Schultz et al. (1998) Proc. Natl. Acad. Sci. USA 95, 5857-5864
Letunic et al. (2008) Nucleic Acids Res , doi:10.1093/nar/gkn808

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ELFV_dehydrog Glutamate/Leucine/Phenylalanine/Valine dehydrogenase

There are 1076 ELFV_dehydrog domains in 1076 proteins in SMART's nrdb database.

Click on the following links for more information.

• Evolution (species in which this domain is found)

• Click on to expand nodes. To display all proteins with a ELFV_dehydrog domain in a specific node, click on it.

  This tree shows only several representative species. The complete taxonomic breakdown of all proteins with ELFV_dehydrog domain is also avaliable.

  Useful shortcuts: Expand all nodes or Collapse tree
  Go to specific node: Anopheles gambiae, Arabidopsis thaliana, Caenorhabditis elegans, Drosophila melanogaster, Homo sapiens, Mus musculus, Rattus norvegicus, Saccharomyces cerevisiae, Takifugu rubripes

• Cellular role (predicted cellular role)

• Cellular role: metabolism
  

• Literature (relevant references for this domain)

• Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.

  • Baker PJ, Turnbull AP, Sedelnikova SE, Stillman TJ, Rice DW
  • A role for quaternary structure in the substrate specificity of leucinedehydrogenase.
  • Structure. 1995; 3: 693-705
  • Display abstract

  • BACKGROUND: Glutamate, phenylalanine and leucine dehydrogenases catalyzethe NAD(P)(+)-linked oxidative deamination of L-amino acids to thecorresponding 2-oxoacids, and sequence homology between these enzymesclearly indicates the existence of an enzyme superfamily related bydivergent evolution. We have undertaken structural studies on a number ofmembers of this family in order to investigate the molecular basis oftheir differential amino acid specificity. RESULTS: We have solved theX-ray structure of the leucine dehydrogenase from Bacillus sphaericus to aresolution of 2.2 A. Each subunit of this octameric enzyme contains 364amino acids and folds into two domains, separated by a deep cleft. Thenicotinamide ring of the NAD+ cofactor binds deep in this cleft, which isthought to close during the hydride transfer step of the catalytic cycle.CONCLUSIONS: Comparison of the structure of leucine dehydrogenase with ahexameric glutamate dehydrogenase has shown that these two enzymes share arelated fold and possess a similar catalytic chemistry. A mechanism forthe basis of the differential amino acid specificity between these enzymesinvolves point mutations in the amino acid side-chain specificity pocketand subtle changes in the shape of this pocket caused by the differencesin quaternary structure.

• Metabolism (metabolic pathways involving proteins which contain this domain)

• Click the image to view the interactive version of the map in iPath

  % proteins involved KEGG pathway ID Description 31.27 map00251 Glutamate metabolism 31.27 map00910 Nitrogen metabolism 11.52 map00471 D-Glutamine and D-glutamate metabolism 11.52 map00330 Arginine and proline metabolism 6.84 map00280 Valine, leucine and isoleucine degradation 6.84 map00290 Valine, leucine and isoleucine biosynthesis 0.37 map00272 Cysteine metabolism 0.19 map00400 Phenylalanine, tyrosine and tryptophan biosynthesis 0.19 map00360 Phenylalanine metabolism This information is based on mapping of SMART genomic protein database to KEGG orthologous groups. Percentage points are related to the number of proteins with ELFV_dehydrog domain which could be assigned to a KEGG orthologous group, and not all proteins containing ELFV_dehydrog domain. Please note that proteins can be included in multiple pathways, ie. the numbers above will not always add up to 100%.

• Structure (3D structures containing this domain)

• 3D Structures of ELFV_dehydrog domains in PDB

  PDB code	Main view	Title
  1aup		Glutamate dehydrogenase
  1b26		Glutamate dehydrogenase
  1b3b		Thermotoga maritima glutamate dehydrogenase mutant n97d, g376k
  1bgv		Glutamate dehydrogenase
  1bvu		Glutamate dehydrogenase from thermococcus litoralis
  1bw9		Phenylalanine dehydrogenase structure in ternary complex with nad+ and phenylpyruvate
  1bxg		Phenylalanine dehydrogenase structure in ternary complex with nad+ and beta-phenylpropionate
  1c1d		L-phenylalanine dehydrogenase structure in ternary complex with nadh and l-phenylalanine
  1c1x		L-phenylalanine dehydrogenase structure in ternary complex with nad+ and l-3-phenyllactate
  1euz		Glutamate dehydrogenase from thermococcus profundus in the unligated state
  1gtm		Structure of glutamate dehydrogenase
  1hrd		Glutamate dehydrogenase
  1hwx		Crystal structure of bovine liver glutamate dehydrogenase complexed with gtp, nadh, and l-glutamic acid
  1hwy		Bovine glutamate dehydrogenase complexed with nad and 2- oxoglutarate
  1hwz		Bovine glutamate dehydrogenase complexed with nadph, glutamate, and gtp
  1k89		K89l mutant of glutamate dehydrogenase
  1l1f		Structure of human glutamate dehydrogenase-apo form
  1leh		Leucine dehydrogenase from bacillus sphaericus
  1nqt		Crystal structure of bovine glutamate dehydrogenase-adp complex
  1nr1		Crystal structure of the r463a mutant of human glutamate dehydrogenase
  1nr7		Crystal structure of apo bovine glutamate dehydrogenase
  1v9l		L-glutamate dehydrogenase from pyrobaculum islandicum complexed with nad
  2bma		The crystal structure of plasmodium falciparum glutamate dehydrogenase, a putative target for novel antimalarial drugs
  2tmg		Thermotoga maritima glutamate dehydrogenase mutant s128r, t158e, n117r, s160e
  3etd
  3ete
  3etg

• Links (links to other resources describing this domain)

• PFAM	ELFV_dehydrog