DHLE_THEIN
ID DHLE_THEIN Reviewed; 366 AA.
AC Q60030;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Leucine dehydrogenase;
DE Short=LeuDH;
DE EC=1.4.1.9;
GN Name=ldh;
OS Thermoactinomyces intermedius.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Thermoactinomycetaceae;
OC Thermoactinomyces.
OX NCBI_TaxID=2024;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-42; 69-89; 266-272
RP AND 309-317, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, AND SUBUNIT.
RC STRAIN=ATCC 33205 / DSM 43846 / JCM 3312 / KCTC 9646 / NBRC 14230 / NRRL
RC B-16979 / VKM Ac-1427 / T-323;
RX PubMed=8020469; DOI=10.1111/j.1432-1033.1994.tb18869.x;
RA Ohshima T., Nishida N., Bakthavatsalam S., Kataoka K., Takada H.,
RA Yoshimura T., Esaki N., Soda K.;
RT "The purification, characterization, cloning and sequencing of the gene for
RT a halostable and thermostable leucine dehydrogenase from Thermoactinomyces
RT intermedius.";
RL Eur. J. Biochem. 222:305-312(1994).
CC -!- FUNCTION: Catalyzes the reversible deamination of L-leucine to 4-
CC methyl-2-oxopentanoate. Exhibits the highest activity with L-leucine as
CC substrate, but can also use other L-amino acids such as L-isoleucine,
CC L-valine and L-2-aminovaleric acid. All of the oxo analogs of the amino
CC acid substrates serve as good substrates for the reverse reaction.
CC {ECO:0000269|PubMed:8020469}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-leucine + NAD(+) = 4-methyl-2-oxopentanoate + H(+) +
CC NADH + NH4(+); Xref=Rhea:RHEA:12220, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17865, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:57427, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.4.1.9;
CC Evidence={ECO:0000269|PubMed:8020469};
CC -!- ACTIVITY REGULATION: Inhibited by pyridoxal phosphate.
CC {ECO:0000269|PubMed:8020469}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.0 mM for L-leucine {ECO:0000269|PubMed:8020469};
CC KM=0.4 mM for L-isoleucine {ECO:0000269|PubMed:8020469};
CC KM=2.4 mM for L-valine {ECO:0000269|PubMed:8020469};
CC KM=0.36 mM for NAD(+) {ECO:0000269|PubMed:8020469};
CC KM=0.63 mM for 4-methyl-2-oxopentanoate {ECO:0000269|PubMed:8020469};
CC KM=4.4 mM for 2-oxoisovalerate {ECO:0000269|PubMed:8020469};
CC KM=2.2 mM for 2-oxo-3-methylvaleate {ECO:0000269|PubMed:8020469};
CC KM=0.042 mM for NADH {ECO:0000269|PubMed:8020469};
CC KM=118 mM for NH(3) {ECO:0000269|PubMed:8020469};
CC pH dependence:
CC Optimum pH is 10.0-10.5 for the oxidative deamination of L-leucine,
CC L-isoleucine and L-valine. {ECO:0000269|PubMed:8020469};
CC Temperature dependence:
CC Thermostable. Retains full activity on incubation for 10 min at 65
CC degrees Celsius, but loses about 75% of the activity at 75 degrees
CC Celsius. {ECO:0000269|PubMed:8020469};
CC -!- PATHWAY: Amino-acid degradation; L-leucine degradation; 4-methyl-2-
CC oxopentanoate from L-leucine (dehydrogenase route): step 1/1.
CC {ECO:0000269|PubMed:8020469}.
CC -!- SUBUNIT: Homooctamer. {ECO:0000269|PubMed:8020469}.
CC -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC {ECO:0000305}.
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DR EMBL; X79068; CAA55671.1; -; Genomic_DNA.
DR PIR; S45607; S45607.
DR AlphaFoldDB; Q60030; -.
DR SMR; Q60030; -.
DR UniPathway; UPA00363; UER00858.
DR GO; GO:0050049; F:leucine dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0006552; P:leucine catabolic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR046346; Aminiacid_DH-like_N_sf.
DR InterPro; IPR006095; Glu/Leu/Phe/Val_DH.
DR InterPro; IPR033524; Glu/Leu/Phe/Val_DH_AS.
DR InterPro; IPR006096; Glu/Leu/Phe/Val_DH_C.
DR InterPro; IPR006097; Glu/Leu/Phe/Val_DH_dimer_dom.
DR InterPro; IPR016211; Glu/Phe/Leu/Val_DH_bac/arc.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR42722; PTHR42722; 1.
DR Pfam; PF00208; ELFV_dehydrog; 2.
DR Pfam; PF02812; ELFV_dehydrog_N; 1.
DR PIRSF; PIRSF000188; Phe_leu_dh; 1.
DR PRINTS; PR00082; GLFDHDRGNASE.
DR SMART; SM00839; ELFV_dehydrog; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF53223; SSF53223; 1.
DR PROSITE; PS00074; GLFV_DEHYDROGENASE; 1.
PE 1: Evidence at protein level;
KW Branched-chain amino acid catabolism; Direct protein sequencing; NAD;
KW Oxidoreductase.
FT CHAIN 1..366
FT /note="Leucine dehydrogenase"
FT /id="PRO_0000182805"
FT ACT_SITE 80
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10011"
FT BINDING 180..186
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255"
SQ SEQUENCE 366 AA; 40586 MW; 4830BF118AD656AE CRC64;
MKIFDYMEKY DYEQLVMCQD KESGLKAIIC IHVTTLGPAL GGMRMWTYAS EEEAIEDALR
LGRGMTYKNA AAGLNLGGGK TVIIGDPRKD KNEAMFRALG RFIQGLNGRY ITAEDVGTTV
EDMDIIHEET RYVTGVSPAF GSSGNPSPVT AYGVYRGMKA AAKEAFGDDS LEGKVVAVQG
VGHVAYELCK HLHNEGAKLI VTDINKENAD RAVQEFGAEF VHPDKIYDVE CDIFAPCALG
AIINDETIER LKCKVVAGSA NNQLKEERHG KMLEEKGIVY APDYVINAGG VINVADELLG
YNRERAMKKV EGIYDKILKV FEIAKRDGIP SYLAADRMAE ERIEMMRKTR STFLQDQRNL
INFNNK
