共查询到20条相似文献,搜索用时 15 毫秒
1.
《Bioscience, biotechnology, and biochemistry》2013,77(10):2408-2419
We investigated the biosynthetic pathway for 2-phenylethanol, the dominant floral scent compound in roses, using enzyme assays. L-[2H8] Phenylalanine was converted to [2H8] phenylacetaldehyde and [2H8]-2-phenylethanol by two enzymes derived from the flower petals of R. ‘Hoh-Jun,’ these being identified as pyridoxal-5′-phosphate-dependent L-aromatic amino acid decarboxylase (AADC) and phenylacetaldehyde reductase (PAR). The activity of rose petal AADC to yield phenylacetaldehyde was nine times higher toward L-phenylalanine than toward its D-isomer, and this conversion was not inhibited by iproniazid, a specific inhibitor of monoamine oxidase. Under aerobic conditions, rose petal AADC stoichiometrically produced NH3 together with phenylacetaldehyde during the course of decarboxylation and oxidation, followed by the hydrolysis of L-phenylalanine. Phenylacetaldehyde was subsequently converted to 2-phenylethanol by the action of PAR. PAR showed specificity toward several volatile aldehydes. 相似文献
2.
Kenzo Yokozeki Konosuke Sano Chikahiko Eguchi Hisao Iwagami Koji Mitsugi 《Bioscience, biotechnology, and biochemistry》2013,77(3):729-736
The reaction conditions for the production of l-tryptophan from dl-5-indolyl- methylhydantoin by Flavobacterium sp. AJ-3940, and the cultural conditions for the formation of the enzyme involved by this bacterium were investigated. The optimal pH of this reaction was around 8.5 and the optimal temperature was between 45 to 55°C. The amount of l-tryptophan produced was remarkably increased by the addition of inosine, which formed a water insoluble adduct with l-tryptophan, to the reaction mixture because of the release of end-product inhibition by l-tryptophan. This enzyme was inducibly and intracellularly produced by Flavobacterium sp. AJ-3940 in proportion to the increase in cell growth. Cells showing high activity were obtained using a medium containing 5 g glucose, 5 g (NH4)2SO4, 1 g KH2PO4, 3 g K2HPO4, 0.1 g MgSO4 · 7H2O, 0.01 g CaCl2 · 2H2O, 50 ml corn steep liquor and 3.5 g dl-5-indolylmethylhydantoin in a total volume of 1 liter (pH 7.0). Under the best conditions, 43 mg/ml of l-tryptophan was produced from 50 mg/ml of dl-5-indolylmethylhydantoin with a molar yield of 97% in the presence of cells of Flavobacterium sp. AJ-3940. In addition, other l-aromatic amino acids such as l-phenylalanine, l-tyrosine, l-DOPA and related l-amino acids were also produced from the corresponding 5-substituted hydantoins by this bacterium containing the l-tryptophan-producing enzyme induced by dl-5-indolylmethylhydantoin. 相似文献
3.
Masayuki Tejima Michio Takeuchi Eiji Ichishima Setsuko Kobayashi 《Bioscience, biotechnology, and biochemistry》2013,77(7):1423-1426
The synthesis of a new series of Nα-benzyloxycarbonyl (Z)-amino acid and Z-dipeptide chloromethyl ketone derivatives is described. The new derivatives are as follows; Z-l-Leu-CH2Cl, Z-l-Phe (N02)-CH2Cl, Z-l-Tyr (Bzl)-CH2Cl, Z-l-Tyr (Z)-CH2Cl, Z-l-Tyr-CH2Cl, Z-l-Glu (Me)-CH2Cl, Z-l-Phe-l-Leu-CH2Cl, Z-l-Tyr-l-Leu-CH3Cl, Z-l-Leu-l-Phe-CH2Cl, Z-l-Leu-l-Tyr-CH2Cl, Z-l-G1U (Me)-l-Tyr-CH2Cl, Z-l-G1U (Me)-l-Phe-CH2Cl. 相似文献
4.
Katsumi Yuasa Keiko Ishizuka Susumu Kaburaki Toshio Sakasai 《Bioscience, biotechnology, and biochemistry》2013,77(11):2199-2206
It was found that a new compound of phenylalanine metabolites (2-hydroxy-3-phenylpropenoic acid) and phenylacetic acid were formed in the cultured Czapek medium containing phenylalanine by Aspergillus sojae. 2-Hydroxy-3-phenylpropenoic acid (HPPA) was formed from phenylalanine (d- and l-form) via phenyllactic acid (d- and l-form), and degraded to benzoic acid, p-hydroxybenzoic acid, protocatechuic acid, and catechol in this order.On the other hand, phenylacetic acid was formed from phenylpyruvic acid, and converted to homogentisic acid via o-hydroxyphenylacetic acid. From these results, a metabolic pathway of phenylalanine in Asp. sojae was proposed. 相似文献
5.
Takashi Hamasaki Kouzou Nagayama Yuichi Hatsuda 《Bioscience, biotechnology, and biochemistry》2013,77(1):203-205
A new metabolite has been isolated from Aspergillus chevalieri as colorless needles, mp 294–296°C, [α]d + 46°. It has a dioxopiperazine ring system formed from tryptophan and alanine. Chemical and spectroscopic data indicate that this metabolite is l-alanyl-2-(1,1-dimethylallyl)-l-tryptophan anhydride (I). 相似文献
6.
Kyoko Noda 《Bioscience, biotechnology, and biochemistry》2017,81(2):343-349
Pyrrolothiazolate formed by the Maillard reaction between l-cysteine and d-glucose has a pyrrolothiazole skeleton as a chromophore. We searched for a Maillard pigment having a pyrrolooxazole skeleton formed from l-threonine or l-serine instead of l-cysteine in the presence of d-glucose. As a result, two novel yellow pigments, named pyrrolooxazolates A and B, were isolated from model solutions of the Maillard reaction containing l-threonine and d-glucose, and l-serine and d-glucose, respectively, and identified as (2R,3S,7aS)-2,3,7,7a-tetrahydro-6-hydroxy-2,5,7a-trimethyl-7-oxo-pyrrolo[2,1-b]oxazole-3-calboxylic acid and (3S,7aS)-2,3,7,7a-tetrahydro-6-hydroxy-5,7a-dimethyl-7-oxo-pyrrolo[2,1-b]oxazole-3-calboxylic acid by instrumental analyses. These compounds were pyrrolooxazole derivatives carrying a carboxy group, and showed the absorption maxima at 300–360 nm under acidic and neutral conditions and at 320–390 nm under alkaline conditions. 相似文献
7.
Koji Muramoto Hiroshi Kawauchi Katura Tuzimura 《Bioscience, biotechnology, and biochemistry》2013,77(11):2241-2242
The formation of aromatic l-amino acid decarboxylase in bacteria was studied with intact cells in a reaction mixture containing the aromatic l-amino acids, 3,4-dihydroxy-l-phenyl-alanine, l-tyrosine, l-phenylalanine, l-tryptophan and 5-hydroxy-l-tryptophan. Activity was widely distributed in such genera as Achromobacter, Micrococcus, Staphylococcus and Sarcina. Bacterial strains belonging to the Micrococcaceae showed especially high decarboxylase activity toward l-tryptophan, 5-hydroxy-l-tryptophan and l-phenylalanine. M. percitreus AJ 1065 was selected as a promising source of aromatic l-amino acid decarboxylase. Results of experiments with this bacterium showed that the aromatic amine formed from l-tryptophan by the enzymatic method was identical with tryptamine. M. percitreus constitutively produced an enzyme which exhibited decarboxylase activity toward l-tryptophan. However, when large amounts of the aromatic l-amino acids listed above or the tryptamine formed from l-tryptophan were added, enzyme formation was repressed.Cells with high enzyme activity were prepared by cultivating this bacterium at 30°C for 24 hr in a medium containing 0.5% glycerol, 0.5% yeast extract, 0.5% Polypepton, 3.0 vol % soybean protein hydrolyzate, 0.1% KH2PO4, 0.1% MgSO4 · 7H2O, 0.001% FeSO4 · 7H2O and 0.001% MnSO4 · 5H2O in tap water (pH 8.0). 相似文献
8.
Kazunori Hatano Ikuo Nogami Eiji Higashide Toyokazu Kishi 《Bioscience, biotechnology, and biochemistry》2013,77(6):1503-1508
The biosynthetic origin of the amino acid moieties of enduracidin was investigated by feeding experiments with labeled compounds. Results of the incorporation and the distribution of radioactivity into the antibiotic revealed that glycine, l-serine, l-threonine, l-alanine, L-aspartic acid, l-ornithine and l-citrulline were incorporated into the corresponding amino acid moieties. Unique amino acids, enduracididine and its isomer with an imidazolidine ring, were derived from l-arginine, but not histidine. K1 (4-hydroxyphenylglycine) and K2 (3,5-dichloro-K1) moieties were derived from l-tyrosine. 36Cl-Sodium chloride was incorporated into the antibiotic in the early stage of fermentation. 相似文献
9.
Koh-ichi Aketa Nobuo Ohno Nobushige Itaya Isamu Nakayama Hirosuke Yoshioka 《Bioscience, biotechnology, and biochemistry》2013,77(4):895-896
Lipopeptin A is a selective inhibitor of in vitro peptidoglycan synthesis of E. coli Y-10. In the study here it inhibited the formation of lipid intermediates from UDP-[U-14C]GlcNAc and UDP-MurNAc-l-Ala-d-Glu-meso-DAP-d-Ala-d-Ala, but did not inhibit the formation of MurNAc-pentapeptide-p-p-lipid from UDP-MurNAc-l-Ala-d-Glu-[3H]meso-DAP-d-Ala-d-Ala. Lipopeptin A also did not have a significant effect on polymerase reaction. Therefore, the inhibition of the formation of GleNAc-MurNAc-pentapeptide-p-p-lipid from MurNAc-pentapeptide-p-p-lipid and UDP-GlcNAc is concluded to be the site of action.Lipopeptin A inhibits fungal growth, causing swelling in mycelia. It did not significantly inhibit the incorporations of 14C-labeled glucosamine, thymidine, uridine, phenylalanine, and sodium acetate into TCA insoluble fraction of mycelial suspension of Piricularia oryzae. In in vitro test, however, it inhibited the transfer of mannose from GDP-[U-14C]mannose (ID5O = 250 μg/ml) and GlcNAc from UDP-[U-14C]GlcNAc (ID50 = 100 μg/ml) into proteoheteroglycan with a particulate enzyme of Piricularia oryzae. It also slightly inhibited chitin synthesis (ID50 = 750 μg/ml) in the same enzyme system, but did not inhibit β-l,3-glucan synthesis. 相似文献
10.
Shigeyuki Takenishi Yoshio Tsujisaka 《Bioscience, biotechnology, and biochemistry》2013,77(6):1385-1391
A trisaccharide consisting of two d-xylose units and one l-arabinose unit, and a tetrasaccharide consisting of three d-xylose units and one l-arabinose unit were isolated from the hydrolyzate of rice-straw arabinoxylan by the xylanase I produced by Asp. niger.The structures of the trisaccharide and the tetrasaccharide were determined to be 31-α-l-arabinofuranosylxylobiose ([α]d? 80°) and 31-α-l-arabinofuranosylxylotriose ([α]d? 84°), respectively, by chemical and enzymic methods.According to the structures of two arabinose-xylose mixed oligosaccharides, it was shown that the rice-straw arabinoxylan is composed of chain of 1,4-linked βd-xylopyranose residues and some of xylose residues have side-chain of 1,3-linked α-l-arabinofuranose. 相似文献
11.
Regulatory properties of chorismate mutase from Corynebacterium glutamicum were studied using the dialyzed cell-free extract. The enzyme activity was strongly feedback inhibited by l-phenylalanine (90% inhibition at 0.1~1 mm) and almost completely by a pair of l-tyrosine and l-phenylalanine (each at 0.1~1 mm). The enzyme from phenylalanine auxotrophs was scarcely inhibited by l-tyrosine alone but the enzyme from a wild-type strain or a tyrosine auxotroph was weakly inhibited by l-tyrosine alone (40~50% inhibition, l-tyrosine at 1 mm). The enzyme activity was stimulated by l-tryptophan and the inhibition by l-phenylalanine alone or in the simultaneous presence of l-tyrosine was reversed by l-tryptophan. The Km value of the reaction for chorismate was 2.9 } 10?3 m. Formation of chorismate mutase was repressed by l-phenylalanine. A phenylalanine auxotrophic l-tyrosine producer, C. glutamicum 98–Tx–71, which is resistant to 3-amino-tyrosine, p-aminophenylanaine, p-fluorophenylalanine and tyrosine hydroxamate had chorismate mutase derepressed to two-fold level of the parent KY 10233. The enzyme in C. glutamicum seems to have two physiological roles; one is the control of the metabolic flow to l-phenylalanine and l-tyrosine biosynthesis and the other is the balanced partition of chorismate between l-phenylalanine-l-tyrosine biosynthesis and l-tryptophan biosynthesis. 相似文献
12.
Regulatory properties of the enzymes in l-tyrosine and l-phenyalanine terminal pathway in Corynebacterium glutamicum were investigated. Prephenate dehydrogenase was partially feedback inhibited by l-tyrosine. Prephenate dehydratase was strongly inhibited by l-phenylalanine and l-tryptophan and 100% inhibition was attained at the concentrations of 5 × 10?2mm and 10?1mm, respectively. l-Tyrosine stimulated prephenate dehydratase activity (6-fold stimulation at 1 mm) and restored the enzyme activity inhibited by l-phenylalanine or l-tryptophan. These regulations seem to give the balanced synthesis of l-tyrosine and l-phenyl-alanine. Prephenate dehydratase from C. glutamicum was stimulated by l-methionine and l-leucine similarly to the enzyme in Bacillus subtilis and moreover by l-isoleucine and l-histidine. C. glutamicum mutant No. 66, an l-phenylalanine producer resistant to p-fluorophenyl-alanine, had a prephenate dehydratase completely resistant to the inhibition by l-phenylalanine and l-tryptophan. 相似文献
13.
Hidetsugu Nakazawa Katsumi Ajisaka Masatsune Kainosho Seiji Sawada Hideaki Yamada 《Bioscience, biotechnology, and biochemistry》2013,77(11):2553-2557
The stereochemistry of the decarboxylation reaction catalyzed by an aromatic l-amino acid decarboxylase, purified from Micrococcus percitreus, was studied using stereospecifically deuterium labelled phenylalanine (Phe). The 1H NMR spectrum of [1,2-2H2]-β-phenethylamine enzymatically derived from (2S, 3R)-[3-2H]-Phe in 2H2O was compared with that of [1-2H]-β-phenethylamine from unlabelled Phe in 2H2O. The results clearly indicate that the decarboxylation reaction of this enzyme proceeds exclusively through a course in which the configuration at C-2 of Phe is retained. 相似文献
14.
Tetsuo Muro Yoshio Tominaga Shigetaka Okada 《Bioscience, biotechnology, and biochemistry》2013,77(5):1231-1237
The protease from Streptomyces cellulosae formed more turbidity in a 16% soybean protein hydrolysate in the initial stage of the reaction than α-chymotrypsin did, when the proteolytic activity of the protease was same as that of α-chymotrypsin. In highly concentrated solutions (2.5%) of various dipeptides, oligopeptides were produced by condensation by the protease. The oligopeptides formed were (l-Leu-Gly)2 and (l-Leu-Gly)3 from l-Leu-Gly, (l-Phe-l-Val)2 from l-Phe-l-Val, (l-Val-l-Phe)2 and (l-Val-l-Phe)3 from l-Val-l-Phe, and (l-Leu-l-Met)2 and (l-Leu-l-Met)3 from l-Leu-l-Met. 相似文献
15.
Isamu Shiio Hiroko Satō Michiko Nakagawa 《Bioscience, biotechnology, and biochemistry》2013,77(13):2315-2322
1. Some of 5-methyltrypotophan (5MT)-resistant mutants derived from glutamate-producing bacteria such as Brevibacterium flavum, Corynebacterium acetoglutamicum and Micrococcus glutamicus produced a small amount of l-tryptophan, while tyrosine and phenylalanine auxotrophs of B. flavum did not.2. 5-MT-resistant mutant derived from the auxotroph for tyrosine and phenylalanine produced 390 mg/liter of l-tryptophan at most. A mutant resistant to a higher concentration of 5MT, which was derived from a tyrosine and phenylalanine auxotrophic mutant which was resistant to a low concentration of 5MT, produced 660 mg/liter of l-tryptophan. Using this mutant, the effects of the concentrations of components of the culture medium on the l-tryptophan production were examined. The high concentration of l-tyrosine, but not l-phenylalanine, inhibited the l-tryptophan production. Using the improved culture medium, this strain produced 1.9 g/liter of l-tryptophan. 相似文献
16.
Regulatory properties of the enzymes involved in aromatic amino acid biosynthesis in the mutant of Corynebacterium glutamicum which produces a large amount of aromatic amino acids were examined. A phenylalanine auxotrophic l-tyrosine producer, pr-20, had a 3-deoxy-d-arabinoheptulosonate-7-phosphate (DAHP) synthetase released from the feedback inhibition by l-phenylalanine, l-tyrosine and l-tryptophan and had a two-fold derepressed chorismate mutase. A pair of l-phenylalanine and l-tyrosine still strongly inhibited the chorismate mutase activity, though the enzyme was partially released from the inhibition by l-phenylalanine alone. A tyrosine auxotrophic l-phenylalanine producer, PFP-19-31, had a DAHP synthetase sensitive to the feedback inhibition by l-phenylalanine, l-tyrosine and l-tryptophan and had a prephenate dehydratase and a chorismate mutase both partially released from the feedback inhibition by l-phenylalanine. The mutant produced a large amount of prephenate as well as l-phenylalanine. A phenylalanine and tyrosine double auxotrophic l-tryptophan producer, Px-115-97, had an anthranilate synthetase partially released from the feedback inhibition by l-tryptophan and had a DAHP synthetase sensitive to the feedback inhibition. These data explained the mechanism of the production of aromatic amino acids by these mutants and supported the in vivo functioning of the control mechanisms of aromatic amino acid biosynthesis in C. glutamicum previously elucidated in vitro experiments. 相似文献
17.
Ryotaro Hara Naoko Uchiumi Naoko Okamoto 《Bioscience, biotechnology, and biochemistry》2013,77(8):1384-1388
We evaluated the substrate specificities of four proline cis-selective hydroxylases toward the efficient synthesis of proline derivatives. In an initial evaluation, 15 proline-related compounds were investigated as substrates. In addition to l-proline and l-pipecolinic acid, we found that 3,4-dehydro-l-proline, l-azetidine-2-carboxylic acid, cis-3-hydroxy-l-proline, and l-thioproline were also oxygenated. Subsequently, the product structures were determined, revealing cis-3,4-epoxy-l-proline, cis-3-hydroxy-l-azetidine-2-carboxylic acid, and 2,3-cis-3,4-cis-3,4-dihydroxy-l-proline. 相似文献
18.
Makio Morita Makoto Tajima Masao Fujimaki 《Bioscience, biotechnology, and biochemistry》2013,77(2):250-255
An intermediate radical, ?H2OH, was produced in aqueous methanol solution containing nitrous oxide by γ-irradiation. Yields of ethylene glycol and formaldehyde, the major and the minor product from ?H2OH, respectively, changed on the addition of some solutes. Cysteine lowered the both product yields to zero even at a low concentration of 5 × 10?5m. Oxygen of low concentrations (2.5~7.5 × 10?5 m) changed effectively the major product from ethylene glycol to formaldehyde. k (CySH+?H2OH)/k(O2+?H2OH) was calculated as 0.5.Ascorbic acid (5 × 10?5 m) lowered ethylene glycol yield to 48%, cystine (10?3m) to 15%, methionine (10?3m) to 31%, histidine (10?3m) to 42%, tryptophan (10?3m) 46%, tyrosine (10?3m) to 77%, phenylalanine (10?3m) to 73%, hypoxanthine (10?3m) to 37%, adenine (10?3m) to 52%, uracil (10?3m) to 20%, thymine (10?3m) to 10%, cytosine (10?3 m) to 49%, rutin (10?3m) to 23%, pyrogallol (10?3m) to 41%, and gallic acid (10?3m) to 78% of the control. These results suggest that the reactions of the secondary radicals such as ?H2OH perform an important role in material change of foods irradiated with γ rays. 相似文献
19.
Seiya Watanabe Yuki Utsumi Shigeki Sawayama Yasuo Watanabe 《Bioscience, biotechnology, and biochemistry》2016,80(11):2151-2158
d-xylose and l-arabinose are the major constituents of plant lignocelluloses, and the related fungal metabolic pathways have been extensively examined. Although Pichia stipitis CBS 6054 grows using d-arabinose as the sole carbon source, the hypothetical pathway has not yet been clarified at the molecular level. We herein purified NAD(P)H-dependent d-arabinose reductase from cells grown on d-arabinose, and found that the enzyme was identical to the known d-xylose reductase (XR). The enzyme activity of XR with d-arabinose was previously reported to be only 1% that with d-xylose. The kcat/Km value with d-arabinose (1.27 min?1 mM?1), which was determined using the recombinant enzyme, was 13.6- and 10.5-fold lower than those with l-arabinose and d-xylose, respectively. Among the 34 putative sugar transporters from P. stipitis, only seven genes exhibited uptake ability not only for d-arabinose, but also for d-glucose and other pentose sugars including d-xylose and l-arabinose in Saccharomyces cerevisiae. 相似文献
20.
Esperin is an acidic antibiotic with a molecular formula of C39H67N5O11 and, on hydrolysis with acid, it afforded l-aspartic acid, l-glutamic acid, l-valine, l-leucine, d-leucine and 2-tridecenoic acid. By treatment with alkali, esperin was transformed to esperinic acid, C39H69N5O12, which was shown to be β-hydroxytridecanoyl-glutamyl-aspartyl-valyl-leucyl-leucine. From chemical and physical studies, esperin was proved to be the lactone of esperinic acid, represented by the formula III. 相似文献