the corresponding endogenous genes. This increase causes a 40-fold rise in IPNS activity or a 8-fold rise in AAT activity. Despite this rise in enzyme levels, forced expression of the ipnA gene results in only a modest increase in levels of exported penicillin, whereas forced expression of the acyA gene reduces penicillin production, showing that neither of these enzymes is rate-limiting for penicillin biosynthesis in A. nidulans. A genomic version of the alcA(p)::acyA fusion in which the acyA gene is interrupted by three small introns, is inducible by threonine to a lesser extent (as determined by both acyA mRNA levels and AAT enzyme levels) than the corresponding cDNA version, suggesting that processing of the introns present in the primary transcript may limit acyA expression.
MeSH term(s)	Acyltransferases/genetics ; Alcohol Dehydrogenase/genetics ; Aspergillus nidulans/enzymology ; Aspergillus nidulans/genetics ; DNA, Fungal ; DNA, Recombinant ; Enzyme Induction ; Fungal Proteins/genetics ; Gene Expression Regulation, Fungal ; Genes, Fungal ; Oxidoreductases/genetics ; Penicillin-Binding Proteins ; Penicillins/biosynthesis ; Promoter Regions, Genetic ; Recombinant Fusion Proteins/biosynthesis ; Restriction Mapping ; Transcription, Genetic
Chemical Substances	DNA, Fungal ; DNA, Recombinant ; Fungal Proteins ; Penicillin-Binding Proteins ; Penicillins ; Recombinant Fusion Proteins ; Oxidoreductases (EC 1.-) ; Alcohol Dehydrogenase (EC 1.1.1.1) ; isopenicillin N synthetase (EC 1.21.3.1) ; Acyltransferases (EC 2.3.-) ; acyl-CoA-6-aminopenicillanic acid acyltransferase (EC 2.3.1.-)
Language	English
Publishing date	1995-01-06
Publishing country	Germany
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2169-6
ISSN	1432-1874 ; 1617-4623 ; 0026-8925
ISSN (online)	1432-1874 ; 1617-4623
ISSN	0026-8925
DOI	10.1007/bf00290139
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Article: Disruption of phacA, an Aspergillus nidulans gene encoding a novel cytochrome P450 monooxygenase catalyzing phenylacetate 2-hydroxylation, results in penicillin overproduction.

Mingot, J M / Peñalva, M A / Fernández-Cañón, J M

The Journal of biological chemistry

1999 Volume 274, Issue 21, Page(s) 14545–14550

Abstract: Aspergillus nidulans utilizes phenylacetate as a carbon source via homogentisate, which is degraded to fumarate and acetoacetate. Mutational evidence strongly suggested that phenylacetate is converted to homogentisate through two sequential hydroxylating ...

Abstract	Aspergillus nidulans utilizes phenylacetate as a carbon source via homogentisate, which is degraded to fumarate and acetoacetate. Mutational evidence strongly suggested that phenylacetate is converted to homogentisate through two sequential hydroxylating reactions in positions 2 and 5 of the aromatic ring. Using cDNA substraction techniques, we have characterized a gene, denoted phacA, whose transcription is strongly induced by phenylacetate and which putatively encodes a cytochrome P450 protein. A disrupted phacA strain does not grow on phenylacetate but grows on 2-hydroxy- or 2, 5-dihydroxyphenylacetate. Microsomal extracts of the disrupted strain are deficient in the NADPH-dependent conversion of phenylacetate to 2-hydroxyphenylacetate. We conclude that PhacA catalyzes the ortho-hydroxylation of phenylacetate, the first step of A. nidulans phenylacetate catabolism. The involvement of a P450 enzyme in the ortho-hydroxylation of a monoaromatic compound has no precedent. In addition, PhacA shows substantial sequence divergence with known cytochromes P450 and defines a new family of these enzymes, suggesting that saprophytic fungi may represent a source of novel cytochromes P450. Phenylacetate is a precursor for benzylpenicillin production. phacA disruption increases penicillin production 3-5-fold, indicating that catabolism competes with antibiotic biosynthesis for phenylacetate and strongly suggesting strategies for Penicillium chrysogenum strain improvement by reverse genetics.
MeSH term(s)	Aspergillus nidulans/enzymology ; Cytochrome P-450 Enzyme System/genetics ; Cytochrome P-450 Enzyme System/physiology ; Fungal Proteins ; Gene Expression ; Hydroxylation ; Microsomes ; Molecular Sequence Data ; Oxygenases/genetics ; Penicillins/biosynthesis ; Phenotype ; Phenylacetates/metabolism
Chemical Substances	Fungal Proteins ; Penicillins ; Phenylacetates ; Cytochrome P-450 Enzyme System (9035-51-2) ; Oxygenases (EC 1.13.-) ; phenylacetate 2-hydroxylase (EC 1.14.13.-) ; phenylacetic acid (ER5I1W795A)
Language	English
Publishing date	1999-05-21
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.274.21.14545
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Article: Identification of the mutation in the alkaptonuria mouse model. Mutations in brief no. 216. Online.

Manning, K / Fernández-Cañón, J M / Montagutelli, X / Grompe, M

Human mutation

1999 Volume 13, Issue 2, Page(s) 171

Abstract: Alkaptonuria (aku), an inborn error of metabolism caused by the loss of homogentisate 1,2-dioxygenase (HGD), has been described in a mouse model created by ethylnitrosourea mutagenesis but the mutation in these mice has not previously been identified. We ...

Abstract	Alkaptonuria (aku), an inborn error of metabolism caused by the loss of homogentisate 1,2-dioxygenase (HGD), has been described in a mouse model created by ethylnitrosourea mutagenesis but the mutation in these mice has not previously been identified. We used RT-PCR to amplify the Hgd cDNA from Hgd(aku)/Hgd(aku) mice. Two products shorter than the wild-type product were amplified. Restriction mapping and DNA sequencing were then used to identify the Hgd(aku) mouse mutation, found to be a single base change in a splice donor consensus sequence, causing exon skipping and frame-shifted products. This base change allowed us to create a non-radioactive genotyping assay for this allele.
MeSH term(s)	Alkaptonuria/genetics ; Animals ; Dioxygenases ; Disease Models, Animal ; Homogentisate 1,2-Dioxygenase ; Mice ; Mice, Inbred Strains ; Mutation/genetics ; Oxygenases/deficiency ; Oxygenases/genetics ; Reverse Transcriptase Polymerase Chain Reaction/methods
Chemical Substances	Oxygenases (EC 1.13.-) ; Dioxygenases (EC 1.13.11.-) ; Homogentisate 1,2-Dioxygenase (EC 1.13.11.5)
Language	English
Publishing date	1999
Publishing country	United States
Document type	Journal Article ; Research Support, U.S. Gov't, P.H.S.
ZDB-ID	1126646-6
ISSN	1098-1004 ; 1059-7794
ISSN (online)	1098-1004
ISSN	1059-7794
DOI	10.1002/(SICI)1098-1004(1999)13:2<171::AID-HUMU15>3.0.CO;2-W
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