Bcd

• Description: valine dehydrogenase, isoleucine dehydrogenase, L-leucine dehydrogenase
  
  

Gene name	bcd
Synonyms	bkd, yqiT
Essential	no
Product	valine dehydrogenase, isoleucine dehydrogenase, L-leucine dehydrogenase
Function	utilization of branched-chain keto acids
Metabolic function and regulation of this protein in SubtiPathways: Lipid synthesis, Ile, Leu, Val
MW, pI	39 kDa, 4.942
Gene length, protein length	1092 bp, 364 aa
Immediate neighbours	buk, ptb
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList

Categories containing this gene/protein

utilization of amino acids

This gene is a member of the following regulons

BkdR regulon, CodY regulon, SigL regulon

The gene

Basic information

• Locus tag: BSU24080

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: L-leucine + H₂O + NAD⁺ = 4-methyl-2-oxopentanoate + NH₃ + NADH (according to Swiss-Prot)

• Protein family: Glu/Leu/Phe/Val dehydrogenases family (according to Swiss-Prot)

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions:

• Localization:

Database entries

• Structure: 1LEH (from Lysinibacillus sphaericus, 71% identity, 82% similarity) PubMed

• UniProt: P54531

• KEGG entry: [3]

• E.C. number: 1.4.1.9

Expression and regulation

• Operon: ptb-bcd-buk-lpdV-bkdAA-bkdAB-bkdB PubMed

• Expression browser: bcd PubMed

• Sigma factor: SigL PubMed

• Regulation:
  • induced in the presence of isoleucine or valine (BkdR) PubMed

• Regulatory mechanism:
  • CodY: transcription repression PubMed
  • BkdR: transcription activation PubMed

• Additional information:

Biological materials

• Mutant:
  • a bcd mutant and a bcd ybgE ywaA triple mutant are available in Linc Sonenshein's lab

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Reviews

N M Brunhuber, J S Blanchard
The biochemistry and enzymology of amino acid dehydrogenases.
Crit Rev Biochem Mol Biol: 1994, 29(6);415-67
[PubMed:7705101] [WorldCat.org] [DOI] (P p)

Original publications

M Nickel, G Homuth, C Böhnisch, U Mäder, T Schweder
Cold induction of the Bacillus subtilis bkd operon is mediated by increased mRNA stability.
Mol Genet Genomics: 2004, 272(1);98-107
[PubMed:15241682] [WorldCat.org] [DOI] (P p)

Ken-ichi Yoshida, Hirotake Yamaguchi, Masaki Kinehara, Yo-hei Ohki, Yoshiko Nakaura, Yasutaro Fujita
Identification of additional TnrA-regulated genes of Bacillus subtilis associated with a TnrA box.
Mol Microbiol: 2003, 49(1);157-65
[PubMed:12823818] [WorldCat.org] [DOI] (P p)

Tanja Kaan, Georg Homuth, Ulrike Mäder, Julia Bandow, Thomas Schweder
Genome-wide transcriptional profiling of the Bacillus subtilis cold-shock response.
Microbiology (Reading): 2002, 148(Pt 11);3441-3455
[PubMed:12427936] [WorldCat.org] [DOI] (P p)

M Debarbouille, R Gardan, M Arnaud, G Rapoport
Role of bkdR, a transcriptional activator of the sigL-dependent isoleucine and valine degradation pathway in Bacillus subtilis.
J Bacteriol: 1999, 181(7);2059-66
[PubMed:10094682] [WorldCat.org] [DOI] (P p)