Achromobacter

Acheson process Achlorhydria Achondrites Achromatic hologram Achromobacter sp. Achromycin Achromycin [60-54-8]... 

Carbamate hydrolysis is frequendy observed as the initial reaction for pesticides having carbamate bonds, such as aldicarb, carbofuran, carbaryl, and benomyl (eq. 12) (19). Numerous genera of carbamate-hydroly2ing bacteria have been identified, including Pseudomonas, Jhihrobacter, Bacillus, Nocardia, Achromobacter, Flavobacterium, Streptomyces, Alcaligenes, A spirillum, Micrococcus, and Bhodococcus. 

L-alanine can be prepared from aspartic acid (Figure A8.13). L-Aspartate-(5-decarboxylase produced by Xanthomonas oryzae No 531 has been used to prepared L-alanine in 95% yield from 15% L-aspartic add solution. Other strains, ie Pseudomonas dacunhae or Achromobacter pestifer, give comparable yields of L-alanine. The process has been commercialised by Tanabe. 

To identify the specific aldehyde that is actually involved in the light-emitting reaction of living luminous bacteria, Shimomura et al. (1974a) extracted and purified the aldehyde from 40 g each of the bacterial cells of P. phosphoreum, Achromobacter (Vibrio or Photobacterium) fischeri, and an aldehydeless mutant of A. fischeri. The aldehyde fractions were purified, and then oxidized with Tollens reagent (silver oxide dissolved in ammonia) to convert the CHO group into the COOH group. Then the acids obtained were analyzed by mass spectrometry. The results indicated that P. phosphoreum had contained a mixture of aldehydes dodecanal (5%), tetradecanal (63%) and hexadecanal (30%), as shown in Table 2.2. Thus, tetradecanal was clearly predominant in... 

Strehler, B. L., and Cormier, M. J. (1953). Factors affecting the luminescence of cell-free extracts of the luminous bacterium, Achromobacter fischeri. Arch. Biochem. Biophys. 47 16-33. 

Acantbephyra, 162, 336 Acantboscina, 336 Acholoe, 335 Achromobacter, 35, 36 Acorn worms (enteropneusts), 315 Acylhomoserine lactone, 43 Advice to students, 375 Aequorea, 159, 161, 162, 334, 375 Aequorea aequorea, 92-94, 346 collection, 93, 94 distribution, 92 squeezate, 94 synonyms, 92 Aequorea GFP, 150-154 chromophore, 153 cloning, 154 crystallization, 130 fluorescence quantum yield, 152 isolation, 129 molecular weight, 152 spectral properties, 130, 152 Aequorea victoria, 92 Aequorin, 92-129, 159, 160,172,173, 175, 346, 349, 350, 364, 375 assay, 98... 

IJrocaninsaure aus Histidin (mit Achromobacter liquidum IAM 1667)3 l.-Asparaginsdure aus Ammoniumfumarat (mit Escherichia Coli ATCC 11 303)4 5 2 6 i.-Citridlin aus Arginin (mit Pseudomonas Putida ATCC 4359)7. 

Both 2-hydroxy- and 3-hydroxypyridine are hydroxylated to 2,5-dihydroxypyridine by strains of Achromobacter sp. (Houghton and Cain 1972). These metabolites are probably, however, formed by different reactions whereas 3-hydroxypyridine behaves as a true pyridine, addition of H2O across the Cg Nj bond would produce the 2,5-dihydroxy compound 2-hydroxypyridine is a cyclic amide and hydroxylation apparently occurs at the diagonal position. The degradation of 4-hydroxypyridine is also initiated by hydroxylation and is followed by dioxygenation before ring fission (Figure 10.12) (Watson et al. 1974). 

Oilseed rape (Canola) Monsanto/1995 EPSPS, glyphosate oxidoreductase (GOX) Agrobacterium sp. strain CP4, Achromobacter sp. strain LBAA Tolerance to the herbicide glyphosate... 

In addition to the cultures identified for quinoline degradation, pyridine degraders were also found, namely Agrobacterium sp., Nocardia sp. strain PNO, Achromobacter sp., Rhodococcus opacus, and Arthrobacter crystallopoietes. The strain Alcaligenes sp. strain IN3 was reported to metabolize indole. 

Kozhukh, G. V., Hagihara, Y., Kawakami, T., Hasegawa, K., Naiki, H., and Goto, Y. (2002). Investigation of a peptide responsible for amyloid fibril formation of beta 2-microglobulin by achromobacter protease I./. Biol. Chem. 277, 1310-1315. 

Cinkotai et al. (11,12) airborne dust cardrooms of mills 1550-3500 (one volume 335) Achromobacter Flavobacterium Aerobacter... 

Sud et al. (1972) discovered that a strain of Achromobacter sp. utilized carbaryl as the sole source of carbon in a salt medium. The organism grew on the degradation products 1-naphthol, hydroquinone, and catechol. 1-Naphthol, a metabolite of carbaryl in soil, was recalcitrant to degradation by a bacterium tentatively identified as an Arthrobacter sp. under anaerobic conditions (Ramanand et al., 1988a). Carbaryl or its metabolite 1-naphthol at normal and ten times the field application rate had no effect on the growth of Rhizobium sp. or Azotobacter chroococcum (Kale et al., 1989). The half-lives of carbaryl under flooded and nonflooded conditions were 13-14 and 23-28 d, respectively (Venkateswarlu et al., 1980). 

Soil. Hydrolyzes in soil forming 3-chloroaniline (Bartha, 1971 Hartley and Kidd, 1987 Smith, 1988). In soil. Pseudomonas striata Chester, a Flavobacterium s >., an Agrobacterium s >., and an Achromobacter sp. readily degraded chlorpropham to 3-chloroaniline and 2-propanol. Subsequent degradation by enzymatic hydrolysis yielded carbon dioxide, chloride ions, and unidentified compounds (Kaufman, 1967). 

CASRN 122-42-9 molecular formula CioHieClNs FW 179.22 Biological. Rajagopal et al. (1984) reported that Achromobacter sp. and an Arthrobacter sp. utilized propham as a sole carbon source. Metabolites identified were A-phenylcarbamic acid, aniline, catechol, monoisopropyl carbonate, 2-propanol, and carbon dioxide. 

Hydrolysis of Polyester by Lipase. Aliphatic polyester, PEA and PCL were hydrolyzed by lipases from Achromobacter sp., C. cylindracea,... 

The blue protein from A. faecalis strain S-6, which was isolated as a requirement for transferring electrons to a copper-containing nitrite reductase, has since been shown to have sequence homology with proteins arbitrarily designated pseudoazurin by Ambler and Tobari (1985), from Achromobacter cycloclastes and from Pseudomonas AMI. [Pseudomonas AMI also produces amicyanin, which is the recipient of electrons from methylamine dehydrogenase, (see below)]. In A. cycloclastes reduced pseudoazurin donates electrons to a copper nitrite reductase (Liu et ai, 1986), as it does in A. faecalis. Ambler and Tobari (1985)... 

The nature of the copper in these proteins is not totally clear. Dooley et al (1988) reported that the Achromobacter protein may have two kinds of type I sites in a total of three copper sites per dimeric protein, while the A. faecalis protein was reported to be a tetrameric protein with both type I and type II coppers (KakutanielaZ., 1981). Interestingly, the Achromobacter protein is green. Both of these nitrite reductases accept electrons from a cupredoxin. 

It is currently believed that NO reacts with the type I copper. Hulse et al. (1989) showed that Cu (NO) is an intermediate in the enzyme reaction. Suzuki et al. (1989) examined the reaction of NO (unfortunately, not reporting the relative concentrations of materials used) with the Alcaligenes and Achromobacter NIR and found that the type I EPR signal vanishes on reaction with NO and is restored when NO is removed. At... 

The 2.3 A structure of the achromobacter NIR (Godden et al., 1991) has been determined from an MIR map based on native and two derivative data sets collected on an area detector. In the crystal the tightly packed arrangement of monomers around the crystallographic threefold axis suggests that the molecule must be a trimer, rather than a dimer, as originally determined from gel filtration studies. The chain tracing substantiates this. 

The N-terminal fragment 1-62 and the C-terminal fragment 76-174 of two recombinant analogues of GCSF were isolated after enzymatic cleavage with the Lys-specific protease from Achromobacter lyticus. In one fragment, the only Lys in the protein was at position 62, and was immediately followed by Ser. In the other fragment, the only Lys, also followed by a... 

---