2-Acetolactate Mutase: An enzyme involved in the biosynthesis of isoleucine and valine. It converts 2-acetolactate into 3-hydroxy-2-oxo-isovalerate. Also acts on 2-hydroxy-2-acetobutyrate to form 2-hydroxy-2-oxo-3-methylvalerate. EC 5.4.99.3.Acetolactate Synthase: A flavoprotein enzyme that catalyzes the formation of acetolactate from 2 moles of PYRUVATE in the biosynthesis of VALINE and the formation of acetohydroxybutyrate from pyruvate and alpha-ketobutyrate in the biosynthesis of ISOLEUCINE. This enzyme was formerly listed as EC 4.1.3.18.Methylmalonyl-CoA Mutase: An enzyme that catalyzes the conversion of methylmalonyl-CoA to succinyl-CoA by transfer of the carbonyl group. It requires a cobamide coenzyme. A block in this enzymatic conversion leads to the metabolic disease, methylmalonic aciduria. EC 5.4.99.2.Phosphoglycerate Mutase: An enzyme that catalyzes the conversion of 2-phospho-D-glycerate to 3-phospho-D-glycerate. EC 5.4.2.1.Oxo-Acid-Lyases: Enzymes that catalyze the cleavage of a carbon-carbon bond of a 3-hydroxy acid. (Dorland, 28th ed) EC 4.1.3.Bisphosphoglycerate Mutase: An enzyme that catalyzes the transfer of phosphate from C-3 of 1,3-diphosphoglycerate to C-2 of 3-phosphoglycerate, forming 2,3-diphosphoglycerate. EC 5.4.2.4.Herbicides: Pesticides used to destroy unwanted vegetation, especially various types of weeds, grasses (POACEAE), and woody plants. Some plants develop HERBICIDE RESISTANCE.Sulfonylurea CompoundsIsoleucine: An essential branched-chain aliphatic amino acid found in many proteins. It is an isomer of LEUCINE. It is important in hemoglobin synthesis and regulation of blood sugar and energy levels.Acetoin: A product of fermentation. It is a component of the butanediol cycle in microorganisms. In mammals it is oxidized to carbon dioxide.Valine: A branched-chain essential amino acid that has stimulant activity. It promotes muscle growth and tissue repair. It is a precursor in the penicillin biosynthetic pathway.Pontederiaceae: A plant family of the order Liliales, subclass Liliidae, class Liliopsida (monocotyledons). Most species are perennials, native primarily to tropical America. They have creeping rootstocks, fibrous roots, and leaves in clusters at the base of the plant or borne on branched stems. The fruit is a capsule containing many seeds, or a one-seeded winged structure.Amino Acids, Branched-Chain: Amino acids which have a branched carbon chain.Herbicide Resistance: Diminished or failed response of PLANTS to HERBICIDES.Thiamine Pyrophosphate: The coenzyme form of Vitamin B1 present in many animal tissues. It is a required intermediate in the PYRUVATE DEHYDROGENASE COMPLEX and the KETOGLUTARATE DEHYDROGENASE COMPLEX.Hydroxybutyrates: Salts and esters of hydroxybutyric acid.Intramolecular Transferases: Enzymes of the isomerase class that catalyze the transfer of acyl-, phospho-, amino- or other groups from one position within a molecule to another. EC 5.4.Lactates: Salts or esters of LACTIC ACID containing the general formula CH3CHOHCOOR.CobamidesEscherichia coli: A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.Pyruvic Acid: An intermediate compound in the metabolism of carbohydrates, proteins, and fats. In thiamine deficiency, its oxidation is retarded and it accumulates in the tissues, especially in nervous structures. (From Stedman, 26th ed)Butyrates: Derivatives of BUTYRIC ACID. Included under this heading are a broad variety of acid forms, salts, esters, and amides that contain the carboxypropane structure.
(1/13) The yeast A kinases differentially regulate iron uptake and respiratory function.

Yeast has three A kinase catalytic subunits, which have greater than 75% identity and are encoded by the TPK genes (TPK1, TPK2, and TPK3) [Toda, T., Cameron, S., Sass, P., Zoller, M. & Wigler, M. (1987) Cell 50, 277-287]. Although they are redundant for viability, the three A kinases are not redundant for pseudohyphal growth [Robertson, L. S. & Fink, G. R. (1998) Proc. Natl. Acad. Sci. USA 95, 13783-13787; Pan, X. & Heitman, J. (1999) Mol. Cell. Biol. 19, 4874-4887]; Tpk2, but not Tpk1 or Tpk3, is required for pseudohyphal growth. Genome-wide transcriptional profiling has revealed unique signatures for each of the three A kinases leading to the identification of additional functional diversity among these proteins. Tpk2 negatively regulates genes involved in iron uptake and positively regulates genes involved in trehalose degradation and water homeostasis. Tpk1 is required for the derepression of branched chain amino acid biosynthesis genes that seem to have a second role in the maintenance of iron levels and DNA stability within mitochondria. The fact that TPK2 mutants grow better than wild types on nonfermentable carbon sources and on media deficient in iron supports the unique role of Tpk2 in respiratory growth and carbon source use.  (+info)

(2/13) Structure and expression of a cyanobacterial ilvC gene encoding acetohydroxyacid isomeroreductase.

Acetohydroxyacid isomeroreductase (AHAIR) is the shared second enzyme in the biosynthetic pathways leading to isoleucine and valine. AHAIR is encoded by the ilvC gene in bacteria. A 1,544-bp fragment of genomic DNA containing the ilvC gene was cloned from the cyanobacterium Synechocystis sp. strain PCC 6803, and the complete nucleotide sequence was determined. The identity of the gene was established by comparison of the nucleotide and derived peptide sequences with those of other ilvC genes. The highest degree of sequence similarity was found with the ilvC gene from Rhizobium meliloti. The isolated Synechocystis ilvC gene complemented an Escherichia coli ilvC mutant lacking AHAIR activity. The expressed Synechocystis gene encodes a protein that has a molecular mass of 35.7 kDa and that has AHAIR activity in an in vitro assay. Polyclonal antibodies raised against purified Synechocystis AHAIR produced a single band on a Western blot (immunoblot) of a Synechocystis cell extract and detected the protein in an extract of an E. coli ilvC mutant strain that was transformed with a plasmid containing the Synechocystis ilvC gene. The antibody did not react with an extract of an E. coli ilvC mutant strain that was transformed with a control plasmid lacking the Synechocystis ilvC gene or with an extract of an E. coli IlvC+ control strain.  (+info)

(3/13) Isolation and kinetic properties of acetohydroxy acid isomeroreductase from spinach (Spinacia oleracea) chloroplasts overexpressed in Escherichia coli.

Acetohydroxy acid isomeroreductase catalyses a two-step reaction, an alkyl migration and a NADPH-dependent reduction, in the assembly of the carbon skeletons of branched-chain amino acids. Detailed investigations of acetohydroxy acid isomeroreductase aimed at elucidating the biosynthetic pathway of branched-chain amino acids and at designing new inhibitors of the enzyme having herbicidal potency have so far been conducted with the enzymes isolated from bacteria. To gain more information on a plant system, the gene encoding the mature acetohydroxy acid isomeroreductase from spinach (Spinacia oleracea) leaf chloroplasts has been used to transform Escherichia coli cells and to overexpress the enzyme. A rapid protocol is described that allows the preparation of large quantities of pure spinach chloroplast acetohydroxy acid isomeroreductase. Kinetic and structural properties of the plant enzyme expressed in Escherichia coli are compared with those reported in our previous studies on the native enzymes purified from spinach chloroplasts and with those reported for the corresponding enzymes isolated from Escherichia coli and Salmonella typhimurium. Both the plant and the bacterial enzymes obey an ordered mechanism in which NADPH binds first, followed by substrate (either 2-acetolactate or 2-aceto-2-hydroxybutyrate). Inhibition studies employing an inactive substrate analogue, 2-hydroxy-2-methyl-3-oxopentanoate, showed, however, that the binding of 2-hydroxy-2-methyl-3-oxopentanoate and NADPH occurs randomly, suggestive of some flexibility of the plant enzyme active site. The observed preference of the enzyme for 2-aceto-2-hydroxybutyrate over 2-acetolactate is discussed with regard to the contribution of acetohydroxy acid isomeroreductase activity in the partitioning between isoleucine and valine biosyntheses. Moreover, the kinetic properties of the chloroplast enzyme support the notion that biosynthesis of branched-chain amino acids in plants is controlled by light. As judged by analytical-ultracentrifugation and gel-filtration analyses the overexpressed plant enzyme is a dimer of identical subunits.  (+info)

(4/13) Isolation, characterization and sequence analysis of a full-length cDNA clone encoding acetohydroxy acid reductoisomerase from spinach chloroplasts.

Acetohydroxy acid reductoisomerase (AHRI), the second enzyme in the parallel isoleucine/valine-biosynthetic pathway, catalyses an unusual two-step reaction in which the substrate, either 2-acetolactate or 2-aceto-2-hydroxybutyrate, is converted via an alkyl migration and an NADPH-dependent reduction to give 2,3-dihydroxy-3-methylbutyrate or 2,3-dihydroxy-3-methylvalerate respectively. We have isolated and characterized a full-length cDNA from a lambda gt11 spinach library encoding the complete acetohydroxy acid reductoisomerase protein precursor. The 2050-nucleotide sequence contains a 1785-nucleotide open reading frame. The derived amino acid sequence indicates that the protein precursor consists of 595 amino acid residues including a presequence peptide of 72 amino acid residues. The N-terminal sequence of the first 16 amino acid residues of the purified AHRI confirms the identity of the cDNA. The derived amino acid sequence from this open reading frame shows 23% identity with the deduced amino acid sequences of the Escherichia coli and Saccharomyces cerevisiae AHRI proteins. There are two blocks of conserved amino acid residues in these three proteins. One of these is a sequence similar to the 'fingerprint' region of the NAD(P)H-binding site found in a large number of NAD(P)H-dependent oxidoreductases. The other, a short sequence (Lys-Xaa-Xaa-Xaa-Xaa-Xaa-Xaa-Xaa-Ser-His-Gly-Phe) containing the amino acids lysine and histidine, could well be the catalytic site of the first step of the AHRI reaction. Southern-blot analysis indicated that AHRI is encoded by a single gene per haploid genome of about 7.5 kbp containing at least four introns.  (+info)

(5/13) Characterization of enzymes of the branched-chain amino acid biosynthetic pathway in Methanococcus spp.

Methanococcus aeolicus, Methanococcus maripaludis, and Methanococcus voltae contain similar levels of four enzymes of branched-chain amino acid biosynthesis: acetohydroxy acid synthase, acetohydroxy acid isomeroreductase, dihydroxy acid dehydratase, and transaminase B. Following growth at low partial pressures of H2-CO2, the levels of these enzymes in extracts of M. voltae are reduced three- to fivefold, which suggests that their synthesis is regulated. The enzymes from M. aeolicus were found to be similar to the eubacterial and eucaryotic enzymes with respect to molecular weights, pH optima, kinetic properties, and sensitivities to O2. The acetohydroxy acid isomeroreductase has a specific requirement for Mg2+, and other divalent cations were inhibitory. It was stimulated threefold by K+ and NH4+ ions and was able to utilize NADH as well as NADPH. The partially purified enzyme was not sensitive to O2. The dihydroxy acid dehydratase is extremely sensitive to O2, and it has a half-life under 5% O2 of 6 min at 25 degrees C. Divalent cations were required for activity, and Mg2+, Mn2+, Ni2+, Co2+, and Fe2+ were nearly equally effective. In conclusion, the archaebacterial enzymes are functionally homologous to the eubacterial and eucaryotic enzymes, which implies that this pathway is very ancient.  (+info)

(6/13) Purification and characterization of acetohydroxyacid reductoisomerase from spinach chloroplasts.

Acetohydroxyacid reductoisomerase was purified over 400-fold to a specific activity of 62 nkat.mg-1, with 2-aceto-2-hydroxybutyrate as substrate, from the stroma of spinach leaf chloroplasts. The enzyme was not intrinsically membrane bound. The native enzyme was a tetramer with a subunit Mr of 59,000. The activity was optimum between pH 7.5 and 8.5. The apparent Km for 2-acetolactate was 25 microM and for 2-aceto-2-hydroxybutyrate was 37 microM. The enzyme required Mg2+ and the Vmax. was attained at physiological Mg2+ concentrations. NADP+ competitively inhibited the reaction when NADPH was the varied substrate. The native enzyme eluted from Mono-Q ion-exchange resins as three distinct peaks of activity. This elution pattern was preserved when the peaks were combined, dialysed and re-chromatographed. Each form exhibited identical Mr of 59,000 after SDS/polyacrylamide gel electrophoresis (PAGE), whereas they were easily distinguishable from each other after PAGE under non-denaturing conditions. These results provide evidence for the existence of multiple forms of acetohydroxyacid reductoisomerase in chloroplasts isolated from spinach leaves.  (+info)

(7/13) The ILV5 gene of Saccharomyces cerevisiae is highly expressed.

The nucleotide sequence of the yeast ILV5 gene, which codes for the branched-chain amino acid biosynthesis enzyme acetohydroxyacid reductoisomerase, has been determined. The ILV5 coding region is 1,185 nucleotides, corresponding to a polypeptide with a molecular weight of 44,280. Transcription of the ILV5 mRNA initiates at position -81 upstream from the ATG translation start codon and terminates between 218 and 222 bases downstream from the stop codon. Consensus sequences have been identified for initiation and termination of transcription, and for general control of amino acid biosynthesis, as well as repression by leucine. The ILV5 gene is regulated slightly by general amino acid control. Codon usage of the ILV5 gene has the strong bias observed in yeast genes that are highly expressed. In agreement with this, the reductoisomerase monomer, with an apparent molecular weight of 40,000, has been identified in an SDS polyacrylamide gel pattern of total soluble yeast proteins as a gene dosage dependent band.  (+info)

(8/13) The herbicidally active experimental compound Hoe 704 is a potent inhibitor of the enzyme acetolactate reductoisomerase.

Growth inhibition of plants and bacteria by the experimental herbicide Hoe 704 (2-methylphosphinoyl-2-hydroxyacetic acid) was alleviated by the addition of the branched-chain amino acids to growth media. Hoe 704 caused a massive accumulation of acetoin and acetolactate, indicating its direct interference with the branched-chain amino acid biosynthetic pathway. The second enzyme of this pathway, acetolactate reductoisomerase (EC 1.1.1.86), was found to be subject to strong inhibition by Hoe 704. The inhibition was time-dependent and competitive with the enzyme's substrate, acetolactate. This report establishes acetolactate reductoisomerase as a new target for a herbicidal compound.  (+info)

*  2-acetolactate mutase
Other names in common use include acetolactate mutase, and acetohydroxy acid isomerase. This enzyme participates in valine, ... In enzymology, a 2-acetolactate mutase (EC 5.4.99.3) is an enzyme that catalyzes the chemical reaction 2-acetolactate ⇌ {\ ... The systematic name of this enzyme class is 2-acetolactate methylmutase. ... 2-acetolactate, and one product, 3-hydroxy-3-methyl-2-oxobutanoate. This enzyme belongs to the family of isomerases, ...
*  List of MeSH codes (D08)
... phosphoglycerate mutase MeSH D08.811.399.894.200 --- amino acid isomerases MeSH D08.811.399.894.200.200 --- alanine racemase ... acetolactate synthase MeSH D08.811.913.200.650 --- transaldolase MeSH D08.811.913.200.825 --- transketolase MeSH D08.811. ... chorismate mutase MeSH D08.811.399.520.250.500 --- prephenate dehydratase MeSH D08.811.399.520.250.750 --- prephenate ... bisphosphoglycerate mutase MeSH D08.811.399.520.750.625 --- phosphoglucomutase MeSH D08.811.399.520.750.700 --- ...
*  List of EC numbers (EC 5)
... benzene mutase EC 5.4.4.2: isochorismate synthase EC 5.4.4.3: 3-(hydroxyamino)phenol mutase EC 5.4.4.4: geraniol isomerase EC ... isobutyryl-CoA mutase EC 5.4.99.14: 4-carboxymethyl-4-methylbutenolide mutase EC 5.4.99.15: (1→4)-a-D-glucan 1-a-D- ... phosphoenolpyruvate mutase EC 5.4.2.10: phosphoglucosamine mutase EC 5.4.3.1: deleted EC 5.4.3.2: lysine 2,3-aminomutase EC 5.4 ... methylaspartate mutase EC 5.4.99.2: methylmalonyl-CoA mutase EC 5.4.99.3: 2-acetolactate mutase EC 5.4.99.4: 2- ...
*  Amino acid synthesis
Step two is the NADPH+ + H+ - dependent reduction of α-acetolactate and migration of the methane groups to produce α, β- ... This process is mediated by a phenylalanine (PheA) or tyrosine (TyrA) specific chorismate mutase-prephenate dehydrogenase. The ... It begins with the reaction of two pyruvate molecules catalyzed by Acetohydroxy acid synthase yielding α-acetolactate. ... The loop formed by strands 2 and 3 forms an anti-terminator and translation of the his genes will continue and histidine will ...
2-acetolactate mutase - Wikipedia  2-acetolactate mutase - Wikipedia
Other names in common use include acetolactate mutase, and acetohydroxy acid isomerase. This enzyme participates in valine, ... In enzymology, a 2-acetolactate mutase (EC 5.4.99.3) is an enzyme that catalyzes the chemical reaction 2-acetolactate ⇌ {\ ... The systematic name of this enzyme class is 2-acetolactate methylmutase. ... 2-acetolactate, and one product, 3-hydroxy-3-methyl-2-oxobutanoate. This enzyme belongs to the family of isomerases, ...
more infohttps://en.wikipedia.org/wiki/2-acetolactate_mutase
List of MeSH codes (D08) - Wikipedia  List of MeSH codes (D08) - Wikipedia
... phosphoglycerate mutase MeSH D08.811.399.894.200 --- amino acid isomerases MeSH D08.811.399.894.200.200 --- alanine racemase ... acetolactate synthase MeSH D08.811.913.200.650 --- transaldolase MeSH D08.811.913.200.825 --- transketolase MeSH D08.811. ... chorismate mutase MeSH D08.811.399.520.250.500 --- prephenate dehydratase MeSH D08.811.399.520.250.750 --- prephenate ... bisphosphoglycerate mutase MeSH D08.811.399.520.750.625 --- phosphoglucomutase MeSH D08.811.399.520.750.700 --- ...
more infohttps://en.wikipedia.org/wiki/List_of_MeSH_codes_(D08)
Oenococcus oeni proteome reference map | Open Biology  Oenococcus oeni proteome reference map | Open Biology
MLE, malolactic enzyme; LDH, lactate dehydrogenase; CL, citrate lyase; OAD, oxaloacetate decarboxylase; ALS, α-acetolactate ... phosphoglycerate mutase; ENO, enolase; PK, pyruvate kinase; PO, pyruvate oxidase; ALDH, alcohol dehydrogenase; FK, fructokinase ... α-acetolactate decarboxylase (OENOO_54034), acetoin reductase (OENOO_48023) and diacetyl reductase (OENOO_43013). All these ... Figure 2. Comparative analyses of the predicted and the actual proteome of O. oeni ATCC BAA-1163. Frequency distribution of the ...
more infohttp://rsob.royalsocietypublishing.org/content/4/2/130154
Glicerina biotecnologia | Glycolysis | Citric Acid Cycle  Glicerina biotecnologia | Glycolysis | Citric Acid Cycle
Phosphoglycerate mutase. Phosphoglycerate mutase (GPM) converts 3-phosphoglycerate into 2-phosphoglycerate in the later part of ... Probably via nonspecific decarboxylation of acetolactate formed in valine biosynthesis. Butanediol dehydrogenase. Glucose-6- ... Phosphoglycerate mutase (EC 5.4.2.1). Pyruvate decarboxylase (EC 4.1.1.1). Alcohol dehydrogenase (EC 1.1.1.1). Glycerol-3-P ... Phosphoglycerate mutase (GPM). Enolase (ENO). Pyruvate kinase (PYK). Pyruvate decarboxylase (PDC). Alcohol dehydrogenase (ADH) ...
more infohttps://www.scribd.com/document/259508868/Glicerina-biotecnologia
Acetolactate synthase regulatory subunits play divergent and overlapping roles in branched-chain amino acid synthesis and...  Acetolactate synthase regulatory subunits play divergent and overlapping roles in branched-chain amino acid synthesis and...
Acetolactate synthase (ALS) is the first enzyme in the BCAA synthesis pathway. Although the functional contribution of ALS to ... Aspartate kinase, chorismate mutase, TyrA domain. AHAS: Acetohydroxyacid synthase. AIP: ALS-Interacting Protein ... Action mechanisms of acetolactate synthase-inhibiting herbicides. Pestic Biochem Physiol. 2007;89(2):89-96.View ArticleGoogle ... The formation of acetolactate. J Biol Chem. 1958;233(5):1156-60.PubMedGoogle Scholar. ...
more infohttps://bmcplantbiol.biomedcentral.com/articles/10.1186/s12870-017-1022-6
The use of proteomic techniques to study the physiology and virulence of  staphylococcus aureus   The use of proteomic techniques to study the physiology and virulence of staphylococcus aureus
... phosphoglycerate mutase, are involved in central carbon metabolism and energy generation These proteins would be expected in ... SACOL1758 34 acetolactate synthase, catabolic (budB) SACOL2199 33 ribosomal protein L22 (rplV) SACOL2234 33 CTP synthase (pyrG ... phosphoglycerate mutase, and enolase are generally found to be downregulated in stationary phase when compared to post ... Q5HCV2 3 0 Acetolactate synthase, catabolic Q5HDZ7,Q5HDZ7 0 2 Chorismate mutase/phospho 2 dehydro 3 deoxyheptonate aldolase ...
more infohttp://digital.lib.usf.edu/SFS0028061/00001
dict.md | M  dict.md | M
mutase activity. Mutase-Prephenate Dehydratase, Chorismate. Mutase-Prephenate Dehydrogenase, Chorismate. Mutase, 2-Acetolactate ... MutS Homolog 2, Colon Cancer, Nonpolyposis Type 1 (E. coli) Gene. mutS homolog 2, colon cancer, nonpolyposis type 1 (E. coli) ... MutL Homolog 1, Colon Cancer, nonpolyposis type 2 (E. coli) Gene. mutL homolog 1, colon cancer, nonpolyposis type 2 (E. coli) ... mutS homolog 2, colon cancer, nonpolyposis type 1 (E. coli). ... mutS homolog 2 (E. coli) protein, rat. mutS homolog 2 (E. coli ...
more infohttp://en.dict.md/M/672
EDN01821.1 protein (Pseudoflavonifractor capillosus) - STRING interaction network  EDN01821.1 protein (Pseudoflavonifractor capillosus) - STRING interaction network
Acetolactate synthase; KEGG- cac-CAC3169 3.9e-146 ilvB; acetolactate synthase large subunit K01652; COG- COG0028 Thiamine ... Phosphoglucosamine mutase; Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate; Belongs to the ... Phosphoglucosamine mutase; Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate; Belongs to the ... Phosphoglucosamine mutase; Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate; Belongs to the ...
more infohttps://string-db.org/network/411467.BACCAP_00487
Respiratory complex I - Wikipedia  Respiratory complex I - Wikipedia
451 (2): 157-161. ISSN 0014-5793. PMID 10371157.. *^ a b Batista AP, Pereira MM (March 2011). "Sodium influence on energy ... 169 (2): 300-304. ISSN 0014-5793. PMID 6325245.. *^ Galkin A, Dröse S, Brandt U (December 2006). "The proton pumping ... 409 (2): 491-9. doi:10.1042/BJ20071162. PMID 17916065.. *^ Sahni, Prateek V.; Zhang, Jimmy; Sosunov, Sergey; Galkin, Alexander ... doi:10.1016/0378-8741(82)90002-2. PMID 7132401.. *^ Nakamaru-Ogiso E, Han H, Matsuno-Yagi A, Keinan E, Sinha SC, Yagi T, ...
more infohttps://en.wikipedia.org/wiki/NADH_dehydrogenase_
Team:Bielefeld-CeBiTec/Results/Modelling - 2014.igem.org  Team:Bielefeld-CeBiTec/Results/Modelling - 2014.igem.org
Atsumi, S., Li, Z., and Liao, J.C. (2009). Acetolactate Synthase from Bacillus subtilis Serves as a 2-Ketoisovalerate ... Development of a Mutagenesis, Expression and Purification System for Yeast Phosphoglycerate Mutase". European Journal of ... The Two Analogous Phosphoglycerate Mutases of Escherichia Coli". FEBS Letters 455, no. 3 (1999): 344-48. ... Table 2: This table shows all enzymatic parameters which were used for our dynamic model. Enzyme. kcat [-]. KM [mM]. Reference ...
more infohttp://2014.igem.org/Team:Bielefeld-CeBiTec/Results/Modelling
Network Portal - Gene BC0442  Network Portal - Gene BC0442
Acetolactate synthase large subunit (NCBI ptt file). 43, 445. BC0884. BC0884. Alpha-acetolactate decarboxylase (NCBI ptt file) ... Phosphoglycerate mutase (NCBI ptt file). 322, 483. BC2436. BC2436. SpoIISA like protein (NCBI ptt file). 194, 322. ... POSITION A C G T 1 0.0 0.2 0.8 0.0 2 0.8 0.0 0.0 0.2 3 0.0 0.2 0.0 0.8 4 0.0 0.0 0.6 0.4 5 0.0 0.8 0.0 0.2 6 0.0 0.2 0.8 0.0 7 ... 2-oxoglutarate dehydrogenase E1 component (NCBI ptt file). 43, 445. BC1390. BC1390. Potassium uptake protein KtrB (NCBI ptt ...
more infohttp://networks.systemsbiology.net/bce/gene/BC0442
Network Portal - Gene BC4593  Network Portal - Gene BC4593
Acetolactate synthase large subunit (NCBI ptt file). 43, 445. BC0884. BC0884. Alpha-acetolactate decarboxylase (NCBI ptt file) ... Phosphoglycerate mutase (NCBI ptt file). 322, 483. BC2436. BC2436. SpoIISA like protein (NCBI ptt file). 194, 322. ... POSITION A C G T 1 0.0 0.2 0.8 0.0 2 0.8 0.0 0.0 0.2 3 0.0 0.2 0.0 0.8 4 0.0 0.0 0.6 0.4 5 0.0 0.8 0.0 0.2 6 0.0 0.2 0.8 0.0 7 ... 2-oxoglutarate dehydrogenase E1 component (NCBI ptt file). 43, 445. BC1390. BC1390. Potassium uptake protein KtrB (NCBI ptt ...
more infohttp://networks.systemsbiology.net/bce/gene/BC4593
ASMscience | Carbohydrate Uptake and  ASMscience | Carbohydrate Uptake and
... α-acetolactate synthase; alsD, α-acetolactate decarboxylase; pdhABCD, pyruvate dehydrogenase complex; pta, ... phosphoglycerate mutase; eno, enolase; pykA, pyruvate kinase. Pentose-P pathway genes: yqjJ, putative glucose-6-P dehydrogenase ... α-acetolactate synthase; alsD, α-acetolactate decarboxylase; pdhABCD, pyruvate dehydrogenase complex; pta, ... phosphoglycerate mutase; eno, enolase; pykA, pyruvate kinase. Pentose-P pathway genes: yqjJ, putative glucose-6-P dehydrogenase ...
more infohttp://www.asmscience.org/content/book/10.1128/9781555817992.chap11
Methods and compositions for producing solvents - Patent application  Methods and compositions for producing solvents - Patent application
Phosphoglycerate mutase 1662 Critical small acid-soluble spore protein, alpha/beta type 1685 Small acid-soluble spore protein ... Catabolic acetolactate synthase 139 Aspartyl/asparaginyl-tRNA synthetase 168 Ribose 5-phosphate isomerase A 175 Putative ... Phosphoglycerate mutase family protein 826 3-Oxoacyl-(acyl carrier protein) reductase 834 Alcohol dehydrogenase 873 Possible ... Phosphoglycerate mutase 3691 Uncharacterized conserved protein YHAD family 3755 L-lactate dehydrogenase 3774 L-serine ...
more infohttp://www.patentsencyclopedia.com/app/20090047718
KEGG SSDB Best Search Result: toc:Toce 0383  KEGG SSDB Best Search Result: toc:Toce 0383
siv:SSIL_3403 methylmalonyl-CoA mutase, N-terminal doma K11942 1080 106 ( -) 30 0.305 131 -, 1 ssil:SOLI23_01420 methylmalonyl- ... mjd:JDM601_0734 acetolactate synthase IlvG 568 106 ( -) 30 0.300 140 ,-, 1 mlq:ASQ50_14520 hypothetical protein 797 106 ( 3) 30 ... dco:SAMEA4475696_0908 Methylmalonyl-CoA mutase small su K01847 660 115 ( -) 32 0.307 88 -, 1 ham:HALO0230 Ammonium transporter ... CoA mutase K11942 1080 106 ( -) 30 0.305 131 -, 1 sve:SVEN_2918 hypothetical protein 3599 106 ( -) 30 0.343 105 ,-, 1 swp:swp_ ...
more infohttp://www.kegg.jp/ssdb-bin/ssdb_best?org_gene=toc:Toce_0383
LIGNOCELLULOSIC HYDROLYSATES AS FEEDSTOCKS FOR ISOBUTANOL FERMENTATION - Patent application  LIGNOCELLULOSIC HYDROLYSATES AS FEEDSTOCKS FOR ISOBUTANOL FERMENTATION - Patent application
... pyruvate to alpha-acetolactate; (b) alpha-acetolactate to acetoin; (c) acetoin to 3-amino-2-butanol; (d) 3-amino-2-butanol to 3 ... In some embodiments, the microorganism comprises polynucleotides encoding polypeptides having isobutyryl-CoA mutase, ... pyruvate to alpha-acetolactate; (b) alpha-acetolactate to acetoin; (c) acetoin to 3-amino-2-butanol; (d) 3-amino-2-butanol to 3 ... pyruvate to alpha-acetolactate; (b) alpha-acetolactate to acetoin; (c) acetoin to 3-amino-2-butanol; (d) 3-amino-2-butanol to 3 ...
more infohttp://www.patentsencyclopedia.com/app/20130035515
PONSTAN 500MG/TAB ΕΠΙΚΑΛΥΜΜΕΝΟ ΜΕ ΛΕΠΤΟ ΥΜΕΝΙΟ ΔΙΣΚΙΟ | myHealthbox  PONSTAN 500MG/TAB ΕΠΙΚΑΛΥΜΜΕΝΟ ΜΕ ΛΕΠΤΟ ΥΜΕΝΙΟ ΔΙΣΚΙΟ | myHealthbox
Published on: Wed, 14 Nov 2018 The food enzyme acetolactate decarboxylase (α‐acetolactate decarboxylase; EC 4.1.1.5) is ... Orphan designation: Modified mRNA encoding human methylmalonyl-coenzyme A mutase encapsulated into lipid nanoparticles, for the ... This acetolactate decarboxylase is intended to be used in distilled alcohol production and brewing processes. Residual amounts ... Safety evaluation of the food enzyme acetolactate decarboxylase from a genetically modified Bacillus licheniformis (strain NZYM ...
more infohttps://myhealthbox.eu/el/%CF%86%CE%AC%CF%81%CE%BC%CE%B1%CE%BA%CE%BF/ponstan-500mg-tab-%CE%B5%CF%80%CE%B9%CE%BA%CE%B1%CE%BB%CF%85%CE%BC%CE%BC%CE%B5%CE%BD%CE%BF-%CE%BC%CE%B5-%CE%BB%CE%B5%CF%80%CF%84%CE%BF-%CF%85%CE%BC%CE%B5%CE%BD%CE%B9%CE%BF-%CE%B4%CE%B9%CF%83%CE%BA%CE%B9%CE%BF/1028664
IMP: Integrative Multi-species Prediction  IMP: Integrative Multi-species Prediction
ilvB (bacterial acetolactate synthase)-like. 0.014. HPGDS. hematopoietic prostaglandin D synthase. 0.014. ... phosphoglycerate mutase 1 (brain). 0.012. FRZB. frizzled-related protein. 0.012. GJA4. gap junction protein, alpha 4, 37kDa. ... lymphocyte cytosolic protein 2 (SH2 domain containing leukocyte protein of 76kDa). 0.167. ... v-erb-b2 erythroblastic leukemia viral oncogene homolog 2, neuro/glioblastoma derived oncogene homolog (avian). 0.372. ...
more infohttp://imp.princeton.edu/predictions/process/human-context-global/8059/?gene=14179
Stimulation of plant growth and biocontrol by Bacillus amyloliquefaciens subsp. plantarum FZB42 engineered for improved action ...  Stimulation of plant growth and biocontrol by Bacillus amyloliquefaciens subsp. plantarum FZB42 engineered for improved action ...
Acetolactate synthase, synthesis of 2,3-butanediol, plant growth promotion, elicitation of plant ISR ... 3-Bisphosphoglycerate-independent phosphoglycerate mutase Pgm. RBAM_008330. acoL Acetoin dehydrogenase E3 (dihydrolipoamide ... 2, pp. 883-898Google Scholar. *. He P, Hao K, Blom J, Rueckert C, Vater J, Mao Z, Wu Y, Hou M, He P, He Y, Borriss R: Genome ... 2, pp. 561-573Google Scholar. *. Alfano JR, Collmer A: Type 3 secretion system effector proteins: double agents in bacterial ...
more infohttps://chembioagro.springeropen.com/articles/10.1186/s40538-014-0012-2
rice.txt  rice.txt
ORYSJ UDP-arabinopyranose mutase 1 (EC 5.4.99.30) (OsUAM1) (Reversibly glycosylated polypeptide 1) (UDP-L-arabinose mutase 1) [ ... ORYSJ Acetolactate synthase 1, chloroplastic precursor (EC 2.2.1.6) (Acetohydroxy-acid synthase 1) [ALS1] [LOC_Os02g30630] [ ... ORYSJ UDP-arabinopyranose mutase 3 (EC 5.4.99.30) (OsUAM3) (Reversibly glycosylated polypeptide 3) (UDP-L-arabinose mutase 3) [ ... ORYSJ Probable acetolactate synthase 2, chloroplastic precursor (EC 2.2.1.6) (Acetohydroxy-acid synthase 2) [ALS2] [LOC_ ...
more infohttp://www.uniprot.org/docs/rice
  • We present an in vivo regulatory model of BCAA homeostasis derived from analysis of feedback-resistant Arabidopsis thaliana mutants for the three allosteric committed enzymes in the biosynthetic network: threonine deaminase (also named l - O -methylthreonine resistant 1 [OMR, acetohydroxyacid synthase small subunit 2 (AHASS2), and isopropylmalate synthase 1 (IPMS1). (plantcell.org)
  • The de novo synthesis of BCAAs has been an historical object of attention for two main reasons: this pathway is a known target for at least five independent classes of inhibitory herbicides [ 2 ] and, secondly, animals lack the necessary genes encoding enzymes for BCAA synthesis thus requiring that this class of essential amino acids be obtained via dietary intake. (biomedcentral.com)
  • All redox reactions take place in the hydrophilic domain of complex I. NADH initially binds to complex I, and transfers two electrons to the flavin mononucleotide (FMN) prosthetic group of the enzyme, creating FMNH 2 . (wikipedia.org)
  • Therefore, a better understanding of the molecular mechanisms related to the stress adaptation and technical performance of O. oeni is crucial for the characterization and selection of strains for industrial purposes [ 2 , 3 ]. (royalsocietypublishing.org)
  • To achieve our aims we reduced the complex system shown in Figure 1 to the version shown in Figure 2. (igem.org)
  • Four different B. subtilis sugar-specific transport systems representing the four PTS classes (see Fig. 2 ) are shown. (asmscience.org)
  • It revealed that 42 electrons are needed for the production of one isobutanol molecule from CO 2 . (igem.org)