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Protein

Leucine dehydrogenase

Gene

ldh

Organism
Thermoactinomyces intermedius
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the reversible deamination of L-leucine to 4-methyl-2-oxopentanoate. Exhibits the highest activity with L-leucine as substrate, but can also use other L-amino acids such as L-isoleucine, L-valine and L-2-aminovaleric acid. All of the oxo analogs of the amino acid substrates serve as good substrates for the reverse reaction.1 Publication

Catalytic activityi

L-leucine + H2O + NAD+ = 4-methyl-2-oxopentanoate + NH3 + NADH.1 Publication

Enzyme regulationi

Inhibited by pyridoxal phosphate.1 Publication

Kineticsi

  1. KM=2.0 mM for L-leucine1 Publication
  2. KM=0.4 mM for L-isoleucine1 Publication
  3. KM=2.4 mM for L-valine1 Publication
  4. KM=0.36 mM for NAD+1 Publication
  5. KM=0.63 mM for 4-methyl-2-oxopentanoate1 Publication
  6. KM=4.4 mM for 2-oxoisovalerate1 Publication
  7. KM=2.2 mM for 2-oxo-3-methylvaleate1 Publication
  8. KM=0.042 mM for NADH1 Publication
  9. KM=118 mM for NH31 Publication

    pH dependencei

    Optimum pH is 10.0-10.5 for the oxidative deamination of L-leucine, L-isoleucine and L-valine.1 Publication

    Temperature dependencei

    Thermostable. Retains full activity on incubation for 10 min at 65 degrees Celsius, but loses about 75% of the activity at 75 degrees Celsius.1 Publication

    Pathwayi: L-leucine degradation

    This protein is involved in step 1 of the subpathway that synthesizes 4-methyl-2-oxopentanoate from L-leucine (dehydrogenase route).1 Publication
    Proteins known to be involved in this subpathway in this organism are:
    1. Leucine dehydrogenase (ldh)
    This subpathway is part of the pathway L-leucine degradation, which is itself part of Amino-acid degradation.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes 4-methyl-2-oxopentanoate from L-leucine (dehydrogenase route), the pathway L-leucine degradation and in Amino-acid degradation.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Active sitei80PROSITE-ProRule annotation1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi180 – 186NADSequence analysis7

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Branched-chain amino acid catabolism

    Keywords - Ligandi

    NAD

    Enzyme and pathway databases

    UniPathwayiUPA00363; UER00858.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Leucine dehydrogenase (EC:1.4.1.9)
    Short name:
    LeuDH
    Gene namesi
    Name:ldh
    OrganismiThermoactinomyces intermedius
    Taxonomic identifieri2024 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesThermoactinomycetaceaeThermoactinomyces

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00001828051 – 366Leucine dehydrogenaseAdd BLAST366

    Interactioni

    Subunit structurei

    Homooctamer.1 Publication

    Structurei

    3D structure databases

    ProteinModelPortaliQ60030.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    InterProiIPR006095. Glu/Leu/Phe/Val_DH.
    IPR033524. Glu/Leu/Phe/Val_DH_AS.
    IPR006096. Glu/Leu/Phe/Val_DH_C.
    IPR006097. Glu/Leu/Phe/Val_DH_dimer_dom.
    IPR016211. Glu/Phe/Leu/Val_DH_bac/arc.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PANTHERiPTHR11606:SF3. PTHR11606:SF3. 1 hit.
    PfamiPF00208. ELFV_dehydrog. 2 hits.
    PF02812. ELFV_dehydrog_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000188. Phe_leu_dh. 1 hit.
    PRINTSiPR00082. GLFDHDRGNASE.
    SMARTiSM00839. ELFV_dehydrog. 1 hit.
    [Graphical view]
    SUPFAMiSSF51735. SSF51735. 1 hit.
    PROSITEiPS00074. GLFV_DEHYDROGENASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q60030-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MKIFDYMEKY DYEQLVMCQD KESGLKAIIC IHVTTLGPAL GGMRMWTYAS
    60 70 80 90 100
    EEEAIEDALR LGRGMTYKNA AAGLNLGGGK TVIIGDPRKD KNEAMFRALG
    110 120 130 140 150
    RFIQGLNGRY ITAEDVGTTV EDMDIIHEET RYVTGVSPAF GSSGNPSPVT
    160 170 180 190 200
    AYGVYRGMKA AAKEAFGDDS LEGKVVAVQG VGHVAYELCK HLHNEGAKLI
    210 220 230 240 250
    VTDINKENAD RAVQEFGAEF VHPDKIYDVE CDIFAPCALG AIINDETIER
    260 270 280 290 300
    LKCKVVAGSA NNQLKEERHG KMLEEKGIVY APDYVINAGG VINVADELLG
    310 320 330 340 350
    YNRERAMKKV EGIYDKILKV FEIAKRDGIP SYLAADRMAE ERIEMMRKTR
    360
    STFLQDQRNL INFNNK
    Length:366
    Mass (Da):40,586
    Last modified:November 1, 1996 - v1
    Checksum:i4830BF118AD656AE
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X79068 Genomic DNA. Translation: CAA55671.1.
    PIRiS45607.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X79068 Genomic DNA. Translation: CAA55671.1.
    PIRiS45607.

    3D structure databases

    ProteinModelPortaliQ60030.
    ModBaseiSearch...
    MobiDBiSearch...

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Enzyme and pathway databases

    UniPathwayiUPA00363; UER00858.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    InterProiIPR006095. Glu/Leu/Phe/Val_DH.
    IPR033524. Glu/Leu/Phe/Val_DH_AS.
    IPR006096. Glu/Leu/Phe/Val_DH_C.
    IPR006097. Glu/Leu/Phe/Val_DH_dimer_dom.
    IPR016211. Glu/Phe/Leu/Val_DH_bac/arc.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PANTHERiPTHR11606:SF3. PTHR11606:SF3. 1 hit.
    PfamiPF00208. ELFV_dehydrog. 2 hits.
    PF02812. ELFV_dehydrog_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000188. Phe_leu_dh. 1 hit.
    PRINTSiPR00082. GLFDHDRGNASE.
    SMARTiSM00839. ELFV_dehydrog. 1 hit.
    [Graphical view]
    SUPFAMiSSF51735. SSF51735. 1 hit.
    PROSITEiPS00074. GLFV_DEHYDROGENASE. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiDHLE_THEIN
    AccessioniPrimary (citable) accession number: Q60030
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: November 1, 1996
    Last modified: October 5, 2016
    This is version 84 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Direct protein sequencing

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.