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leuA 2-isopropylmalate synthase [ Mycobacterium tuberculosis H37Rv ]

Gene ID: 885092, updated on 6-Oct-2023
Gene symbol
leuA
Gene description
2-isopropylmalate synthase
Locus tag
Rv3710
Gene type
protein coding
RefSeq status
PROVISIONAL
Organism
Mycobacterium tuberculosis H37Rv (strain: H37Rv, type-material: type strain of Mycobacterium tuberculosis)
Lineage
Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium tuberculosis complex
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Sequence:
NC_000962.3 (4153740..4155674)

NC_000962.3Genomic Context describing neighboring genes Neighboring gene aspartate-semialdehyde dehydrogenase Neighboring gene aspartokinase Neighboring gene DNA polymerase III subunit epsilon Neighboring gene ligase

Genomic Sequence:
NC_000962.3

Go to nucleotide: Graphics FASTA GenBank

Related articles in PubMed

  1. Mechanistic and bioinformatic investigation of a conserved active site helix in α-isopropylmalate synthase from Mycobacterium tuberculosis, a member of the DRE-TIM metallolyase superfamily. Casey AK, et al. Biochemistry, 2014 May 13. PMID 24720347, Free PMC Article
  2. Kinetic evidence for interdomain communication in the allosteric regulation of alpha-isopropylmalate synthase from Mycobacterium tuberculosis. de Carvalho LP, et al. Biochemistry, 2009 Mar 10. PMID 19166329, Free PMC Article
  3. Kinetic and chemical mechanism of alpha-isopropylmalate synthase from Mycobacterium tuberculosis. de Carvalho LP, et al. Biochemistry, 2006 Jul 25. PMID 16846242, Free PMC Article
  4. TubercuList--10 years after. Lew JM, et al. Tuberculosis (Edinb), 2011 Jan. PMID 20980199
  5. Re-annotation of the genome sequence of Mycobacterium tuberculosis H37Rv. Camus JC, et al. Microbiology (Reading), 2002 Oct. PMID 12368430

See all (6) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. comparison of results with previous biochemical data indicates an active site arginine residue (R80 in IPMS) is required for activity across the superfamily, suggesting that it plays a key role in catalysis, most likely through enolate stabilization
    Title: Mechanistic and bioinformatic investigation of a conserved active site helix in α-isopropylmalate synthase from Mycobacterium tuberculosis, a member of the DRE-TIM metallolyase superfamily.
  2. Data show that the Y410F mutant form of MtIPMS is insensitive to l-leucine inhibition, suggesting that this residue has completely uncoupled the inhibitory signal to the active site.
    Title: Kinetic evidence for interdomain communication in the allosteric regulation of alpha-isopropylmalate synthase from Mycobacterium tuberculosis.
  3. The alpha-keto acid specificity of the enzyme is narrow, and the acyl-CoA specificity is absolute for AcCoA. In the absence of alpha-KIV, MtIPMS does not enolize the alpha protons of AcCoA but slowly hydrolyzes acyl-CoA analogues.
    Title: Kinetic and chemical mechanism of alpha-isopropylmalate synthase from Mycobacterium tuberculosis.
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Homology

Preferred Names
2-isopropylmalate synthase
NP_218227.3
  • alpha-isopropylmalate synthase) (alpha-IPM synthetase) (IPMS)

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

  1. NC_000962.3 Reference assembly

    Range
    4153740..4155674
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NP_218227.3 2-isopropylmalate synthase [Mycobacterium tuberculosis H37Rv]

    See identical proteins and their annotated locations for NP_218227.3

    Status: PROVISIONAL

    UniProtKB/TrEMBL
    A0A9P2H494
    Conserved Domains (1) summary
    PRK03739
    Location:39 → 644
    PRK03739; 2-isopropylmalate synthase; Validated
Nucleotide Protein
Heading Accession and Version
Protein Accession Links
GenPept Link UniProtKB Link
3HPS_A.1
3HPS_B.1
3HPZ_A.1
3HPZ_B.1
3HQ1_A.1
3HQ1_B.1
P9WQB3.1

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