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
Gene expression levels in SubtiExpress: bcd
Metabolic function and regulation of this protein in SubtiPathways: bcd
MW, pI	39 kDa, 4.942
Gene length, protein length	1092 bp, 364 aa
Immediate neighbours	buk, ptb
Sequences	Protein DNA DNA_with_flanks
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

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

• BsubCyc: BSU24080

• 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

• BsubCyc: BSU24080

• 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: indirect regulation PubMed
  • BkdR: transcription activation PubMed

• Additional information:
  • number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 3408 PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 2690 PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 11556 PubMed

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)