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PubMed2002

Metal-ligand interplay in blue copper proteins studied by 1H NMR spectroscopy: Cu(II)-pseudoazurin and Cu(II)-rusticyanin.

The blue copper proteins (BCPs), pseudoazurin from Achromobacter cycloclastes and rusticyanin from Thiobacillus ferrooxidans, have been investigated by (1)H NMR at a magnetic field of 18.8 T. Hyperfine shifts of the protons belonging to the coordinated ligands have been identified by exchange spectroscopy, including the indirect detection for those resonances that cannot be directly observed (the beta-CH(2) of the Cys ligand, and the NH amide hydrogen bonded to the S(gamma)(Cys) atom). These data reveal that the Cu(II)-Cys interaction in pseudoazurin and rusticyanin is weakened compared to that in classic blue sites (plastocyanin and azurin). This weakening is not induced by a stronger interaction with the axial ligand, as found in stellacyanin, but might be determined by the protein folding around the metal site. The average chemical shift of the beta-CH(2) Cys ligand in all BCPs can be correlated to geometric factors of the metal site (the Cu-S(gamma)(Cys) distance and the angle between the CuN(His)N(His) plane and the Cu-S(gamma)(Cys) vector). It is concluded that the degree of tetragonal distortion is not necessarily related to the strength of the Cu(II)-S(gamma)(Cys) bond. The copper-His interaction is similar in all BCPs, even for the solvent-exposed His ligand. It is proposed that the copper xy magnetic axes in blue sites are determined by subtle geometrical differences, particularly the orientation of the His ligands. Finally, the observed chemical shifts for beta-CH(2) Cys and Ser NH protons in rusticyanin suggest that a less negative charge at the sulfur atom could contribute to the high redox potential (680 mV) of this protein.

Alcaligenes↗
PubMed1970

Biosynthesis of ubiquinone in non-photosynthetic gram-negative bacteria.

1. The polyprenylphenol and quinone complements of the non-photosynthetic Gram-negative bacteria, Pseudomonas ovalis Chester, Proteus mirabilis and ;Vibrio O1' (Moraxella sp.), were investigated. 2. Ps. ovalis Chester and Prot. mirabilis were shown to contain 2-polyprenylphenols, 6-methoxy-2-polyprenylphenols, 6-methoxy-2-polyprenyl-1,4-benzoquinones, 5-demethoxyubiquinones, ubiquinones, an unidentified 1,4-benzoquinone [2-polyprenyl-1,4-benzoquinone (?)] and ;epoxyubiquinones'. ;Vibrio O1' was shown to contain only 5-demethoxyubiquinones, ubiquinones and ;epoxyubiquinones'. 3. It was established that in Ps. ovalis Chester 2-polyprenylphenols, 6-methoxy-2-polyprenylphenols, 6-methoxy-2-polyprenyl-1,4-benzoquinones, 5-demethoxyubiquinones and 2-polyprenyl-1,4-benzoquinones (?) are precursors of ubiquinones. 4. Intracellular distribution studies showed that in Ps. ovalis Chester ubiquinone and its prenylated precursors are localized entirely on the protoplast membrane. 5. Investigations into the oxygen requirements for ubiquinone biosynthesis by Ps. ovalis Chester showed that the organism could not convert p-hydroxybenzoic acid into ubiquinone in the absence of oxygen, although it could convert a limited amount into 2-polyprenylphenols. 6. Attempts were made to prepare cell-free preparations capable of synthesizing ubiquinone. Purified protoplast membranes of Ps. ovalis Chester were found to be incapable of carrying out this synthesis, even when supplemented with cytoplasm. With crushed-cell preparations of Ps. ovalis Chester, organism PC4 (Achromobacter sp.) and Escherichia coli, synthesis was observed, although this was attributable in part to a small number of intact cells present in the preparations.

Alcaligenes↗
PubMed1972

Microbial metabolism of pyridinium compounds. Metabolism of 4-carboxy-1-methylpyridinium chloride, a photolytic product of paraquat.

1. A bacterium, Achromobacter D, isolated from garden soil by elective culture, utilized N-methylisonicotinic acid (4-carboxy-1-methylpyridinium chloride) as sole carbon source. 2. Extracts of N-methylisonicotinate-grown cells oxidized this substrate only after supplementation with a source of nicotinamide nucleotides and then consumed 1 mol of O(2) and released 1 mol of CO(2)/mol of N-methylisonicotinate supplied. 3. The N-methyl group of the substrate was released as methylamine whereas the five C atoms of the pyridine ring were accounted for as succinate and formate. The CO(2) evolved by extracts was believed to derive from the carboxyl group on C-4 of the heterocyclic ring. 4. The immediate precursor of the succinate end-product was succinic semialdehyde; the inducible nature of succinic semialdehyde dehydrogenase in N-methylisonicotinate-grown cells supported this finding. 5. There was no evidence for monohydroxylation of the ring, but the time sequence of the appearance of the end-products indicated that the oxygen-requiring, NADH-requiring and decarboxylation steps clearly preceded the formation of methylamine and succinate. 6. The results are consistent with the oxidative cleavage of a partially reduced heterocyclic ring followed by several hydrolytic and dehydrogenase steps resulting in the appearance of the end-products.

Alcaligenes↗
PubMed1972

Microbial metabolism of pyridinium compounds. Radioisotope studies of the metabolic fat of 4-carboxy-1-methylpyridinium chloride.

Extracts of Achromobacter D formed CO(2), methylamine, succinate and formate as metabolic end-products from N-methylisonicotinic acid (4-carboxy-1-methylpyridinium chloride). The origin of the CO(2) in the 4-carboxyl group and of the methylamine in the N-methyl group of N-methylisonicotinate was demonstrated with carboxyl-(14)C- and N-Me-(14)C-labelled substrates respectively. The carbon skeletons of formate and succinate were shown to arise from the C-2 and the C-3-C-6 atoms of the heterocyclic ring respectively by using N-methyl[2,3-(14)C(2)]isonicotinate. This result is consistent with ring cleavage by the organism between C-2 and C-3.

Alcaligenes↗
PubMed1972

Microbial metabolism of the pyridine ring. Formation of pyridinediols (dihydroxypyridines) as intermediates in the degradation of pyridine compounds by micro-organisms.

1. Several species of micro-organisms that were capable of utilizing pyridine compounds as carbon and energy source were isolated from soil and sewage. Compounds degraded included pyridine and the three isomeric hydroxypyridines. 2. Suitable modifications of the cultural conditions led to the accumulation of pyridinediols (dihydroxypyridines), which were isolated and characterized. 3. Three species of Achromobacter produced pyridine-2,5-diol from 2- or 3-hydroxypyridine whereas an uncommon Agrobacterium sp. (N.C.I.B. 10413) produced pyridine-3,4-diol from 4-hydroxypyridine. 4. On the basis of chemical isolation, induction of the necessary enzymes in washed suspensions and the substrate specificity exhibited by the isolated bacteria, the initial transformations proposed are: 2-hydroxypyridine --> pyridine-2,5-diol; 3-hydroxypyridine --> pyridine-2,5-diol and 4-hydroxypyridine --> pyridine-3,4-diol. 5. A selected pyridine-utilizer, Nocardia Z1, did not produce any detectable hydroxy derivative from pyridine, but carried out a slow oxidation of 3-hydroxypyridine to pyridine-2,3-diol and pyridine-3,4-diol. These diols were not further metabolized. 6. Addition of the isomeric hydroxypyridines to a model hydroxylating system resulted in the formation of those diols predicted by theory.

Alcaligenes↗
PubMed1973

Microbial metabolism of amino alcohols. 1-Aminopropan-2-ol and ethanolamine metabolism via propionaldehyde and acetaldehyde in a species of Pseudomonas.

1. Growth and manometric experiments showed that a Pseudomonas sp. P6 (N.C.I.B. 10431), formerly known as Achromobacter sp. P6, was capable of growth on both stereoisomers of 1-aminopropan-2-ol, and supported the hypothesis that assimilation involved metabolism to propionaldehyde, propionate and possibly 2-hydroxyglutarate. A number of alternative intermediary metabolites were ruled out. 2. Accumulation of propionaldehyde from 1-aminopropan-2-ol by intact cells occurred only during active growth, was transitory and was accompanied by morphological changes in the pseudomonad. 3. Enzymic and radioactive tracer evidence showed that 1-aminopropan-2-ol O-phosphate was the intermediate between amino alcohol and aldehyde. The operation of an inducibly formed ATP-amino alcohol phosphotransferase was established by measuring substrate disappearance, ADP formation and amino alcohol O-phosphate formation. This novel kinase had two activity peaks at about pH7 and 9. It acted on both l- and d-isomers of 1-aminopropan-2-ol, and also on l-threonine and ethanolamine, but had only low activity towards choline. The enzyme was partially purified by ion-exchange chromatography. 4. An amino alcohol O-phosphate phospho-lyase (deaminating) produced propionaldehyde from dl- and d-1-aminopropan-2-ol O-phosphate, and also formed acetaldehyde less rapidly from ethanolamine O-phosphate. It had optimum activity at about pH8 in Tris-HCl buffers. The enzyme was partially purified and evidence was obtained that a single enzyme was responsible for both activities. Apparent K(m) values for the substrates were determined. Activity was inhibited by dl-threonine O-phosphate, dl-serine O-phosphate, choline O-phosphate and P(i). Enzyme formation was induced by growth with either amino alcohol substrate. 5. Radioactive tracer experiments with dl-1-amino[3-(14)C]propan-2-ol confirmed the operation of the amino alcohol kinase and demonstrated coupling with the phospho-lyase enzyme in vitro to produce [(14)C]-propionaldehyde. 6. An aldehyde dehydrogenase, found in extracts of the pseudomonad after growth on 1-aminopropan-2-ol, was characterized and concluded to be responsible for propionaldehyde and acetaldehyde oxidation. The enzyme was inactive with methylglyoxal. 7. Propionate and acetate were concluded to be metabolized via propionyl-CoA and acetyl-CoA, and studies were made of a CoA ester synthase found in extracts. 8. Studies of a strain of Pseudomonas putida N.C.I.B. 10558 suggested that 1-aminopropan-2-ols were metabolized via their O-phosphates, propionaldehyde and propionate. Amino alcohol kinase activity was detected and extracts contained a phospho-lyase showing higher activity with the 1-aminopropan-2-ol O-phosphate than with ethanolamine O-phosphate.

1-Propanol↗
PubMed1979

Differences in the degradation of native collagen by two microbial collagenases.

The early stages of degradation of native collagen by two bacterial collagenases were studied by electron microscopy and by automatic Edman degradation. The purified collagenase from Clostridium histolyticum was shown to cleave native collagen at several sites, but not progressively from the N-terminus, as had been previously suggested. The homogeneous collagenase from Achromobacter iophagus cleaves native collagen preferentially at two sites corresponding to the interbands 33-34 and 41-42. The latter lies within the region cleaved by the eukaryotic collagenases.

Alcaligenes↗
PubMed2003

Sulphoacetaldehyde acetyltransferase yields acetyl phosphate: purification from Alcaligenes defragrans and gene clusters in taurine degradation.

The facultatively anaerobic bacterium Alcaligenes defragrans NKNTAU was found to oxidize taurine (2-aminoethanesulphonate) with nitrate as the terminal electron acceptor. Taurine was transaminated to 2-sulphoacetaldehyde. This was not converted into sulphite and acetate by a "sulphoacetaldehyde sulpho-lyase" (EC 4.4.1.12), but into sulphite and acetyl phosphate, which was identified by three methods. The enzyme, which required the addition of phosphate, thiamin diphosphate and Mg(2+) ions for activity, was renamed sulphoacetaldehyde acetyltransferase (Xsc; EC 2.3.1.-). Inducible Xsc was expressed at high levels, and a three-step 11-fold purification yielded an essentially homogeneous soluble protein, which was a homotetramer in its native form; the molecular mass of the subunit was found to be between about 63 kDa (SDS/PAGE) and 65.3 kDa (matrix-assisted laser-desorption ionization-time-of-flight MS). The N-terminal and two internal amino acid sequences were determined, and PCR primers were generated. The xsc gene was amplified and sequenced; the derived molecular mass of the processed protein was 65.0 kDa. The downstream gene presumably encoded the inducible phosphate acetyltransferase (Pta) found in crude extracts. The desulphonative enzymes ("EC 4.4.1.12") from Achromobacter xylosoxidans NCIMB 10751 and Desulfonispora thiosulfatigenes GKNTAU were shown to be Xscs. We detected at least three subclasses of xsc in Proteobacteria and in Gram-positive bacteria, and they comprised a distinct group within the acetohydroxyacid synthase supergene family. Genome sequencing data revealed xsc genes in Burkholderia fungorum (80% sequence identity) and Sinorhizobium meliloti (61%) with closely linked pta genes. Different patterns of regulation for the transport and dissimilation of taurine were hypothesized for S. meliloti and B. fungorum.

Acetaldehyde↗
PubMed1991

Cysteine-86 is not needed for the enzymic activity of glutathione S-transferase 3-3.

Recombinant glutathione S-transferase 3-3 expressed in Spodoptera frugiperda (SF9) cells with the use of a baculovirus expression system was modified with 1 mM-iodoacetamide. Amino acid analysis indicated that 0.79 +/- 0.15 cysteine residue was modified per enzyme subunit. The S-carbaminomethylated protein retains the GSH-conjugating activity. Glutathione S-transferase 3-3 modified with iodo[14C]acetamide was digested with Achromobacter proteinase I and the resulting peptides were separated by h.p.l.c. The modified peptides were pooled and further digested with Staphylococcus aureus V8 proteinase. Isotope-labelled peptides were isolated and collected for N-terminal sequence analysis. By this procedure, cysteine-86 was identified as the major S-carbaminomethylated residue. Verification of this findings came from the use of site-directed mutagenesis in which this cysteine was replaced by serine (C86S mutant). The C86S mutant is enzymically active. Therefore cysteine-86 is not needed for the conjugation of GSH with electrophilic compounds on glutathione S-transferase 3-3.

Amino Acid Sequence↗
PubMed1992

Cloning and expression of a chick liver glutathione S-transferase CL 3 subunit with the use of a baculovirus expression system.

Glutathione S-transferase CL 3 subunits purified from 1-day-old-chick livers were digested with Achromobacter proteinase I and the resulting fragments were isolated for amino acid sequence analysis. An oligonucleotide probe was constructed accordingly for cDNA library screening. A cDNA clone of 1342 bases, pGCL301, encoding a protein of 26209 Da was isolated and sequenced. Including conservative substitutions, this protein has 75-79% sequence similarity to other Alpha family glutathione S-transferases. The coding sequence of pGCL301 was inserted into a baculovirus vector for infection of Spodoptera frugiperda (SF9) cells. The expressed protein has a high relative activity with ethacrynic acid (47% of the specific activity with 1-chloro-2,4-dinitrobenzene). The enzyme has a subunit molecular mass of 25.2 +/- 1.2 kDa (by SDS/PAGE), a pI of 9.45 and an absorption coefficient A1%1cm of 13.0 +/- 0.5 at 280 nm.

Amino Acid Sequence↗
PubMed1994

Delta 3, delta 2-enoyl-CoA isomerase is the protein that copurifies with human glutathione S-transferases from S-hexylglutathione affinity matrices.

An unidentified 30 kDa protein frequently copurifies with human glutathione S-transferases from S-hexyl-glutathione affinity matrices. Application of two-step sequential affinity chromatographic methods yielded a homogeneous preparation of that protein from human liver specimens. The protein was digested with Achromobacter protease I, and sequences of peptides resolved by h.p.l.c. showed a high degree of identity with those of rat mitochondrial delta 3, delta 2-enoyl-CoA isomerase. The human protein also exhibited catalytic activity with delta 3-cis-octenyl CoA as a substrate. Thus it is identified as liver delta 3, delta 2-enoyl-CoA isomerase.

Adult↗
PubMed1995

Amino acid sequencing, molecular cloning and modelling of the chick liver class-theta glutathione S-transferase CL1.

Glutathione S-transferase CL1-2 heterodimers purified from 1-day-old chick livers were digested with Achromobacter proteinase I. The resulting fragments were separated for amino acid sequence analysis. Oligonucleotide probes were constructed based on sequence similarity to class-Theta glutathione S-transferases for PCR using a chicken liver cDNA library as template. A full-length clone (1725 bp) encoding a polypeptide comprising 261 amino acids was isolated. Including conservative substitutions, this protein has 70-73% sequence similarity with other mammalian class-Theta glutathione S-transferases. Based on known X-ray crystal structures of class-Alpha, -Mu and -Pi glutathione S-transferases, a model is constructed for the N-terminal 232 residues of CL1.

Amino Acid Sequence↗
PubMed1998

Amino acid sequence of glutathione S-transferase rGSTM5* from rat testis.

Glutathione S-transferase rGSTM5* was isolated from rat testis with a combination of glutathione affinity column and reverse-phase column chromatography. The protein was digested with Achromobacter protease I or endoproteinase Arg-C. The peptide fragments were isolated for electrospray MS and N-terminal peptide sequencing analyses. The primary amino acid sequence of rGSTM5* comprises 217 residues and has a calculated average molecular mass of 25495.3 Da. The result is identical to that obtained for rGSTM5* with liquid chromatography-MS from a mixture of rat testicular GSTs. Therefore, rGSTM5* has not been post-translationally modified.

Amino Acid Sequence↗
PubMed2001

Plastid-expressed 5-enolpyruvylshikimate-3-phosphate synthase genes provide high level glyphosate tolerance in tobacco.

Plastid transformation (transplastomic) technology has several potential advantages for biotechnological applications including the use of unmodified prokaryotic genes for engineering, potential high-level gene expression and gene containment due to maternal inheritance in most crop plants. However, the efficacy of a plastid-encoded trait may change depending on plastid number and tissue type. We report a feasibility study in tobacco plastids to achieve high-level herbicide resistance in both vegetative tissues and reproductive organs. We chose to test glyphosate resistance via over-expression in plastids of tolerant forms of 5-enolpyruvylshikimate-3-phosphate synthase (EPSPS). Immunological, enzymatic and whole-plant assays were used to prove the efficacy of three different prokaryotic (Achromobacter, Agrobacterium and Bacillus) EPSPS genes. Using the Agrobacterium strain CP4 EPSPS as a model we identified translational control sequences that direct a 10,000-fold range of protein accumulation (to >10% total soluble protein in leaves). Plastid-expressed EPSPS could provide very high levels of glyphosate resistance, although levels of resistance in vegetative and reproductive tissues differed depending on EPSPS accumulation levels, and correlated to the plastid abundance in these tissues. Paradoxically, higher levels of plastid-expressed EPSPS protein accumulation were apparently required for efficacy than from a similar nuclear-encoded gene. Nevertheless, the demonstration of high-level glyphosate tolerance in vegetative and reproductive organs using transplastomic technology provides a necessary step for transfer of this technology to other crop species.

3-Phosphoshikimate 1-Carboxyvinyltransferase↗
PubMed2003

The microbiology of glue ear in Australian Aboriginal children.

OBJECTIVE: To study the bacterial cultures of middle ear aspirates from 27 Aboriginal children with otitis media with effusion. METHODS: Standard bacteriological techniques were used to analyse the middle-ear aspirates collected during surgery to insert grommets in 27 Aboriginal children. Swabs of the tympanic membrane were taken for comparison. RESULTS: Forty-five aspirates were collected from 59 myringotomies. Positive cultures were obtained from 19 of these (13 children) with potentially pathogenic organisms identified in 11 children including Staphylococcus, Pseudomonas, Haemophilus influenzae, Moraxella, Achromobacter, Enterobacter and Corynebacterium. CONCLUSION: This is only the second study to look at the bacteria in middle ear effusions in Aboriginal children. Streptococcus pneumoniae was notable in its absence as was found in a previous study.

Age Distribution↗
PubMedDate not supplied

Ochrobactrum anthropi bacteremia.

Ochrobactrum Anthropi (O. anthropi ), formerly known as Achromobacter CDC group Vd, is a gram-negative bacillus that is aerobic, oxidase producing, and nonlactose fermenting. This organism has been found in environmental and hospital water sources and has pathogenic potential in humans. Most reports in the literature of O. anthropi bacteremia are associated with intravenous line infections. We describe a case of bacteremia with O. anthropi in a 33-month-old boy with acute osteomyelitis. O. anthropi bacteremia also has been reported in immunocompromised hosts. Rarely, O. anthropi has been a cause of soft tissue or bone infection.

Alcaligenes↗
PubMed2002

Pulmonary infections in patients with cystic fibrosis.

Cystic fibrosis (CF) is an autosomal-recessive disorder and affects about 60,000 people worldwide. The CF gene, the cystic fibrosis transmembrane conductance regulator (CFTR), was found in 1989 and over 800 mutations have been sequenced. Although our understanding of the pathophysiology of CF has increased, pulmonary infections remain the major cause of morbidity and mortality. During the first decade of life, Staphylococcus aureus and nontypable Haemophilus influenza are most common, but Pseudomonas aeruginosa may be the first pathogen isolated in infants. By 18 years of age, 80% of patients harbor P. aeruginosa and 3.5% harbor Burkholderia cepacia. Stenotrophomonas maltophilia, Achromobacter xylosoxidans, and nontuberculous mycobacteria may be newly emerging CF pathogens. The traditional approach to managing patients with CF is to treat acute pulmonary exacerbations with intravenous antimicrobial agents. However, prophylactic strategies to prevent initial infection or to delay chronic infection with P. aeruginosa or chronic maintenance therapy to slow deterioration of lung function may also improve clinical status. Recognition of the role of inflammation, even early in life, in the absence of clinical symptoms, has led to treatment with anti-inflammatory agents. Novel strategies to disrupt biofilm formation, stimulate chloride conductance, and replace abnormal CFTR are currently being studied.

Burkholderia cepacia↗
PubMed2003

Burkholderia and emerging pathogens in cystic fibrosis.

Persons with cystic fibrosis (CF) are susceptible to respiratory tract infection with a variety of bacterial species. Among these are several species in the genus Burkholderia (including members of the B. cepacia complex, B. gladioli, and B. pseudomallei), Stenotrophomonas maltophilia, Achromobacter ( Alcaligenes) xylosoxidans, certain Ralstonia species, and species within the new genus Pandoraea. Enterobacteriaceae and several other rather unusual or novel species also can be found. Many of these species are closely related phylogenetically and have similar phenotypes, presenting a challenge to accurate laboratory identification. Although their role in contributing to pulmonary disease in CF is not clear, the incidence of infection by some of these species appears to be increasing. The broad-spectrum antimicrobial resistance typically exhibited by these species severely limits treatment options. Newly developed genotypic methods of identification will enable studies to better assess the epidemiology and natural history of these emerging pathogens in CF.

Journal Article↗