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)
Synthetase3
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)
The alpha-isopropylmalate synthetase of Neurospora. (wikipedia.org)
The systematic name of this enzyme class is acetyl-CoA:3-methyl-2-oxobutanoate C-acetyltransferase (thioester-hydrolysing, carboxymethyl-forming). (wikipedia.org)
This enzyme participates in biosynthesis of L-leucine and pyruvate metabolism. (wikipedia.org)
Another feature of the M. tuberculosis homolog is that L-leucine, the feedback inhibitor, inhibits the enzyme in a time-dependent fashion. (wikipedia.org)
Biosynthesis3
This enzyme participates in biosynthesis of L-leucine and pyruvate metabolism. (wikipedia.org)
The 2-keto acid pathway involves five enzymes for IB biosynthesis from the central metabolite pyruvate (Fig. 1 ). (biomedcentral.com)
As an intermediate for valine and leucine biosynthesis, 2-ketoisovalerate is decarboxylated by a heterologously expressed broad-substrate-range α-ketoisovalerate decarboxylase (Kivd) to isobutyaldehyde, and subsequently reduced into IB by an alcohol dehydrogenase (Adh). (biomedcentral.com)
Mycobacterium3
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)
Enzymes1
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)
Pyruvate2
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)
Within the 2-keto acid pathway, the first involved enzyme, acetolactate synthase (AlsS), condenses two pyruvate molecules into a 2-acetolactate molecule. (biomedcentral.com)
Escherichia2
In this study, we rationally developed an efficient L-leucine-producing Escherichia coli strain. (bvsalud.org)
Biological IB production was first demonstrated in Escherichia coli ( E. coli ) by introduction of a synthetic 2-keto acid pathway [ 7 ]. (biomedcentral.com)
Enzyme that catalyzes7
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)
An enzyme that catalyzes the first step in the biosynthetic pathway to LEUCINE , forming isopropyl malate from acetyl-CoA and alpha-ketoisovaleric acid. (bvsalud.org)
9/3/2005) TOTAL DESCRIPTORS = 935 MH - 1-Acylglycerol-3-Phosphate O-Acyltransferase UI - D051103 MN - D8.811.913.50.173 MS - An enzyme that catalyzes the acyl group transfer of ACYL COA to 1-acyl-sn-glycerol 3-phosphate to generate 1,2-diacyl-sn-glycerol 3-phosphate. (nih.gov)
HN - 2006(1981) MH - 2-Aminoadipate Transaminase UI - D051307 MN - D8.811.913.477.700.120 MS - A PYRIDOXAL PHOSPHATE containing enzyme that catalyzes the transfer of amino group of L-2-aminoadipate onto 2-OXOGLUTARATE to generate 2-oxoadipate and L-GLUTAMATE. (nih.gov)
HN - 2006(1983) MH - 2-Oxoisovalerate Dehydrogenase (Acylating) UI - D050645 MN - D8.811.682.657.350.825 MS - An NAD+ dependent enzyme that catalyzes the oxidation 3-methyl-2-oxobutanoate to 2-methylpropanoyl-CoA. (nih.gov)
use AMINO ACIDS, BRANCHED-CHAIN 1979, & KETO ACIDS & VALERATES 1973-1979 MH - 3-Hydroxyanthranilate 3,4-Dioxygenase UI - D050561 MN - D8.811.682.690.416.328 MS - An enzyme that catalyzes the conversion of 3-hydroxyanthranilate to 2-amino-3-carboxymuconate semialdehyde. (nih.gov)
use ANTHRANILIC ACID 1974-1979 MH - 3-Isopropylmalate Dehydrogenase UI - D050539 MN - D8.811.682.47.500 MS - An NAD+ dependent enzyme that catalyzes the oxidation of 3-carboxy-2-hydroxy-4-methylpentanoate to 3-carboxy-4-methyl-2-oxopentanoate. (nih.gov)
Coli1
The strategies presented here will be useful for engineering E. coli strains for producing L-leucine and related products on an industrial scale. (bvsalud.org)
Pathway2
PCC 6803 has been engineered for the isobutanol and 3-methyl-1-butanol production by introducing a synthetic 2-keto acid pathway. (biomedcentral.com)
Novel Synechocystis strain integrated with a native 2-keto acid pathway was generated and showed a production of 98 mg isobutanol L −1 in short-term screening experiments. (biomedcentral.com)
Alpha2
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)
The alpha-isopropylmalate synthetase of Neurospora. (wikipedia.org)
Strain1
Under fed-batch conditions, the final strain LXH-21 produced 63.29 g/L of L-leucine, with a yield and productivity of 0.37 g/g glucose and 2.64 g/(L h), respectively. (bvsalud.org)
Production2
To our knowledge, this study achieved the highest production efficiency of L-leucine to date. (bvsalud.org)
The significantly enhanced isobutanol and 3-methyl-1-butanol production in this study further pave the way for an industrial application of photosynthetic cyanobacteria-based biofuel and chemical synthesis from CO 2 . (biomedcentral.com)