Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:6.4.1.2 (acetyl-CoA carboxylase)
2,876 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Acetyl-CoA carboxylase [ACCase; acetyl-CoA:carbon dioxide ligase (ADP forming), EC 6.4.1.2] catalyses the ATP-dependent carboxylation of acetyl-CoA to form malonyl-CoA. We have amplified a fragment of the biotin carboxylase (BC) domain of the Ustilago maydis acetyl-CoA carboxylase (ACC1) gene from genomic DNA and used this amplified DNA fragment as a probe to recover the complete gene from a lambda EMBL3 genomic library. The ACC1 gene has a reading frame of 6555 nucleotides, which is interrupted by a single intron of 80 bp in length. The gene encodes a protein containing 2185 amino acids, with a calculated M(r) of 242,530; this is in good agreement with the size of ACCases from other sources. Further identification was based on the position of putative binding sites for acetyl-CoA, ATP, biotin and carboxybiotin found in other ACCases. A single ACC1 allele was disrupted in a diploid wild-type strain. After sporulation of diploid disruptants, no haploid progeny containing a disrupted acc1 allele were recovered, even though an exogenous source of fatty acids was provided. The data indicate that, in U. maydis, ACCase is required for essential cellular processes other than de novo fatty acid biosynthesis.
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PMID:The ACC1 gene, encoding acetyl-CoA carboxylase, is essential for growth in Ustilago maydis. 750 Sep 41

The genes encoding two subunits of acetyl coenzyme A carboxylase, biotin carboxyl carrier protein, and biotin carboxylase have been cloned from Bacillus subtilis. DNA sequencing and RNA blot hybridization studies indicated that the B. subtilis accB homolog which encodes biotin carboxyl carrier protein, is part of an operon that includes accC, the gene encoding the biotin carboxylase subunit of acetyl coenzyme A carboxylase.
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PMID:The genes encoding the biotin carboxyl carrier protein and biotin carboxylase subunits of Bacillus subtilis acetyl coenzyme A carboxylase, the first enzyme of fatty acid synthesis. 759 99

Acetyl-coenzyme A carboxylase (ACCase, EC 6.4.1.2) catalyzes the synthesis of malonyl-coenzyme A, which is utilized in the plastid for de novo fatty acid synthesis and outside the plastid for a variety of reactions, including the synthesis of very long chain fatty acids and flavonoids. Recent evidence for both multifunctional and multisubunit ACCase isozymes in dicot plants has been obtained. We describe here the isolation of a tobacco (Nicotiana tabacum L. cv bright yellow 2 [NT1]) cDNA clone (E3) that encodes a 58.4-kD protein that shares 80% sequence similarity and 65% identity with the Anabaena biotin carboxylase subunit of ACCase. Similar to other biotin carboxylase subunits of acetyl-CoA carboxylase, the E3-encoded protein contains a putative ATP-binding motif but lacks a biotin-binding site (methionine-lysine-methionine or methionine-lysine-leucine). The deduced protein sequence contains a putative transit peptide whose function was confirmed by its ability to direct in vitro chloroplast uptake. The subcellular localization of this biotin carboxylase has also been confirmed to be plastidial by western blot analysis of pea (Pisum sativum), alfalfa (Medicago sativa L.), and castor (Ricinus communis L.) plastid preparations. Northern blot analysis indicates that the plastid biotin carboxylase transcripts are expressed at severalfold higher levels in castor seeds than in leaves.
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PMID:Structural analysis, plastid localization, and expression of the biotin carboxylase subunit of acetyl-coenzyme A carboxylase from tobacco. 761 Jan 68

The genetic organization of the Pseudomonas aeruginosa acetyl coenzyme A carboxylase (ACC) was investigated by cloning and characterizing a P. aeruginosa DNA fragment that complements an Escherichia coli strain with a conditional lethal mutation affecting the biotin carboxyl carrier protein (BCCP) subunit of ACC. DNA sequencing and RNA blot hybridization studies indicated that the P. aeruginosa accB (fabE) homolog, which encodes BCCP, is part of a 2-gene operon that includes accC (fabG), the structural gene for the biotin carboxylase subunit of ACC. P. aeruginosa homologs of the E. coli accA and accD, encoding the alpha and beta subunits of the ACC carboxyltransferase, were identified by hybridization of P. aeruginosa genomic DNA with the E. coli accA and accD. Data are presented which suggest that P. aeruginosa accA and accD homologs are not located either immediately upstream or downstream of the P. aeruginosa accBC operon. In contrast to E. coli, where BCCP is the only biotinylated protein, P. aeruginosa was found to contain at least three biotinylated proteins.
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PMID:Organization and nucleotide sequences of the genes encoding the biotin carboxyl carrier protein and biotin carboxylase protein of Pseudomonas aeruginosa acetyl coenzyme A carboxylase. 769 52

Acetyl-CoA carboxylase [ACCase; acetyl-CoA:carbon-dioxide ligase (ADP-forming), EC 6.4.1.2] catalyzes the ATP-dependent carboxylation of acetyl CoA to produce malonyl CoA. In plants, malonyl CoA is needed for plastid localized fatty acid biosynthesis and for a variety of pathways in the cytoplasm including flavonoid biosynthesis. We have determined the full nucleotide sequence of an ACCase from alfalfa, which appears to represent a cytoplasmic isozyme. Partial cDNAs were isolated from a cDNA library of suspension culture cells that had been elicited for isoflavonoid phytoalexin synthesis. The full-length sequence was obtained by primer extension and amplification of the cDNA with synthetic primers. The sequence codes for a protein of 2257 amino acids with a calculated M(r) of 252,039. The biotin carboxylase, biotin carboxyl carrier protein, and carboxyltransferase domains, respectively, show approximately 72%, 50%, and 65% sequence similarity to those of animal, diatom, and yeast ACCase sequences. ACCase enzyme activity and transcripts are induced severalfold upon addition of yeast or fungal elicitors to alfalfa cell cultures.
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PMID:Molecular cloning, characterization, and elicitation of acetyl-CoA carboxylase from alfalfa. 791 Apr 6

Efforts are currently under way in several laboratories to develop renewable fuels from biological sources. Our group conducts research involving the production of lipid-derived "biodiesel" fuel from microscopic algae. Lipid accumulation in algae typically occurs during periods of environmental stress, including growth under nutrient-deficient conditions. Biochemical studies have suggested that acetyl-CoA carboxylase (ACCase), a biotin-containing enzyme that catalyzes an early step in fatty acid biosynthesis, may be involved in the control of this lipid accumulation process. Therefore, it may be possible to enhance lipid production rates by increasing the activity of this enzyme via genetic engineering. As a first step toward this objective, we have cloned the gene that encodes ACCase from the eukaryotic alga Cyclotella cryptica. This is the first time that this gene has been isolated from a photosynthetic organism. The amino acid sequence of ACCase deduced from this gene exhibits a high degree of similarity to the sequences of animal and yeast ACCases in the biotin carboxylase and carboxyltransferase domains, but less similarity exists in the biotin carboxyl carrier protein domain. Comparison of the genomic nucleotide sequence to the sequences of cDNA clones has revealed the presence of two introns in the gene. We are currently constructing expression vectors containing this gene and developing algal transformation protocols to enable overexpression of ACCase in C. cryptica and other algal species.
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PMID:Characteristics of the gene that encodes acetyl-CoA carboxylase in the diatom Cyclotella cryptica. 791 57

One independent and two overlapping rape cDNA clones have been isolated from a rape embryo library. We have shown that they encode a 2.3 kb and a 2.5 kb stretch of the full-length acetyl-CoA carboxylase (ACCase) cDNA, corresponding to the biotin-binding and transcarboxylase domains respectively. Using the cDNA in Northern-blot analysis we have shown that the mRNA for ACCase has a higher level of expression in rape seed than in rape leaf and has a full length of 7.5 kb. The level of expression during rape embryogenesis was compared with both oil deposition and expression of two fatty acid synthetase components enoyl-(acyl-carrier-protein) reductase and 3-oxoacyl-(acyl-carrier-protein) reductase. Levels of ACCase mRNA were shown to peak at 29 days after anthesis during embryonic development, similarly to enoyl-(acyl-carrier-protein) reductase and 3-oxoacyl-(acyl-carrier-protein) reductase mRNA. In addition, a full-length genomic clone (19 kb) of Arabidopsis ACCase has been isolated and partially sequenced. Analysis of the clone has allowed the first plant ACCase activity domains (biotin carboxylase-biotin binding-transcarboxylase) to be ordered and assigned. Southern-blot analysis using the Arabidopsis clone indicates that ACCase is a single-copy gene in Arabidopsis but is encoded by a small gene family in rape.
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PMID:Isolation of cDNAs from Brassica napus encoding the biotin-binding and transcarboxylase domains of acetyl-CoA carboxylase: assignment of the domain structure in a full-length Arabidopsis thaliana genomic clone. 791 5

Acetyl-CoA carboxylase is found in all animals, plants, and bacteria and catalyzes the first committed step in fatty acid synthesis. It is a multicomponent enzyme containing a biotin carboxylase activity, a biotin carboxyl carrier protein, and a carboxyltransferase functionality. Here we report the X-ray structure of the biotin carboxylase component from Escherichia coli determined to 2.4-A resolution. The structure was solved by a combination of multiple isomorphous replacement and electron density modification procedures. The overall fold of the molecule may be described in terms of three structural domains. The N-terminal region, formed by Met 1-Ile 103, adopts a dinucleotide binding motif with five strands of parallel beta-sheet flanked on either side by alpha-helices. The "B-domain" extends from the main body of the subunit where it folds into two alpha-helical regions and three strands of beta-sheet. Following the excursion into the B-domain, the polypeptide chain folds back into the body of the protein where it forms an eight-stranded antiparallel beta-sheet. In addition to this major secondary structural element, the C-terminal domain also contains a smaller three-stranded antiparallel beta-sheet and seven alpha-helices. The active site of the enzyme has been identified tentatively by a difference Fourier map calculated between X-ray data from the native crystals and from crystals soaked in a Ag+/biotin complex. Those amino acid residues believed to form part of the active site pocket include His 209-Glu 211, His 236-Glu 241, Glu 276, Ile 287-Glu 296, and Arg 338.2+ represents the first X-ray model of a biotin-dependent carboxylase.
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PMID:Three-dimensional structure of the biotin carboxylase subunit of acetyl-CoA carboxylase. 791 38

The gene that encodes acetyl-coenzyme A carboxylase (ACCase; EC 6.4.1.2) in the eukaryotic alga Cyclotella cryptica has been isolated and cloned, representing the first time that a full-length gene for this enzyme has been isolated from a photosynthetic organism. The gene contains a 447-base pair intron that is located near the putative translation initiation codon and a 73-base pair intron that is located slightly upstream from the region that encodes the biotin binding site of the enzyme. The gene encodes a polypeptide that is predicted to be composed of 2089 amino acids and to have a molecular mass of 230 kDa. The deduced amino acid sequence exhibits strong similarity to the sequences of animal and yeast ACCases in the biotin carboxylase and carboxyltransferase domains. There is less sequence similarity in the biotin carboxyl carrier protein domain, although the highly conserved Met-Lys-Met of the biotin binding site is present. The amino terminus of the predicted ACCase sequence has characteristics of a signal sequence, suggesting that the enzyme is imported into chloroplasts via the endoplasmic reticulum, as has been shown to be the case for certain nuclear-encoded proteins that are transported into the chloroplasts of the diatom Phaeodactylum tricornutum. Southern blot analyses suggest that a single copy of this gene is present in C. cryptica.
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PMID:Cloning and characterization of the gene that encodes acetyl-coenzyme A carboxylase in the alga Cyclotella cryptica. 810 14

The complete amino acid sequence of 3T3-L1 adipocyte pyruvate carboxylase (PC) [pyruvate:carbon-dioxide ligase (ADP-forming), EC 6.4.1.1] has been deduced from sequencing overlapping cDNA clones obtained from an adipocyte cDNA library constructed in the lambda Zap vector. The encoding mRNA for PC promoter contains 4067 nt, including a 3534-nt coding sequence and noncoding regions of 100 and 433 nt at the 5' and 3' ends, respectively. The biotinylated lysine of the encoded PC promoter (1178 amino acids with a calculated M(r) of apocarboxylase = 129,784) is located 35 residues from the COOH-terminal end and, as in most other biotin enzymes, is in the consensus sequence AMKM. The adipocyte PC is closely similar (53% identity) to the yeast enzyme and contains different segments that are homologous with regions from the biotin carboxylase component of Escherichia coli acetyl-CoA carboxylase, the keto acid-binding subunits of Propionibacterium shermanii oxaloacetate transcarboxylase and Klebsiella pneumoniae oxaloacetate decarboxylase, and to the biotin carboxyl-carrier protein of the bacterial biotin enzymes. In addition to the putative mitochondrial targeting signal, functional domains are readily identifiable in the sequence and are in the following order: biotin carboxylase-carboxyltransferase-biotin carboxyl-carrier protein, as proposed for yeast PC.
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PMID:Adipose pyruvate carboxylase: amino acid sequence and domain structure deduced from cDNA sequencing. 844 88


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