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.
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.
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.
An enzyme that catalyzes the conversion of 2-phospho-D-glycerate to 3-phospho-D-glycerate. EC 5.4.2.1.
Enzymes that catalyze the cleavage of a carbon-carbon bond of a 3-hydroxy acid. (Dorland, 28th ed) EC 4.1.3.
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.
Pesticides used to destroy unwanted vegetation, especially various types of weeds, grasses (POACEAE), and woody plants. Some plants develop HERBICIDE RESISTANCE.
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.
A product of fermentation. It is a component of the butanediol cycle in microorganisms. In mammals it is oxidized to carbon dioxide.
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.
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 which have a branched carbon chain.
Diminished or failed response of PLANTS to HERBICIDES.
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.
Salts and esters of hydroxybutyric acid.
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.
Salts or esters of LACTIC ACID containing the general formula CH3CHOHCOOR.
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.
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)
Derivatives of BUTYRIC ACID. Included under this heading are a broad variety of acid forms, salts, esters, and amides that contain the carboxypropane structure.

The yeast A kinases differentially regulate iron uptake and respiratory function. (1/13)

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)

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

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)

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

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)

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

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)

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

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)

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

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)

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

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)

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

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)

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Butamax suggests that a broad construction is most consistent with the intrinsic evidence and skill in the art, namely, an enzyme that is structurally similar to acetohydroxy acid isomeroreductase or ketol acid reductoisomerase [KARI] enzymes 1 known by the EC number 1.1.1.86 2 and that converts acetolactate to 2,3-dihydroxyisovalerate. (D.I. 492 at 9) Under this construction, to determine whether an enzyme literally meets the claim term, a skilled artisan would: (1) compare the enzymes amino acid sequence to the sequences of known KARI enzymes having EC number 1.1.1.86 (D.I. 492 at 10; [p. 599] D.I. 494 at ¶ 45); and (2) test the enzyme for activity using a standard KARI assay, e.g., the assay described in a 1969 reference by Arfin & Umbarger 3 (D.I. 492 at 10; D.I. 495 at ¶¶ 41-43). According to Butamax, [t]his two prong analysis, consistent with the intrinsic evidence, allows a skilled artisan to come to a conclusion that an enzyme literally meets the KARI claim element. (D.I. 492 ...
Our previous studies revealed that the staphylococcal protein Gcp is essential for bacterial growth; however, the essential function of Gcp remains undefined. In this study, we demonstrated that Gcp plays an important role in the modulation of the br
The enzyme can also transfer the acetaldehyde from pyruvate to 2-oxobutanoate, forming 2-ethyl-2-hydroxy-3-oxobutanoate, also known as 2-aceto-2-hydroxybutanoate, a reaction in the biosynthesis of isoleucine ...
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1OZH: The crystal structure of Klebsiella pneumoniae acetolactate synthase with enzyme-bound cofactor and with an unusual intermediate.
Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate.
Flumetsulam (CDX-F0080), CAS98967-40-9, is a high purity and quality chemical. Used as pesticide, reference material, acetolactate synthase inhibitor.
Hi Dr. Nagler, Do you know if living near mold would effect t? Are they not both related to the central nervous system? I am in my first year of t....
The first case of field evolved acetolactate synthase (ALS) inhibiting herbicide resistance in the model plant, mouse-ear cress, was reported in winter wheat fields in Westmoreland County, Virginia. A putative resistant (R) mouse-ear population was assessed for ALS resistance relative to a putative susceptible (S) and a susceptible lab population Columbia (C). Results indicated that the R population needed 23 to >2400 fold rate of thifensulfuron relative to S or C population, and it has evolved cross-resistance to sulfonylureas (SU), triazolopyrimidine sulfonanilides (TP), and sulfonylaminocarbonyltriazolinones (SCT). Further studies sequenced the whole genome for four field populations, representing two locations and two resistance levels (high and low) per location, to characterize the genetic mechanism of ALS resistance. The results revealed that all populations contained mutations in the ALS gene at the Pro197 site, although the Pro was substituted by Phe in one location and Thr in the ...
Strain Information. E. coli K-12 MG1655. Description. Genotype: F- lambda- ilvG- rfb-50 rph-1. Serotype: OR:H48:K- This strain was sequenced by the Blattner laboratory because it approximates wild-type E. coli and has been maintained as a laboratory strain with minimal genetic manipulation, having only been cured of the temperate bacteriophage lambda and F plasmid by means of ultraviolet light and acridine orange, respectively. (Blattner, et al. 1997). The mutations listed in the genotype are present in most K-12 strains and were probably acquired early in the history of the laboratory strain. A frameshift at the end of rph results in decreased pyrE expression and a mild pyrimidine starvation, such that the strain grows 10 to 15% more slowly in pyrimidine-free medium than in medium containing uracil (Jensen 1993). The ilvG- mutation is a frameshift that knocks out acetohydroxy acid synthase II (Lawther, et al. 1982). The rfb-50 mutation is an IS5 insertion that results in the absence of ...
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... phosphoglycerate mutase MeSH D08.811.399.894.200 - amino acid isomerases MeSH D08.811.399.894.200.200 - alanine racemase MeSH ... acetolactate synthase MeSH D08.811.913.200.650 - transaldolase MeSH D08.811.913.200.825 - transketolase MeSH D08.811.913.225. ... chorismate mutase MeSH D08.811.399.520.250.500 - prephenate dehydratase MeSH D08.811.399.520.250.750 - prephenate dehydrogenase ... bisphosphoglycerate mutase MeSH D08.811.399.520.750.625 - phosphoglucomutase MeSH D08.811.399.520.750.700 - ...
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, ...
... phosphoglucosamine mutase EC 5.4.2.11: phosphoglycerate mutase EC 5.4.2.12: phosphoglycerate mutase EC 5.4.3.1: deleted EC 5.4. ... 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- ... methylaspartate mutase EC 5.4.99.2: methylmalonyl-CoA mutase EC 5.4.99.3: 2-acetolactate mutase EC 5.4.99.4: 2- ...
The second step involves the NADPH+-dependent reduction of α-acetolactate and migration of methyl groups to produce α, β- ... This process is mediated by a phenylalanine (PheA) or tyrosine (TyrA) specific chorismate mutase-prephenate dehydrogenase. PheA ... It begins with the condensation of two equivalents of pyruvate catalyzed by acetohydroxy acid synthase yielding α-acetolactate ... Enzymes involved in this biosynthesis include acetolactate synthase (also known as acetohydroxy acid synthase), acetohydroxy ...
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, ...
Category:EC 5.4 (intramolecular transferases -- mutases)Edit. *Category:EC 5.4.2 *Phosphoglucomutase (EC 5.4.2.2) ... Acetolactate synthase EC 2.2.1.6. *2-Succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase EC 2.2.1.9 ... Category:EC 1.3.2 (with a cytochrome as acceptor). *Category:EC 1.3.3 (with oxygen as acceptor) *Protoporphyrinogen oxidase EC ... Category:EC 1.4 (act on the CH-NH2 group of donors)Edit. *Category:EC 1.4.3 *Monoamine oxidase EC 1.4.3.4 ...
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, ...
... phosphoglycerate mutase MeSH D08.811.399.894.200 - amino acid isomerases MeSH D08.811.399.894.200.200 - alanine racemase MeSH ... acetolactate synthase MeSH D08.811.913.200.650 - transaldolase MeSH D08.811.913.200.825 - transketolase MeSH D08.811.913.225. ... chorismate mutase MeSH D08.811.399.520.250.500 - prephenate dehydratase MeSH D08.811.399.520.250.750 - prephenate dehydrogenase ... bisphosphoglycerate mutase MeSH D08.811.399.520.750.625 - phosphoglucomutase MeSH D08.811.399.520.750.700 - ...
Enzyme (substance) {90668006 , SNOMED-CT } Substance with mutase mechanism of action (substance) {130945002 , SNOMED-CT } ...
5.4.99.13 isobutyryl-CoA mutase 5.4.99.14 4-carboxymethyl-4-methylbutenolide mutase ...
2-Fluoro-2-deoxyglucose use Fluorodeoxyglucose F18 2H-Benzo(a)quinolizin-2-ol, 2-Ethyl-1,3,4,6,7,11b-hexahydro-3-isobutyl-9,10- ... 2-Amino-5-phosphonovaleric Acid use 2-Amino-5-phosphonovalerate 2-Amino-6-(1,2,3-trihydroxypropyl)-4(3H)-pteridinone use ... 2-Oxoisovalerate Dehydrogenase (Lipoamide) use 3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide) 2-PAM Compounds use ... 2-Chloroethyl Alcohol use Ethylene Chlorohydrin 2-Dehydro-3-Deoxyphosphoheptonate Aldolase use 3-Deoxy-7-Phosphoheptulonate ...
2-Amino-5-phosphonovaleric Acid use 2-Amino-5-phosphonovalerate 2-Amino-6-(1,2,3-trihydroxypropyl)-4(3H)-pteridinone use ... 2-Dehydro-3-Deoxyphosphoheptonate Aldolase use 3-Deoxy-7-Phosphoheptulonate Synthase 2-Fluoro-2-deoxy-D-glucose use ... 2,6-Dichlorophenolindophenol use 2,6-Dichloroindophenol 3 beta-Hydroxy-delta-5-Steroid Dehydrogenase use Progesterone Reductase ... 2-Oxoisovalerate Dehydrogenase (Lipoamide) use 3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide) 2-PAM Compounds use ...
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 ...
Substance with mutase mechanism of action (substance). Code System Preferred Concept Name. Substance with mutase mechanism of ... Methylaspartate mutase (substance) {83682009 , SNOMED-CT } Methylmalonyl-coenzyme A mutase (substance) {56024005 , SNOMED-CT } ... Bisphosphoglycerate mutase (substance) {2168009 , SNOMED-CT } Chorismate mutase (substance) {4067000 , SNOMED-CT } Cycloartenol ... Substance with mutase mechanism of action (substance) {130945002 , SNOMED-CT } Parent/Child (Relationship Type) 2-acetolactate ...
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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) ...
... and acetolactate synthase (T478_0886, T478_0887), and vitamin B7 is a required coenzyme for the acetyl-/propionyl-CoA ... methylmalonyl-CoA mutase (T478_0628), methionine synthase (T478_1032), and ribonucleoside reductase (T478_1341). The genome ... Reductive N2O production from NO2− has been demonstrated in enrichment cultures of Ca. N. brevis (10) and in N. maritimus (30, ... 2), and Ca. N. brevis had higher recruitment in nearly twice as many samples (SI Appendix, Dataset S4). Two regions of the Ca. ...
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. ...
... 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 ...
2H-Benzo(a)quinolizin-2-ol, 2-Ethyl-1,3,4,6,7,11b-hexahydro-3-isobutyl-9,10-dimethoxy- ... 3-Pyridinecarboxylic acid, 1,4-dihydro-2,6-dimethyl-5-nitro-4-(2-(trifluoromethyl)phenyl)-, Methyl ester ... Mutase. 2-Acetylaminofluorene. 2-Alanyl-Leucine Enkephalin use Enkephalin, Leucine-2-Alanine ... 3,4-Dichloro-N-methyl-N-(2-(1-pyrrolidinyl)-cyclohexyl)-benzeneacetamide, (trans)-Isomer ...
UDP-galactopyranose mutase;gene=glf sequence26 Prodigal:2.6 CDS 5603 6340 . - 0 ID=ERR570114_01861;locus_tag=ERR570114_01861; ... acetolactate synthase large subunit;gene=ilvB sequence05 Prodigal:2.6 CDS 25650 25865 . - 0 ID=ERR570114_00842;locus_tag= ... phosphoglycerate mutase;gene=gpmB_1 sequence04 Prodigal:2.6 CDS 29686 31554 . - 0 ID=ERR570114_00701;locus_tag=ERR570114_00701; ... phosphoglycerate mutase;gene=gpmB_4 sequence06 Prodigal:2.6 CDS 35104 36231 . - 0 ID=ERR570114_00979;locus_tag=ERR570114_00979; ...
... "acetolactate synthase large subunit" /transl_table=11 /translation="MTEEKYYGANAIVDSLINHDVKFVFGIPGAKIDRVFELLEHSKNS ... "UDP-galactopyranose mutase" /transl_table=11 /translation="MNYLIVGSGLFGAVFAHEAAKRGNKVTVIEQRDHLAGNIYTKEVD ... FEATURES Location/Qualifiers source 1..416916 /mol_type="genomic DNA" /organism="Lactobacillus gasseri" /strain="G220_6_2" gene ... FEATURES Location/Qualifiers source 1..328102 /mol_type="genomic DNA" /organism="Lactobacillus gasseri" /strain="G220_6_2" gene ...
  • 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 [OMR1]), acetohydroxyacid synthase small subunit 2 (AHASS2), and isopropylmalate synthase 1 (IPMS1). (plantcell.org)
  • More recently, genetic engineering of the glycolytic pathway has been used to improve production, involving modulated function of e.g. triose phosphate isomerase, phosphoglycerate mutase, PDC or alcohol dehydrogenase. (scribd.com)
  • 1. The latter is reduced by butanediol dehydrogenase to 2,3-butylene glycol (butanediol), NADH2 acting as H-donor. (fyfo.org)
  • In enzymology, a 2-acetolactate mutase (EC 5.4.99.3) is an enzyme that catalyzes the chemical reaction 2-acetolactate ⇌ {\displaystyle \rightleftharpoons } 3-hydroxy-3-methyl-2-oxobutanoate Hence, this enzyme has one substrate, 2-acetolactate, and one product, 3-hydroxy-3-methyl-2-oxobutanoate. (wikipedia.org)
  • The systematic name of this enzyme class is 2-acetolactate methylmutase. (wikipedia.org)
  • Acetolactate synthase (ALS) is the first enzyme in the BCAA synthesis pathway. (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)
  • Next, succinyl-CoA produces methyl malonyl- CoA by the action of a vitamin B12-linked enzyme methyl malonyl mutase which catalyses an intra-molecular rearrangement. (fyfo.org)
  • Other names in common use include acetolactate mutase, and acetohydroxy acid isomerase. (wikipedia.org)
  • During isoleucine biosynthesis L-threonine is deaminated to 2-ketobutyrate by the IlvA protein. (biomedcentral.com)
  • Dehydrogenases dedicated to L-tyrosine (TYR) biosynthesis comprise a family of TyrA homologs that have different specificities for the cyclohexadienyl substrate: ones specific for L-arogenate (AGN), ones specific for prephenate (PPA), and those that are able to use both [ 1 , 2 ]. (biomedcentral.com)
  • This results, for instance, in three different types of acetolactate synthases (EC:2.2.1.6) acting in the biosynthesis of L-valine and L-leucine in Escherichia coli . (biomedcentral.com)
  • 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)
  • According to our pathway map there are 42 electrons needed for the production of one molecule isobutanol, if CO 2 is used as sole carbon source. (igem.org)
  • Other cold-inducible proteins in E. coli include initiation factor 2 (IF2) ( 7 , 13 ), ribosomal binding factor A (RbfA) ( 22 ), and DEAD-box RNA helicase ( 4 , 23 , 37 ), all of which associate with the ribosome and are believed to play a role in protein synthesis. (asm.org)
  • The gene encoding the TdcF protein of E. coli , a YjgF/YER057c/UK114 family member, resides in an operon that strongly suggests a role in the metabolism of 2-ketobutyrate for this protein. (biomedcentral.com)
  • 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)
  • We show that TdcF is capable of binding several low molecular weight metabolites bearing a carboxylate group, although the interaction with 2-ketobutyrate appears to be the most well defined. (biomedcentral.com)
  • 2. The recombinant solventogenic organism of claim 1, wherein the second organism is a Clostridium sp. (patentsencyclopedia.com)
  • 2) Optimizing the cultural conditions required for obtaining rapid & Massive growth of these organism in laboratory & in frequenter. (fyfo.org)
  • 9. The recombinant solventogenic organism of claim 8, wherein the gene comprises a nucleotide sequence having at least 80% homology to the sequence selected from the group consisting of Adh (SEQ ID NO: 1), Bcd (SEQ ID NO: 2), and Buk (SEQ ID NO: 3) or complements thereof. (patentsencyclopedia.com)
  • 14. The recombinant solventogenic organism of claim 9, wherein the gene comprises a sequence at least 80% homologous to SEQ ID NO: 2 or complement thereof. (patentsencyclopedia.com)
  • The download creating web pages for dummies influences with types of effects currently Unfearing with cereals of prostatitis mutase and following energy from B12 women to the latest code on a evolutionary account. (fourpawspetresort.ca)
  • To achieve our aims we reduced the complex system shown in Figure 1 to the version shown in Figure 2. (igem.org)
  • It revealed that 42 electrons are needed for the production of one isobutanol molecule from CO 2 . (igem.org)