نتایج جستجو برای: coa carboxylase alpha gene

تعداد نتایج: 1318013  

Journal: :iranian journal of applied animal science 2015
s. joezy-shekalgorabi h. moradi shahr-e-babak m. abbasi firoozjaei a. ghorbani

acetyl-coenzyme a carboxylase α (acc-alpha) is considered as the key regulatory enzyme in fatty acid biosynthesis. acc-alpha gene is located on caprine chromosome 11 and is polymorphic in many goat breeds. in the current study, we aimed to find possible single nucleotide polymorphisms (snps) in the exon 1 region of the acc-alpha gene in iranian mahabadi goat breed. genomic dna was extracted fro...

Journal: :Applied and environmental microbiology 2004
A L Díaz-Pérez A N Zavala-Hernández C Cervantes J Campos-García

Pseudomonas aeruginosa PAO1 mutants affected in the ability to degrade acyclic isoprenoids were isolated with transposon mutagenesis. The gny cluster (for geranoyl), which encodes the enzymes involved in the lower pathway of acyclic isoprenoid degradation, was identified. The gny cluster is constituted by five probable structural genes, gnyDBHAL, and a possible regulatory gene, gnyR. Mutations ...

Journal: :Journal of bacteriology 2003
Songkran Chuakrut Hiroyuki Arai Masaharu Ishii Yasuo Igarashi

Acyl coenzyme A carboxylase (acyl-CoA carboxylase) was purified from Acidianus brierleyi. The purified enzyme showed a unique subunit structure (three subunits with apparent molecular masses of 62, 59, and 20 kDa) and a molecular mass of approximately 540 kDa, indicating an alpha(4)beta(4)gamma(4) subunit structure. The optimum temperature for the enzyme was 60 to 70 degrees C, and the optimum ...

Journal: :FEBS letters 2006
Simon J Holton Stephanie King-Scott Ali Nasser Eddine Stefan H E Kaufmann Matthias Wilmanns

Mycobacterium tuberculosis contains multiple versions of the accA and accD genes that encode the alpha- and beta-subunits of at least three distinct multi-functional acyl-CoA carboxylase complexes. Because of its proposed involvement in pathogenic M. tuberculosis survival, the high-resolution crystal structure of the beta-subunit gene accD5 product has been determined and reveals a hexameric 35...

Journal: :علوم گیاهان زراعی ایران 0
مرجان بهزادی راد دانشجوی کارشناسی ارشد پردیس کشاورزی و منابع طبیعی دانشگاه تهران محمدرضا نقوی استاد پردیس کشاورزی و منابع طبیعی دانشگاه تهران علیرضا طالعی استاد پردیس کشاورزی و منابع طبیعی دانشگاه تهران علیرضا عباسی استادیار پردیس کشاورزی و منابع طبیعی دانشگاه تهران

barley belongs to the poaceae which is the largest monocotyledon family. plastid single-copy gene acetyl-coa carboxylase (accase) is the first step in the biosynthesis of fatty acids and therefore, it is used to study the phylogenetic relationships, evolutionary and systematic of grasses. in this study, for the first time, phylogenetic relationship of eight species of hordeum genus from iran in...

Journal: :Applied and environmental microbiology 2006
J A Aguilar A N Zavala C Díaz-Pérez C Cervantes A L Díaz-Pérez J Campos-García

Evidence suggests that the Pseudomonas aeruginosa PAO1 gnyRDBHAL cluster, which is involved in acyclic isoprenoid degradation (A. L. Díaz-Pérez, N. A. Zavala-Hernández, C. Cervantes, and J. Campos-García, Appl. Environ. Microbiol. 70:5102-5110, 2004), corresponds to the liuRABCDE cluster (B. Hoschle, V. Gnau, and D. Jendrossek, Microbiology 151:3649-3656, 2005). A liu (leucine and isovalerate u...

Journal: :Journal of microbiology and biotechnology 2007
Byung Chul Kim Jung Min Lee Jong Seog Ahn Beom Seok Kim

Pradimicins are potent antifungal antibiotics having an unusual dihydrobenzo[alpha]naphthacenequinone aglycone substituted with D-alanine and sugars. Pradimicins are polyketide antibiotics produced by Actinomadura hibisca P157-2. The gene cluster involved in the biosynthesis of pradimicins was cloned and sequenced. The pradimicin gene cluster was localized to a 39-kb DNA segment and its involve...

Journal: :Journal of bacteriology 2004
Takeshi Kanamori Norihisa Kanou Haruyuki Atomi Tadayuki Imanaka

We identified the first prokaryotic urea carboxylase (UCA) from a member of the alpha subclass of the class Proteobacteria, Oleomonas sagaranensis. This enzyme (O. sagaranensis Uca) was composed of 1,171 amino acids, and its N-terminal region resembled the biotin carboxylase domains of various biotin-dependent carboxylases. The C-terminal region of the enzyme harbored the Met-Lys-Met motif foun...

Journal: :Journal of lipid research 1997
F B Hillgartner T Charron

Transcription of acetyl-CoA carboxylase in avian liver is low during starvation or after consumption of a low-carbohydrate, high-fat diet and high during consumption of a high-carbohydrate, low-fat diet. The role of fatty acids or metabolites derived from fatty acids in the nutritional control of acetyl-CoA carboxylase transcription was investigated by determining the effects of long- and mediu...

Journal: :Journal of bacteriology 2000
Y Kimura R Miyake Y Tokumasu M Sato

We have cloned a DNA fragment from a genomic library of Myxococcus xanthus using an oligonucleotide probe representing conserved regions of biotin carboxylase subunits of acetyl coenzyme A (acetyl-CoA) carboxylases. The fragment contained two open reading frames (ORF1 and ORF2), designated the accB and accA genes, capable of encoding a 538-amino-acid protein of 58.1 kDa and a 573-amino-acid pro...

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