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  • 1
    Electronic Resource
    Electronic Resource
    Cytosine deaminase that hydrolyzes creatinine to N-methylhydantoin in various cytosine deaminase-forming microorganisms (1987)
    Springer
    Archives of microbiology 147 (1987), S. 58-63 
    Details
    ISSN: 1432-072X
    Keywords: Creatinine deimination enzymes ; Creatinine deiminase ; Cytosine deaminase ; Creatinine degradation ; N-Methylhydantoin ; Creatinine ; Cytosine ; Pseudomonas putida 77 ; Cytosine deaminase induction ; Escherichia coli
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Creatinine deimination has been newly detected in the following various cytosine deaminase-forming microorganisms: Escherichia coli, Proteus mirabilis, Pseudomonas aureofaciens, Pseudomonas chlororaphis and Pseudomonas cruciviae. All these microorganisms, except for E. coli, formed cytosine deaminase in a constitutive or repressive way. P. putida 77 and E. coli showed highly increased formation of creatinine deiminase in the presence of creatinine and cytosine. Throughout serial DEAE-Sephacel and Sephacryl S-300 column chromatographies, the cytosine deaminases of these microorganisms, except for that of P. ovalis, were found to hydrolyze both creatinine and cytosine at comparable rates. No concrete evidence was obtained for the presence of any other protein that hydrolyzed creatine and/or cytosine than the cytosine deaminases in the three test microorganisms randomly selected for investigation. Different from P. putida 77, none of the test microorganisms degraded N-methylhydantoin; neither N-methylhydantoin amidohydrolase nor N-carbamoylsarcosine amidohydrolase was formed in the presence of creatinine in these microorganisms. As a result, the wide occurrence of cytosine deaminases in microorganisms was found to be related to the wide distribution of those microorganisms which hydrolyze creatinine to N-methylhydantoin without further degradation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00492905
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  • 2
    Electronic Resource
    Electronic Resource
    Production of a novel ω1-eicosapentaenoic acid by Mortierella alpina 1S-4 grown on 1-hexadecene (1991)
    Springer
    Archives of microbiology 156 (1991), S. 163-166 
    Details
    ISSN: 1432-072X
    Keywords: Fatty acid metabolism ; 1-Hexadecene ; ω1-Eicosapentaenoic acid ; Mortierella alpina
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract An arachidonic-producing fungus, Mortierella alpina 1S-4, was found to accumulate ω-unsaturated fatty acids of C-20 chain length together with ω1-hexadecenoic acid, ω1-octadecenoic acid and so on, when grown on 1-alkenes, i.e., 1-hexadecene and 1-octadecene. The results of mass spectroscopy and proton NMR showed that a C20 polyunsaturated fatty acid (PUFA) is a novel cis-5,8,11,14,19-eicosapentaenoic acid (20:5ω1). This PUFA was obtained at a yield of 0.13 mg/ml culture broth (2.8% of the fungal total fatty acid content) on cultivation of the fungus in a medium containing 4% (v/v) 1-hexadecene and 1% yeast extract at 28°C for 1 week. Investigation of the distribution of fatty acids showed that about 90% (by mol.) of the PUFA was present in the triglycerides and 10% was in the phospholipid fraction. About 70% of that found in the phospholipids was phosphatidylcholine (PC) and the value accounted for ca. 10% of the total fatty acid content. The formation of these ω-unsaturated fatty acids was presumed to occur through the arachidonic acid biosynthetic pathway (n-6 route).
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00249109
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  • 3
    Electronic Resource
    Electronic Resource
    Distribution and immunological characterization of microbial aldehyde reductases (1992)
    Springer
    Archives of microbiology 157 (1992), S. 279-283 
    Details
    ISSN: 1432-072X
    Keywords: Aldehyde reductase ; Aldo-keto reductases ; p-Nitrobenzaldehyde reductase ; Pyridine-3-aldehyde reductase ; Sporobolomyces ; Sporidiobolus ; Rhodotorula
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The distribution of microbial aldo-keto reductases was examined and their immunochemical characterization was performed. p-Nitrobenzaldehyde, pyridine-3-aldehyde and ethyl 4-chloro-3-oxobutanoate reductase activities were found to be widely distributed in a variety of microorganisms. In immunodiffusion studies, most yeasts belonging to the genera Sporobolomyces, Sporidiobolus and Rhodotorula formed precipitin bands with anti-Sporobolomyces salmonicolor aldehyde reductase serum. Furthermore, the results of immunotitration experiments suggested that Sporobolomyces salmonicolor AKU 4429 contains other enzyme(s) which can reduce p-nitrobenzaldehyde, pyridine-3-aldehyde and/or ethyl 4-chloro-3-oxobutanoate, and which are inactivated by anti-Sporobolomyces salmonicolor aldehyde reductase serum.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00245162
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  • 4
    Electronic Resource
    Electronic Resource
    Selective transport of divalent cations by transition metal permeases: the Alcaligenes eutrophus HoxN and the Rhodococcus rhodochrous NhlF (1999)
    Springer
    Archives of microbiology 171 (1999), S. 139-145 
    Details
    ISSN: 1432-072X
    Keywords: Key wordsRhodococcus rhodochrous ; Alcaligenes ; eutrophus ; Nickel transport ; Cobalt transport ; Ion ; selectivity
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract nhlF and hoxN, the genes encoding a cobalt transporter of Rhodococcus rhodochrous J1 and a nickel permease of Alcaligenes eutrophus H16, respectively, were expressed in Escherichia coli. 57Co2+ and 63Ni2+ transport of the recombinants was examined by means of a previously described physiological assay. Although the transporters are highly similar, different preferences for divalent transition metal cations were observed. HoxN was unable to transport 57Co2+, but mediated 63Ni2+ uptake. The latter activity was unaffected by a tenfold excess of other divalent cations, showing the specificity of HoxN for Ni2+. In contrast, NhlF transported both 57Co2+ and 63Ni2+ ion. NhlF-mediated 63Ni2+ uptake was markedly reduced in the presence of Co2+, while 57Co2+ uptake was only slightly lower in the presence of Ni2+. These results indicate different affinities of NhlF for Co2+ and Ni2+ and identified Co2+ ion as the preferred substrate.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002030050691
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  • 5
    Electronic Resource
    Electronic Resource
    Isolation and characterization of an ω3-desaturation-defective mutant of an arachidonic acid-producing fungus, Mortierella alpina 1S-4 (1994)
    Springer
    Archives of microbiology 161 (1994), S. 316-319 
    Details
    ISSN: 1432-072X
    Keywords: Key words: Fatty acids –Mortierella alpina–ω3-Desaturation – Mutation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract. A mutant considered to be defective in the conversion of n-6 to n-3 fatty acids (ω3-desaturation) was derived from a Δ5-desaturation-defective mutant (Mut44) of Mortierella alpina 1S-4, after treating its spores with N-methyl-N′-nitro-N-nitrosoguanidine. This mutant cannot produce 8(Z),11(Z),14(Z),17(Z)-eicosatetraenoic acid or any other n-3 fatty acids, of which about 10% was found in its parental strain upon cultivation at 12 °C. The mutant's growth rate was comparable to that of the parental strain when grown at 28 °C, but it became much slower when the mutant grew at 12 °C, at which the lag phase for Mut44 was about 2 d but 5 d for the mutant.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00303586
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  • 6
    Electronic Resource
    Electronic Resource
    Evaluation of two alternative metabolic pathways for creatinine degradation in microorganisms (1986)
    Springer
    Archives of microbiology 145 (1986), S. 322-328 
    Details
    ISSN: 1432-072X
    Keywords: Creatinine degradation ; Pseudomonas putida 77 ; Pseudomonas sp. H21 ; Pseudomonas sp. 0114 ; N-Methylhydantoin degradation ; Creatinine deiminase ; N-Methylhydantoin hydrolase ; N-Carbamoylsarcosine amidohydrolase ; Creatine amidinohydrolase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The microbial decomposition of creatinine was found to proceed mainly via N-methylhydantoin or creatine as the first degradation product. Either N-methylhydantoin or urea or both were detected as metabolites derived from creatinine in various microorganisms, and creatinine deiminase and creatinine amidohydrolase activities were detected concomitantly. N-Methylhydantoin hydrolase and N-carbamoylsarcosine amidohydrolase were found to be formed inducibly in the presence of creatinine or N-methylhydantoin. Three microorganisms which decompose creatinine in different ways were screened from soil. Pseudomonas putida 77 rapidly metabolized creatinine solely via N-methylhydantoin. Degradation of creatinine proceeded with both creatine and N-methylhydantoin as the first degradation products at the same time in Pseudomonas sp. H21. Pseudomonas sp. 0114 was found to metabolize creatinine mainly via creatine and to also metabolize N-methylhydantoin. Changes in the metabolites of creatinine during a cultivation or enzyme reaction were found to be closely related to the enzyme activities of interest which are regulated by creatinine or N-methylhydantoin in different ways depending on the microbial strain.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00470865
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  • 7
    Electronic Resource
    Electronic Resource
    Isolation and characterization of an ω3-desaturation-defective mutant of an arachidonic acid-producing fungus, Mortierella alpina 1S-4 (1994)
    Springer
    Archives of microbiology 161 (1994), S. 316-319 
    Details
    ISSN: 1432-072X
    Keywords: Fatty acids ; Mortierella alpina ; ω3-Desaturation ; Mutation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A mutant considered to be defective in the conversion of n-6 to n-3 fatty acids (ω3-desaturation) was derived from a Δ5-desaturation-defective mutant (Mut44) of Mortierella alpina 1S-4, after treating its spores with N-methyl-N′-nitro-N-nitrosoguanidine. This mutant cannot produce 8(Z),11(Z),14(Z),17(Z)-eicosatetraenoic acid or any other n-3 fatty acids, of which about 10% was found in its parental strain upon cultivation at 12°C. The mutant's growth rate was comparable to that of the parental strain when grown at 28°C, but it became much slower when the mutant grew at 12°C, at which the lag phase for Mut44 was about 2 d but 5 d for the mutant.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00303586
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  • 8
    Electronic Resource
    Electronic Resource
    Distribution of methylthioadenosine phosphorylase in eubacteria (1988)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 51 (1988), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract Eubacteria which contain S-adenosylhomocysteine hydrolase (EC 3.3.1.1) do not contain methylthioadenosine/adenosylhomocysteine nucleosidase (EC 3.2.2.9). In these microorganisms, 5′-deoxymethylthioadenosine is phosphorolyzed by methylthioadenosine phosphorylase (EC 2.4.2.28).
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1988.tb02993.x
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  • 9
    Electronic Resource
    Electronic Resource
    A novel metabolic pathway for creatinine degradation in Pseudomonas putida 77 (1985)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 30 (1985), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract A novel metabolic pathway for creatinine, degradation of creatinine to glycine via N-methylhydantoin, N-carbamoylsarcosine and sarcosine in turn, was found to operate in Pseudomonas putida 77. N-Methylhydantoin, sarcosine and glycine were detected as metabolites from creatinine, and enzyme activities responsible for the degradation of creatinine, N-methylhydantoin, N-carbamoylsarcosine and sarcosine were observed in a crude cell extract, while neither creatinine amidohydrolase activity nor creatine were detected at all. It is suggested that creatinine was utilized as a source of both carbon and nitrogen at the same time, and that N-methylhydantoin was also utilized efficiently.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1985.tb01106.x
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  • 10
    Electronic Resource
    Electronic Resource
    A novel NADPH-dependent aldehyde reductase, catalyzing asymmetric reduction of ß-keto acid esters, from Sporobolomyces salmonicolor: purification and characterization (1990)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 70 (1990), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract NADPH-dependent aldehyde reductase (EC 1.1.1.2) was purified 23-fold with an overall yield of 11% from Sporobolomyces salmonicolor AKU 4429, in 4 steps and, by adding ammonium sulfate, the enzyme was crystallized. The enzyme has a strict requirement for NADPH and irrversibly reduces a number of aldehydes, such as p-nitrobenzaldehyde, pyridine-3-aldehyde and d-glyceraldehyde. Furthermore, it was found that the enzyme catalyses stereospecific reduction of 4-halo-3-oxobutanoate esters to the corresponding (R)-4-halo-3-hydroxybutanoate esters, which are promising chiral compounds for the chemical synthesis of l-carnitine.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1990.tb03775.x
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