An enzyme that catalyzes the first step in the biosynthetic pathway to LEUCINE, forming isopropyl malate from acetyl-CoA and alpha-ketoisovaleric acid. This enzyme was formerly listed as EC 4.1.3.12.
An NAD+ dependent enzyme that catalyzes the oxidation of 3-carboxy-2-hydroxy-4-methylpentanoate to 3-carboxy-4-methyl-2-oxopentanoate. It is involved in the biosynthesis of VALINE; LEUCINE; and ISOLEUCINE.
A species of gram-positive bacteria in the family Clostridiaceae. It is distinctive for its ability to ferment ETHANOL to caproic acid.
Enzymes that catalyze the cleavage of a carbon-carbon bond of a 3-hydroxy acid. (Dorland, 28th ed) EC 4.1.3.
A subclass of enzymes which includes all dehydrogenases acting on primary and secondary alcohols as well as hemiacetals. They are further classified according to the acceptor which can be NAD+ or NADP+ (subclass 1.1.1), cytochrome (1.1.2), oxygen (1.1.3), quinone (1.1.5), or another acceptor (1.1.99).
A species of gram-negative, aerobic, rod-shaped bacteria found in hot springs of neutral to alkaline pH, as well as in hot-water heaters.
Gram-negative aerobic rods found in warm water (40-79 degrees C) such as hot springs, hot water tanks, and thermally polluted rivers.

Inhibition of Escherichia coli isoleucine biosynthesis by isoleucine tetrazole. (1/43)

Growth of a derivative of Escherichia coli K-10 was strongly inhibited by 2 times 10(-4) M L-5(1-amino-2-methylbutyl)-tetrazole (isoleucine tetrazole). Growth inhibition was reversed by isoleucine, threonine, glycyl-L-isoleucine, or glycyl-L-threonine, and, in a valine-resistant mutant, by L-valine. Partial reversal of growth inhibiton was effected by L-leucine, L-methionine, or L-homoserine. The tetrazole inhibited the activity of the biosynthetic threonine deaminase (EC 4.2.1.16 L-threonine hydrolyase [deaminating]), the inhibition being relieved by L-valine. The tetrazole also inhibited isoleucyl-transfer ribonucleic acid (tRNA) synthetase (EC 6.1.1.5 L-isoleucine: tRNA ligase [adenosine monophosphate]), but was without effect on the activities of alpha-isopropylmalate synthetase or acetohydroxy acid synthetase. One class of isoleucine tetrazole-resistant mutants produced biosynthetic threonine deaminases which were no longer subject to feedback inhibition by either isoleucine or the tetrazole.  (+info)

Reversible, coenzyme-A-mediated inactivation of biosynthetic condensing enzymes in yeast: a possible regulatory mechanism. (2/43)

alpha-Isopropylmalate synthase [3-hydroxy-4-methyl-3-carboxyvalerate 2-oxo-3-methylbutyrate-lyase (CoA-acetylating); EC 4.1.3.12], the enzyme catalyzing the first committed step in leucine biosynthesis, and homocitrate synthase [3-hydroxy-3-carboxyadipate 2-oxoglutarate-lyase (CoA-acetylating); EC 4.1.3.21], the first enzyme in lysine biosynthesis in yeast, are rapidly inactivated in the presence of low concentrations of coenzyme A, a product of both reactions. Closely related compounds like 3-dephospho-coenzyme A or oxidized coenzyme A are almost without effect, as are other sulfhydryl compounds. Citrate (si)-synthase [citrate oxaloacetate-lyase (pro-3S-CH2-COO-minus leads to acetyl-CoA); EC 4.1.3.7] appears to be completely resistant against inactivation by coenzyme A. Inactivated alpha-isopropylmalate and homocitrate synthases can be reactivated by dialysis, but not by adding excess substrate. Protection against coenzyme-A-mediated inactivation is provided by relatively high concentrations of the alpha-ketoacid substrate or the specific end product inhibitor of each of the two enzymes. The coenzyme-A-mediated inactivation of alpha-isopropylmalate synthase has been more closely investigated. It requires the presence of divalent metal ions, with Zn++being most effective. The inactivation does not require molecular oxygen. It occurs in the presence of low concentrations of substrates and is observed in toluene-treated cells. These results, together with evidence that alpha-isopropylmalate synthase and homocitrate synthase are located in the mitochondria, suggest a mechanism by which increasing intra-mitochondrial coenzyme A concentrations might serve as a signal of decreasing acetyl-coenzyme A levels, triggering a temporary inactivation of biosynthetic acetyl-coenzyme A-consuming reactions in order to channel the available acetyl-coenzyme A into the citrate cycle.  (+info)

A gene controlling variation in Arabidopsis glucosinolate composition is part of the methionine chain elongation pathway. (3/43)

Arabidopsis and other Brassicaceae produce an enormous diversity of aliphatic glucosinolates, a group of methionine (Met)-derived plant secondary compounds containing a beta-thio-glucose moiety, a sulfonated oxime, and a variable side chain. We fine-scale mapped GSL-ELONG, a locus controlling variation in the side-chain length of aliphatic glucosinolates. Within this locus, a polymorphic gene was identified that determines whether Met is extended predominantly by either one or by two methylene groups to produce aliphatic glucosinolates with either three- or four-carbon side chains. Two allelic mutants deficient in four-carbon side-chain glucosinolates were shown to contain independent missense mutations within this gene. In cell-free enzyme assays, a heterologously expressed cDNA from this locus was capable of condensing 2-oxo-4-methylthiobutanoic acid with acetyl-coenzyme A, the initial reaction in Met chain elongation. The gene methylthioalkylmalate synthase1 (MAM1) is a member of a gene family sharing approximately 60% amino acid sequence similarity with 2-isopropylmalate synthase, an enzyme of leucine biosynthesis that condenses 2-oxo-3-methylbutanoate with acetyl-coenzyme A.  (+info)

Leucine biosynthesis in fungi: entering metabolism through the back door. (4/43)

After exploring evolutionary aspects of branched-chain amino acid biosynthesis, the review focuses on the extended leucine biosynthetic pathway as it operates in Saccharomyces cerevisiae. First, the genes and enzymes specific for the leucine pathway are considered: LEU4 and LEU9 (encoding the alpha-isopropylmalate synthase isoenzymes), LEU1 (isopropylmalate isomerase), and LEU2 (beta-isopropylmalate dehydrogenase). Emphasis is given to the unusual distribution of the branched-chain amino acid pathway enzymes between mitochondrial matrix and cytosol, on the newly defined role of Leu5p, and on regulatory mechanisms governing gene expression and enzyme activity, including new evidence for the metabolic importance of the regulation of alpha-isopropylmalate synthase by coenzyme A. Next, structure-function relationships of the transcriptional regulator Leu3p are addressed, defining its dual role as activator and repressor and discussing evidence in support of the self-masking model. Recent data pointing at a more extended Leu3p regulon are discussed. An overview of the layered controls of the extended leucine pathway is provided that includes a description of the newly recognized roles of Ilv5p and Bat1p in maintaining mitochondrial integrity. Finally, branched-chain amino acid biosynthesis and its regulation in other fungi are summarized, the question of leucine as metabolic signal is addressed, and possible directions of future research in this area are outlined.  (+info)

Repression of the tyrosine, lysine, and methionine biosynthetic pathways in a hisT mutant of Salmonella typhimurium. (5/43)

A comparison was made of the repressibility of certain enzymes in the tyrosine, methionine, and lysine biosynthetic pathways in wild-type Salmonella typhimurium and a hisT mutant. The results show that (i) tyrosine represses the synthesis of the tyrosine-sensitive 3-deoxy-D-arabino-heptulsonic acid 7-phosphate synthetase and the tyrosine aminotransferase to the same extent in a hisT mutant as in wild type and (ii) there is no detectable alteration in the extent to which methionine represses O-succinylhomoserine synthetase or in the extent to which lysine represses the lysine-sensitive beta-aspartokinase as a result of the hisT mutation.  (+info)

Crystal structure of LeuA from Mycobacterium tuberculosis, a key enzyme in leucine biosynthesis. (6/43)

The leucine biosynthetic pathway is essential for the growth of Mycobacterium tuberculosis and is a potential target for the design of new anti-tuberculosis drugs. The crystal structure of alpha-isopropylmalate synthase, which catalyzes the first committed step in this pathway, has been determined by multiwavelength anomalous dispersion methods and refined at 2.0-A resolution in complex with its substrate alpha-ketoisovalerate. The structure reveals a tightly associated, domain-swapped dimer in which each monomer comprises an (alpha/beta)(8) TIM barrel catalytic domain, a helical linker domain, and a regulatory domain of novel fold. Mutational and crystallographic data indicate the latter as the site for leucine feedback inhibition of activity. Domain swapping enables the linker domain of one monomer to sit over the catalytic domain of the other, inserting residues into the active site that may be important in catalysis. The alpha-ketoisovalerate substrate binds to an active site zinc ion, adjacent to a cavity that can accommodate acetyl-CoA. Sequence and structural similarities point to a catalytic mechanism similar to that of malate synthase and an evolutionary relationship with an aldolase that catalyzes the reverse reaction on a similar substrate.  (+info)

Isoleucine biosynthesis in Leptospira interrogans serotype lai strain 56601 proceeds via a threonine-independent pathway. (7/43)

Three leuA-like protein-coding sequences were identified in Leptospira interrogans. One of these, the cimA gene, was shown to encode citramalate synthase (EC 4.1.3.-). The other two encoded alpha-isopropylmalate synthase (EC 4.1.3.12). Expressed in Escherichia coli, the citramalate synthase was purified and characterized. Although its activity was relatively low, it was strictly specific for pyruvate as the keto acid substrate. Unlike the citramalate synthase of the thermophile Methanococcus jannaschii, the L. interrogans enzyme is temperature sensitive but exhibits a much lower K(m) (0.04 mM) for pyruvate. The reaction product was characterized as (R)-citramalate, and the proposed beta-methyl-d-malate pathway was further confirmed by demonstrating that citraconate was the substrate for the following reaction. This alternative pathway for isoleucine biosynthesis from pyruvate was analyzed both in vitro by assays of leptospiral isopropylmalate isomerase (EC 4.2.1.33) and beta-isopropylmalate dehydrogenase (EC 1.1.1.85) in E. coli extracts bearing the corresponding clones and in vivo by complementation of E. coli ilvA, leuC/D, and leuB mutants. Thus, the existence of a leucine-like pathway for isoleucine biosynthesis in L. interrogans under physiological conditions was unequivocally proven. Significant variations in either the enzymatic activities or mRNA levels of the cimA and leuA genes were detected in L. interrogans grown on minimal medium supplemented with different levels of the corresponding amino acids or in cells grown on serum-containing rich medium. The similarity of this metabolic pathway in leptospires and archaea is consistent with the evolutionarily primitive status of the eubacterial spirochetes.  (+info)

Asp578 in LEU4p is one of the key residues for leucine feedback inhibition release in sake yeast. (8/43)

We identified a new mutation, Asp578Tyr, in alpha-isopropylmalate synthase (a LEU4 gene product) that releases leucine feedback inhibition and causes hyperproduction of isoamyl alcohol (i-AmOH) in sake yeast. Spontaneous sake yeast mutants that express resistance to 5,5,5-trifluoro-DL-leucine (TFL) were isolated, and a mutant strain, TFL20, was characterized at the genetic and biochemical levels. An enzyme assay for alpha-isopropylmalate synthase showed that strain TFL20 was released from feedback inhibition by L-leucine. Furthermore, DNA sequencing of the LEU4 gene for a haploid of the mutant TFL20 revealed that aspartic acid in position 578 changes to tyrosine. A comparison of the three-dimensional structures of wild-type LEU4p and mutant LEU4D578Yp by the homology modeling method showed that Asp578 is important for leucine feedback inhibition. We conclude that the mutation from Asp to Tyr in 578 is a novel change causing release from leucine feedback inhibition.  (+info)

2-Isopropylmalate synthase is an enzyme that catalyzes the condensation of a molecule of acetyl-CoA with a molecule of 3-isopropylmalate to form a molecule of 2-isopropylmalate. This reaction is part of the leucine biosynthesis pathway in bacteria, fungi, and plants. The enzyme is also known as 2-isopropylmalate isomerase-ligase or simply isopropylmalate synthase. It requires the cofactor CoA and is inhibited by leucine, a product of the pathway. Deficiency in this enzyme can lead to a rare genetic disorder called 2-isopropylmalate synthase deficiency, which is characterized by developmental delay, seizures, and metabolic acidosis.

3-Isopropylmalate dehydrogenase (IPMDH) is an enzyme that plays a crucial role in the metabolic pathway known as leucine biosynthesis. This enzyme catalyzes the third step of this pathway, which involves the oxidative decarboxylation of 3-isopropylmalate to form 2-isopropylmalate, while simultaneously reducing NAD+ to NADH. The reaction is as follows:

3-Isopropylmalate + NAD+ -> 2-isopropylmalate + CO2 + NADH

The IPMDH enzyme is found in various organisms, including bacteria, yeast, and plants. In humans, defects or mutations in the gene encoding this enzyme can lead to a rare genetic disorder called 3-isopropylmalate dehydrogenase deficiency. This condition results in elevated levels of leucine and other intermediates in the leucine biosynthesis pathway, which can cause neurological symptoms such as developmental delay, seizures, and hypotonia (low muscle tone).

'Clostridium kluyveri' is a type of anaerobic, spore-forming bacterium that is commonly found in the environment, such as in soil and sewage. It is a gram-positive bacterium that can cause opportunistic infections in humans, particularly in individuals with compromised immune systems.

The bacterium is named after the Dutch microbiologist Albert Jan Kluyver, who made significant contributions to the field of microbiology in the early 20th century. 'Clostridium kluyveri' is known for its ability to ferment a variety of substrates and produce acetate, butyrate, and hydrogen as end products.

Infections caused by 'Clostridium kluyveri' are rare but can include bacteremia, brain abscesses, and soft tissue infections. Treatment typically involves the use of antibiotics that are active against anaerobic bacteria, such as metronidazole or clindamycin.

Oxo-acid lyases are a class of enzymes that catalyze the cleavage of a carbon-carbon bond in an oxo-acid to give a molecule with a carbonyl group and a carbanion, which then reacts non-enzymatically with a proton to form a new double bond. The reaction is reversible, and the enzyme can also catalyze the reverse reaction.

Oxo-acid lyases play important roles in various metabolic pathways, such as the citric acid cycle, glyoxylate cycle, and the degradation of certain amino acids. These enzymes are characterized by the presence of a conserved catalytic mechanism involving a nucleophilic attack on the carbonyl carbon atom of the oxo-acid substrate.

The International Union of Biochemistry and Molecular Biology (IUBMB) has classified oxo-acid lyases under EC 4.1.3, which includes enzymes that catalyze the formation of a carbon-carbon bond by means other than carbon-carbon bond formation to an enolate or carbonion, a carbanionic fragment, or a Michael acceptor.

Alcohol oxidoreductases are a class of enzymes that catalyze the oxidation of alcohols to aldehydes or ketones, while reducing nicotinamide adenine dinucleotide (NAD+) to NADH. These enzymes play an important role in the metabolism of alcohols and other organic compounds in living organisms.

The most well-known example of an alcohol oxidoreductase is alcohol dehydrogenase (ADH), which is responsible for the oxidation of ethanol to acetaldehyde in the liver during the metabolism of alcoholic beverages. Other examples include aldehyde dehydrogenases (ALDH) and sorbitol dehydrogenase (SDH).

These enzymes are important targets for the development of drugs used to treat alcohol use disorder, as inhibiting their activity can help to reduce the rate of ethanol metabolism and the severity of its effects on the body.

'Thermus thermophilus' is not a medical term, but a scientific name for a species of bacteria. It is commonly used in molecular biology and genetics research. Here is the biological definition:

'Thermus thermophilus' is a gram-negative, rod-shaped, thermophilic bacterium found in hot springs and other high-temperature environments. Its optimum growth temperature ranges from 65 to 70°C (149-158°F), with some strains able to grow at temperatures as high as 85°C (185°F). The bacterium's DNA polymerase enzyme, Taq polymerase, is widely used in the Polymerase Chain Reaction (PCR) technique for amplifying and analyzing DNA. 'Thermus thermophilus' has a single circular chromosome and can also have one or more plasmids. Its genome has been fully sequenced, making it an important model organism for studying extremophiles and their adaptations to harsh environments.

"Thermus" is not a medical term, but rather a genus of bacteria that are capable of growing in extreme temperatures. These bacteria are named after the Greek word "therme," which means heat. They are commonly found in hot springs and deep-sea hydrothermal vents, where the temperature can reach up to 70°C (158°F).

Some species of Thermus have been found to produce enzymes that remain active at high temperatures, making them useful in various industrial applications such as molecular biology and DNA amplification techniques like polymerase chain reaction (PCR). However, Thermus itself is not a medical term or concept.

... alpha-isopropylmalate synthase, alpha-isopropylmalic synthetase, isopropylmalate synthase, and isopropylmalate synthetase. This ... Mycobacterium tuberculosis α-isopropylmalate synthase requires a divalent metal ion, of which Mg2+ and Mn2+ give highest ... Kohlhaw G, Leary TR, Umbarger HE (1969). "Alpha-isopropylmalate synthase from Salmonella typhimurium Purification and ... Carvalho LP, Blanchard, JS (2006). "Kinetic and Chemical Mechanism of alpha-Isopropylmalate Synthase from Mycobacterium ...
A systematic name for this compound is 2-aminohexanoic acid. The compound is an isomer of the more common amino acid leucine. ... It arises via the action of 2-isopropylmalate synthase on α-ketobutyrate. The incorporation of Nle into peptides reflects the ...
Specifically they are upstream of genes encoding 2-isopropylmalate synthase and related genes, which participate in the ...
... (isopropylmalate) is an intermediate in the biosynthesis of leucine, synthesized from oxoisovalerate by 2- ... isopropylmalate synthase and converted into isopropyl-3-oxosuccinate by 3-isopropylmalate dehydrogenase. Two isomers are ... and these are interconverted by isopropylmalate dehydratase. Strassman, Murray; Ceci, Louis N. (1963). "Enzymatic Formation of ...
11-diene synthase EC 4.2.3.25: S-linalool synthase EC 4.2.3.26: R-linalool synthase EC 4.2.3.27: isoprene synthase EC 4.2.3.28 ... 3-isopropylmalate dehydratase EC 4.2.1.34: (S)-2-methylmalate dehydratase EC 4.2.1.35: (R)-2-methylmalate dehydratase EC 4.2. ... α-santalene synthase EC 4.2.3.83: β-santalene synthase EC 4.2.3.84: 10-epi-γ-eudesmol synthase EC 4.2.3.85: α-eudesmol synthase ... cubebol synthase EC 4.2.3.92: (+)-γ-cadinene synthase EC 4.2.3.93: δ-guaiene synthase EC 4.2.3.94: γ-curcumene synthase EC 4.2. ...
A series of four more enzymes - isopropylmalate synthase, isopropylmalate isomerase, isopropylmalate dehydrogenase, and ... Acetohydroxyacid synthase is the first enzyme for the parallel pathway performing condensation reaction in both steps - ... acetohydroxyacid synthase, ketoacid reductoisomerase, dihydroxyacid dehydrogenase and aminotransferase. Threonine dehydrogenase ... 16 (2): 520-530. doi:10.1016/j.celrep.2016.05.092. PMC 4947548. PMID 27346343. Cummings NE, Williams EM, Kasza I, Konon EN, ...
... homocitrate synthases, (3) biotin carboxyl carrier proteins, (4) isopropylmalate synthases and (5) acyl-CoA carboxylase. The α- ... The generalized reaction for the NaT-DC family is: R - CO− 2 (in) + H+ (out) and 1 or 2 Na+ (in) ←→ R-H + CO2 (in) and 1 or 2 ... 31 (2): 473-87. doi:10.1046/j.1365-2958.1999.01189.x. PMID 10027965. S2CID 35018668. Balsera M, Buey RM, Li XD (March 2011). " ... 10 (2-4): 105-19. doi:10.1159/000091558. PMID 16645308. S2CID 22898166. Granjon T, Maniti O, Auchli Y, Dahinden P, Buchet R, ...
... riboflavin synthase MeSH D08.811.913.225.825 - spermidine synthase MeSH D08.811.913.225.912 - spermine synthase MeSH D08.811. ... 3-isopropylmalate dehydrogenase MeSH D08.811.682.047.524 - ketol-acid reductoisomerase MeSH D08.811.682.047.551 - lactate ... nitric oxide synthase type i MeSH D08.811.682.664.500.772.500 - nitric oxide synthase type ii MeSH D08.811.682.664.500.772.750 ... glycogen synthase kinases MeSH D08.811.913.696.620.682.700.429.500 - glycogen synthase kinase 3 MeSH D08.811.913.696.620.682. ...
... synthase EC 2.3.3.2: decylcitrate synthase EC 2.3.3.3: citrate (Re)-synthase EC 2.3.3.4: decylhomocitrate synthase EC 2.3.3.5: ... synthase EC 2.4.1.12: cellulose synthase (UDP-forming) EC 2.4.1.13: sucrose synthase EC 2.4.1.14: sucrose-phosphate synthase EC ... squalene synthase EC 2.5.1.22: spermine synthase EC 2.5.1.23: sym-norspermidine synthase EC 2.5.1.24: discadenine synthase EC ... synthase (*) EC 2.3.2.21: cyclo(L-tyrosyl-L-tyrosyl) synthase (*) EC 2.3.2.22: cyclo(L-leucyl-L-leucyl) synthase (*) EC 2.3. ...
α-Isopropylmalate synthase catalyzes this condensation with acetyl CoA to produce α-isopropylmalate. An isomerase converts α- ... isopropylmalate to β-isopropylmalate. The third step is the NAD+-dependent oxidation of β-isopropylmalate catalyzed by a ... Leucine, like valine, regulates the first step of its pathway by inhibiting the action of the α-Isopropylmalate synthase. ... Enzymes involved in this biosynthesis include acetolactate synthase (also known as acetohydroxy acid synthase), acetohydroxy ...
Acetolactate synthase Acetohydroxy acid isomeroreductase Dihydroxyacid dehydratase α-Isopropylmalate synthase α-Isopropylmalate ... 226 (2): 411-8. doi:10.1152/ajplegacy.1974.226.2.411. PMID 4855772. Zanchi NE, Gerlinger-Romero F, Guimarães-Ferreira L, de ... 16 (2): 520-530. doi:10.1016/j.celrep.2016.05.092. PMC 4947548. PMID 27346343. Lynch CJ, Adams SH (December 2014). "Branched- ... 569 (Pt 2): 489-99. doi:10.1113/jphysiol.2005.098004. PMC 1464228. PMID 16195315. Verhoeven S, Vanschoonbeek K, Verdijk LB, ...
... promiscuity can be decreased as was the case of γ-humulene synthase (a sesquiterpene synthase) from Abies grandis that is known ... and the bifunctional isopropylmalate isomerase/homoaconitase from Pyrococcus horikoshii have revealed that active site loop ... Codexis). Another example is the possibility of using the promiscuous activities of cysteine synthase (cysM) towards ... including overexpression of the large component of a synthase in the absence of the amine transferase subunit), pathway bypass ...
... berbamunine synthase EC 1.1.3.35: Now EC 1.14.21.4, salutaridine synthase EC 1.1.3.36: Now EC 1.14.21.5, (S)-canadine synthase ... 3-isopropylmalate dehydrogenase EC 1.1.1.86: ketol-acid reductoisomerase (NADP+) EC 1.1.1.87: homoisocitrate dehydrogenase EC ... clavaminate synthase EC 1.14.11.22: Now EC 1.14.20.5, flavone synthase EC 1.14.11.23: Now EC 1.14.20.6, flavonol synthase EC ... anthocyanidin synthase * EC 1.14.20.5: flavone synthase I * EC 1.14.20.6: flavonol synthase * EC 1.14.20.7: 2-oxoglutarate/L- ...
... alpha-isopropylmalate synthase, alpha-isopropylmalic synthetase, isopropylmalate synthase, and isopropylmalate synthetase. This ... Mycobacterium tuberculosis α-isopropylmalate synthase requires a divalent metal ion, of which Mg2+ and Mn2+ give highest ... Kohlhaw G, Leary TR, Umbarger HE (1969). "Alpha-isopropylmalate synthase from Salmonella typhimurium Purification and ... Carvalho LP, Blanchard, JS (2006). "Kinetic and Chemical Mechanism of alpha-Isopropylmalate Synthase from Mycobacterium ...
BRENDA - The Comprehensive Enzyme Information System
METHYLTHIOALKYMALATE SYNTHASE-LIKE, MYJ24.1, MYJ24_1 ...
Alpha-IPM synthase; Alpha-isopropylmalate synthase ... Belongs to the alpha-IPM synthase/homocitrate synthase family. ... Belongs to the alpha-IPM synthase/homocitrate synthase family. LeuA type 2 subfamily. ... SPalmE:2. Dowal L et al. 2011. Homo sapiens. Platelet. Total membrane. ABE. x List: 214 hits ... LeuA type 2 subfamily.. Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2- ...
3-isopropylmalate dehydratase large subunit. 1327. leuD. 1567. chromosome. 1484226 ← 1483618. 3-isopropylmalate/(R)-2- ... R)-citramalate synthase. 1324. leuA2. 1573. chromosome. 1490824 ← 1489778. 2-isopropylmalate synthase ...
... ethylmalate synthase activity. IEP. Neighborhood. MF. GO:0016705. oxidoreductase activity, acting on paired donors, with ... 2-isopropylmalate synthase activity. IEP. Neighborhood. MF. GO:0004400. histidinol-phosphate transaminase activity. IEP. ... oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one ...
3-isopropylmalate dehydratase small subunit [Ensembl]..... 0.08. OrthoFinder. AAL19074. STM0110, leuD. 3-isopropylmalate ... tryptophan synthase activity. IEP. Enrichment. BP. GO:0006082. organic acid metabolic process. IEP. Enrichment. ... isopropylmalate isomerase small subunit [Ensembl]..... 0.03. OrthoFinder. AKI49985. leuD, L2625_02138. 3-isopropylmalate ... putative 3-isopropylmalate isomerase (dehydratase),.... 0.04. OrthoFinder. AGT25964. N559_4354. isopropylmalate isomerase small ...
homocitrate synthase (EC 2.3.3.14) (characterized). 45%. 95%. 420.6. 2-isopropylmalate synthase (EC 2.3.3.13). 54%. 536.2. ... Putative (R)-citramalate synthase CimA; EC 2.3.3.21 (uncharacterized). 42%. 98%. 361.7. 2-isopropylmalate synthase (EC 2.3.3.13 ... 2-isopropylmalate synthase (EC 2.3.3.13) (characterized). 54%. 100%. 536.2. L-leucine biosynthesis. leuA. hi. leuA: 2- ... isopropylmalate synthase (EC 2.3.3.13) (TIGR00973). 100%. 692.9. L-lysine biosynthesis. hcs. med. ...
2. Properties of the hax1 locus and its encoded regulatory factor. a Locus targeted by amdS integration in QM9414_Dhax1 strains ... ORCID: orcid.org/0000-0002-7575-23171,2 Show authors. Biotechnology for Biofuels volume 11, Article number: 78 (2018) Cite this ... Additional file 2.. Codon usage of the predicted hax1 gene. For each of the 64 codons potentially making up a protein the ... 2a indicates only slight sequence similarities between T. reesei to a noncoding region on the Trichoderma virens genome and no ...
Metabolite accoa_c in iAF1260. Acetyl-CoA.
","tRNA pseudouridylate synthase B, C-terminal; Pseudouridine synthase II, N-terminal; Dyskerin-like; PUA domain [Interproscan ... ","Pseudouridine synthase I, TruA, alpha/beta domain [Interproscan].","protein_coding" "PTI_15G02310.1","No alias"," ... ","ATP synthase subunit delta mitochondrial-like","protein_coding" "lcl,LHPG02000002.1_cds_PRW60642.1_4599","PRW60642"," ... ","ATP synthase beta mitochondrial precursor","protein_coding" "lcl,LHPG02000004.1_cds_PRW59255.1_7347","PRW59255","Chlorella ...
Hydroxymethylglutaryl-CoA Synthase. *Malate Synthase. *Phosphatidylcholine-Sterol O-Acyltransferase. *Retinol O-Fatty- ...
Hydroxymethylglutaryl-CoA Synthase. *Malate Synthase. *Phosphatidylcholine-Sterol O-Acyltransferase. *Retinol O-Fatty- ...
3-Oxoacyl-(Acyl-Carrier-Protein) Synthase [D08.811.913.050.622] * Phosphatidylcholine-Sterol O-Acyltransferase [D08.811.913.050 ...
2-ME use Mercaptoethanol 2-N-Butyl-3-((2-(1H-tetrazol-5-yl)biphenyl-4-yl)methyl)-1,3-diazaspiro(4,4)non-1-en-4-one use ... 1H-2-Benzopyran-1-ones use Isocoumarins 1H-3-Benzazepine-7,8-diol, 2,3,4,5-tetrahydro-1-phenyl- use 2,3,4,5-Tetrahydro-7,8- ... 2-(1-Piperazinyl)quinoline use Quipazine 2-(1,3-Dihydro-3-oxo-5-sulpho-2H-indol-2-ylidene)-3- oxoindoline-5-sulphonic acid use ... 2-Butenoic Acids use Crotonates 2-Butyl-4-chloro-1-((2-(1H-etrazol-5-yl) (1,1-biphenyl)-4-yl)methyl)-1H-imidazole-5-methanol ...
3 hydroxy 3 methylglutaryl coenzyme A synthase use Hydroxymethylglutaryl-CoA Synthase 3 Hydroxy 3 methylpentanedioic Acid use ... 3 Deoxy 7 Phosphoheptulonate Synthase use 3-Deoxy-7-Phosphoheptulonate Synthase 3 Deoxy Arabino Heptulosonate 7 Phosphate ... Synthase use 3-Deoxy-7-Phosphoheptulonate Synthase 3 Deoxy D Arabino Heptulosonate 7 Phosphate Synthase use 3-Deoxy-7- ... 3 Enolpyruvylshikimate 5 Phosphate Synthase use 3-Phosphoshikimate 1-Carboxyvinyltransferase 3 HAA Oxygenase use 3- ...
A variable number of tandem repeats result in polymorphic alpha-isopropylmalate synthase in Mycobacterium tuberculosis. ... encodes the production of active alpha-isopropylmalate synthase. Within the sequence lies the locus of VNTR 4155, and this may ... Table 2. Patient factors associated with rifampin- and isoniazid-resistant isolatesa * Table 3. Proportion of Beijing family in ... 2). Fifty-five viable cultures were available for RFLP typing, targeting the IS6110 by using the internationally standardized ...
Although the structure of an HCS has not been solved, the structure of isopropylmalate synthase (IPMS), a homologue, has been ... Evidence for a catalytic dyad in the active site of homocitrate synthase from saccaromyces cerevisiae. ... Homocitrate synthase (acetyl-coenzyme A: 2-ketoglutarate C-transferase; E.C. 2.3.3.14) (HCS) catalyzes the condensation of ... β-secretase 1 and 2 (BACE1 and BACE2), in complex with a small-molecule inhibitor. Simulations revealed that, upon binding, the ...
3-Deoxyarabinoheptulosonate-7-Phosphate Synthetase use 3-Deoxy-7-Phosphoheptulonate Synthase 3 End Processing, RNA use RNA 3 ... 3-Isopropylmalate Dehydrogenase 3-Keto-5-alpha-Steroid delta-4-Dehydrogenase use Testosterone 5-alpha-Reductase ... 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 ...
2.3.3.21 (R)-citramalate synthase EC subclass 2.4", WIDTH, 550, FGCOLOR, "#ffffff", TEXTSIZE, "10px", CAPTIONSIZE, "12px", ... 2 Transferases EC subclass 2.1", WIDTH, 550, FGCOLOR, "#ffffff", TEXTSIZE, "10px", CAPTIONSIZE, "12px", BORDER, 1); onmouseout ... EC class 2", WIDTH, 550, FGCOLOR, "#ffffff", TEXTSIZE, "10px", CAPTIONSIZE, "12px", BORDER, 1); onmouseout="return nd();">. ...
4S)-beta-phellandrene synthase (geranyl-diphosphate-cyclizing). 4.2.3.53. (+)-endo-beta-bergamotene synthase [(2Z,6Z)-farnesyl ... 3-isopropylmalate dehydratase. 4.2.1.34. (S)-2-methylmalate dehydratase. 4.2.1.35. (R)-2-methylmalate dehydratase. ... alpha-santalene synthase [(2Z,6Z)-farnesyl diphosphate cyclizing]. 4.2.3.51. beta-phellandrene synthase (neryl-diphosphate- ... dTDP-4-dehydro-6-deoxy-alpha-D-glucopyranose 2,3-dehydratase. 4.2.1.160. 2,5-diamino-6-(5-phospho-D-ribosylamino)pyrimidin-4(3H ...
Tryptophan synthase - Cystathionine beta synthase - Porphobilinogen synthase - 3-isopropylmalate dehydratase - Urocanate ... in lungs and nephrons of the kidney - low CO2 concentration, in plant cells) Mechanism A zinc prosthetic group in the enzyme is ... doi:10.1016/S0163-7258(96)00198-2. PMID 9336012.. *^ Carbonic acid has a pKa of around 6.36 (the exact value depends on the ... 3] (in tissues - high CO2 concentration) The reaction rate of carbonic anhydrase is one of the fastest of all enzymes, and its ...
... synthase_B3/B4 1 XM0045378042 IPR019548 DOMAIN:CTF/NFI_DNA-bd_N 1 XM0122996241 IPR014041 HOMOLOGOUS_SUPERFAMILY:ESCRT-II_cplx_ ... IsoCit/isopropylmalate_DH_CS 3 XM0045241282;XM0045250282;XM0045256072 IPR024826 FAMILY:DNA_pol_delta/II_ssu 1 XM0045251712 ... synthase 1 XM0045273292 IPR004360 DOMAIN:Glyas_Fos-R_dOase_dom 2 XM0045201972;XM0045221292 IPR014381 FAMILY:DNA_RNA_pol_RPB5_ ... synthase_N_euk 1 XM0123062901 IPR042407 FAMILY:NCBP2-AS2 1 XM0045262692 IPR036424 HOMOLOGOUS_SUPERFAMILY:UPP_synth-like_sf 1 ...
Characterization of bacterial homocitrate synthase involved in lysine biosynthesis. AP Wulandari, J Miyazaki, N Kobashi, M ... Ancestral residues stabilizing 3-isopropylmalate dehydrogenase of an extreme thermophile: experimental evidence supporting the ...
phosphoribosylaminoimidazole-succinocarboxamide synthase 8, 112, 143. MMP0572. slyD. FKBP-type peptidylprolyl isomerase 11, 96 ... multifunctional 3-isopropylmalate dehydrogenase/D-malate dehydrogenase 7, 8. MMP0540. purC. ... POSITION A C G T 1 0.0 1.0 0.0 0.0 2 0.0 1.0 0.0 0.0 3 0.0 1.0 0.0 0.0 4 1.0 0.0 0.0 0.0 5 1.0 0.0 0.0 0.0 6 0.0 0.0 1.0 0.0 7 ... POSITION A C G T 1 0.4 0.6 0.0 0.0 2 0.0 0.0 0.2 0.8 3 0.0 1.0 0.0 0.0 4 0.6 0.0 0.4 0.0 5 0.0 1.0 0.0 0.0 6 0.0 1.0 0.0 0.0 ...
Influence of mutation in the regulatory domain of α-isopropylmalate synthase from Saccharomyces cerevisiae on its activity and ... in the l-leucine biosynthetic pathway in yeast and controlled by the negative feedback regulation of α-isopropylmalate synthase ... Case 2 was a 75-year-old female who died several hours after surgery for proximal femur fracture. DIAGNOSES: At autopsy, slight ... Echocardiography revealed 2 aneurysms in the mitral valve with mitral regurgitation and aortic regurgitation,in a 42-years-old ...
... disaccharide synthase JOURNAL J. Bacteriol. 169, 5727-5734 (1987) REFERENCE 82 AUTHORS Tabor,C.W. and Tabor,H. TITLE The ... DNA and amino-acid sequences of 3-isopropylmalate dehydrogenase of Bacillus coagulans. Comparison with the enzymes of ... 2, 2006.0007 (2006) REMARK Publication Status: Online-Only REFERENCE 3 AUTHORS Riley,M., Abe,T., Arnaud,M.B., Berlyn,M.K., ... 3, 363-377 (1996) REFERENCE 7 AUTHORS Arn,E.A. and Abelson,J.N. TITLE The 2'-5' RNA ligase of Escherichia coli. ...
A Putative Polyketide Synthase/Peptide Synthetase from Magnaporthe grisea Signals Pathogen Attack to Resistant Rice[J]. The ... Isopropylmalate isomerase MoLeu1 orchestrates leucine biosynjournal, fungal development, and pathogenicity in Magnaporthe ... 2]. 梁华兵, 王晓婉, 胡晓岚, 等. 水稻稻瘟病抗病基因Pi63顺式作用元件的载体构建[J]. 中国农学通报, 2015,31(30):220-224. ... 2]. 王盛昊, 于
  • In enzymology, a 2-isopropylmalate synthase (EC 2.3.3.13) is an enzyme that catalyzes the chemical reaction acetyl-CoA + 3-methyl-2-oxobutanoate + H2O ⇌ {\displaystyle \rightleftharpoons } (2S)-2-isopropylmalate + CoA The three substrates of this enzyme are acetyl-CoA, 3-methyl-2-oxobutanoate, and H2O, and its products are (2S)-2-isopropylmalate and CoA. (wikipedia.org)
  • Other names in common use include 3-carboxy-3-hydroxy-4-methylpentanoate 3-methyl-2-oxobutanoate-lyase, (CoA-acetylating), alpha-isopropylmalate synthetase, alpha-isopropylmalate synthase, alpha-isopropylmalic synthetase, isopropylmalate synthase, and isopropylmalate synthetase. (wikipedia.org)
  • Alpha-isopropylmalate synthase (LeuA), a key enzyme in leucine biosynthesis, catalyzes the first committed step in the pathway, converting acetyl-CoA and alpha-ketoisovalerate to alpha-isopropyl malate and CoA. (nih.gov)
  • For the typical bacterium that can make all 20 amino acids, there are 1-2 gaps in amino acid biosynthesis pathways. (lbl.gov)
  • The proteins are IspG and IspH, involved in reductive dehydroxylations in isoprenoid biosynthesis;quinolinate synthase (NadA), involved in NAD biosynthesis;and dihydroxyacid dehydratase (DHAD) and isopropylmalate isomerase (LeuCD), involved in amino-acid biosynthesis. (grantome.com)
  • 3-isopropylmalate dehydratase small subunit 1 [Ensembl]. (ntu.edu.sg)
  • Belongs to the alpha-IPM synthase/homocitrate synthase family. (swisspalm.org)
  • The systematic name of this enzyme class is acetyl-CoA:3-methyl-2-oxobutanoate C-acetyltransferase (thioester-hydrolysing, carboxymethyl-forming). (wikipedia.org)
  • Aim 2 involves investigation of NadA, an enzyme whose apo-structure resembles that of IspH but whose structure with its 4Fe-4S cluster is unknown. (grantome.com)
  • In plants, carbonic anhydrase helps raise the concentration of CO 2 within the chloroplast in order to increase the carboxylation rate of the enzyme Rubisco . (bionity.com)
  • This family includes alpha-isopropylmalate synthases I (LEU4) and II (LEU9) from Saccharomyces cerevisiae. (nih.gov)
  • 3-isopropylmalate isomerase (dehydratase), subunit with. (ntu.edu.sg)
  • isopropylmalate isomerase small subunit [Ensembl]. (ntu.edu.sg)
  • The alpha-isopropylmalate synthetase of Neurospora. (wikipedia.org)
  • L-leucine from 3-methyl-2-oxobutanoate: step 1/4. (swisspalm.org)
  • These proteins are 2-3x larger than most bacterial IspHs and contain an IspH-RPS1 (ribosomal binding protein S1) fusion and might act as iron or oxygen sensors. (grantome.com)
  • This is the reaction that integrates CO 2 into organic carbon sugars during photosynthesis , and can use only the CO 2 form of carbon, not carbonic acid or bicarbonate. (bionity.com)
  • Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate). (swisspalm.org)
  • Acetyl-CoA + 3-methyl-2-oxobutanoate + H(2)O = (2S)-2-isopropylmalate + CoA. (swisspalm.org)
  • Mycobacterium tuberculosis α-isopropylmalate synthase requires a divalent metal ion, of which Mg2+ and Mn2+ give highest activity, and a monovalent cation, with K+ as the best activator. (wikipedia.org)
  • A locus of variable number of the tandem repeat, VNTR4155, resides in the putative leuA gene, encoding for alpha -isopropylmalate synthase (alpha -IPMS) of Mycobacterium tuberculosis, a repeat that is unique to the bacterium. (nih.gov)
  • Characterization of alpha-isopropylmalate synthases containing different copy numbers of tandem repeats in Mycobacterium tuberculosis. (nih.gov)
  • Initially, the L-leucine synthesis pathway was enhanced by overexpressing feedback-resistant 2-isopropylmalate synthase and acetohydroxy acid synthase both derived from Corynebacterium glutamicum, along with two other native enzymes. (bvsalud.org)
  • Next, the pyruvate and acetyl-CoA pools were enriched by deleting competitive pathways, employing the nonoxidative glycolysis pathway, and dynamically modulating the citrate synthase activity, which significantly promoted the L-leucine production and yield to 40.69 g/L and 0.30 g/g glucose, respectively. (bvsalud.org)
  • Glyphosate and MON 52276 treatment resulted in ceca accumulation of shikimic acid and 3-dehydroshikimic acid, suggesting inhibition of 5-enolpyruvylshikimate-3-phosphate synthase of the shikimate pathway in the gut microbiome. (nih.gov)
  • This is the reaction that integrates CO 2 into organic carbon sugars during photosynthesis , and can use only the CO 2 form of carbon, not carbonic acid or bicarbonate. (bionity.com)
  • 2002 . Cystathionine γ-synthase and threonine synthase operate in concert to regulate carbon flow towards methionine in plants. (annualreviews.org)
  • In plants, carbonic anhydrase helps raise the concentration of CO 2 within the chloroplast in order to increase the carboxylation rate of the enzyme Rubisco . (bionity.com)