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213  structures 3955  species 2  interactions 6065  sequences 15  architectures

Family: ELFV_dehydrog_N (PF02812)

Summary: Glu/Leu/Phe/Val dehydrogenase, dimerisation domain

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This is the Wikipedia entry entitled "ELFV dehydrogenase". More...

ELFV dehydrogenase Edit Wikipedia article

Glutamate/Leucine/Phenylalanine/Valine dehydrogenase
PDB 1b3b EBI.jpg
thermotoga maritima glutamate dehydrogenase mutant n97d, g376k
Identifiers
Symbol ELFV_dehydrog
Pfam PF00208
Pfam clan CL0063
InterPro IPR006096
PROSITE PDOC00071
SCOP 1leh
SUPERFAMILY 1leh
Glu/Leu/Phe/Val dehydrogenase, dimerisation domain
Identifiers
Symbol ELFV_dehydrog_N
Pfam PF02812
SCOP 1leh
SUPERFAMILY 1leh

In molecular biology, the ELFV dehydrogenase family of enzymes include glutamate, leucine, phenylalanine and valine dehydrogenases. These enzymes are structurally and functionally related. They contain a Gly-rich region containing a conserved Lys residue, which has been implicated in the catalytic activity, in each case a reversible oxidative deamination reaction.

Glutamate dehydrogenases EC 1.4.1.2, EC 1.4.1.3 and EC 1.4.1.4 (GluDH) are enzymes that catalyse the NAD- and/or NADP-dependent reversible deamination of L-glutamate into alpha-ketoglutarate.[1][2] GluDH isozymes are generally involved with either ammonia assimilation or glutamate catabolism. Two separate enzymes are present in yeasts: the NADP-dependent enzyme, which catalyses the amination of alpha-ketoglutarate to L-glutamate; and the NAD-dependent enzyme, which catalyses the reverse reaction [3] - this form links the L-amino acids with the Krebs cycle, which provides a major pathway for metabolic interconversion of alpha-amino acids and alpha-keto acids.[4]

Leucine dehydrogenase EC 1.4.1.9 (LeuDH) is a NAD-dependent enzyme that catalyses the reversible deamination of leucine and several other aliphatic amino acids to their keto analogues.[5] Each subunit of this octameric enzyme from Bacillus sphaericus contains 364 amino acids and folds into two domains, separated by a deep cleft. The nicotinamide ring of the NAD+ cofactor binds deep in this cleft, which is thought to close during the hydride transfer step of the catalytic cycle.

Phenylalanine dehydrogenase EC 1.4.1.20 (PheDH) is an NAD-dependent enzyme that catalyses the reversible deamidation of L-phenylalanine into phenyl-pyruvate.[6]

Valine dehydrogenase EC 1.4.1.8 (ValDH) is an NADP-dependent enzyme that catalyses the reversible deamidation of L-valine into 3-methyl-2-oxobutanoate.[7]

These enzymes contain two domains, an N-terminal dimerisation domain, and a C-terminal domain.[8]

References[edit]

  1. ^ Britton KL, Baker PJ, Rice DW, Stillman TJ (November 1992). "Structural relationship between the hexameric and tetrameric family of glutamate dehydrogenases". Eur. J. Biochem. 209 (3): 851–9. doi:10.1111/j.1432-1033.1992.tb17357.x. PMID 1358610. 
  2. ^ Benachenhou-Lahfa N, Forterre P, Labedan B (April 1993). "Evolution of glutamate dehydrogenase genes: evidence for two paralogous protein families and unusual branching patterns of the archaebacteria in the universal tree of life". J. Mol. Evol. 36 (4): 335–46. PMID 8315654. 
  3. ^ Moye WS, Amuro N, Rao JK, Zalkin H (July 1985). "Nucleotide sequence of yeast GDH1 encoding nicotinamide adenine dinucleotide phosphate-dependent glutamate dehydrogenase". J. Biol. Chem. 260 (14): 8502–8. PMID 2989290. 
  4. ^ Mavrothalassitis G, Tzimagiorgis G, Mitsialis A, Zannis V, Plaitakis A, Papamatheakis J, Moschonas N (May 1988). "Isolation and characterization of cDNA clones encoding human liver glutamate dehydrogenase: evidence for a small gene family". Proc. Natl. Acad. Sci. U.S.A. 85 (10): 3494–8. doi:10.1073/pnas.85.10.3494. PMC 280238. PMID 3368458. 
  5. ^ Nagata S, Tanizawa K, Esaki N, Sakamoto Y, Ohshima T, Tanaka H, Soda K (December 1988). "Gene cloning and sequence determination of leucine dehydrogenase from Bacillus stearothermophilus and structural comparison with other NAD(P)+-dependent dehydrogenases". Biochemistry 27 (25): 9056–62. doi:10.1021/bi00425a026. PMID 3069133. 
  6. ^ Takada H, Yoshimura T, Ohshima T, Esaki N, Soda K (March 1991). "Thermostable phenylalanine dehydrogenase of Thermoactinomyces intermedius: cloning, expression, and sequencing of its gene". J. Biochem. 109 (3): 371–6. PMID 1880121. 
  7. ^ Tang L, Hutchinson CR (July 1993). "Sequence, transcriptional, and functional analyses of the valine (branched-chain amino acid) dehydrogenase gene of Streptomyces coelicolor". J. Bacteriol. 175 (13): 4176–85. PMC 204847. PMID 8320231. 
  8. ^ Baker, P. J.; Turnbull, A. P.; Sedelnikova, S. E.; Stillman, T. J.; Rice, D. W. (1995). "A role for quaternary structure in the substrate specificity of leucine dehydrogenase". Structure (London, England : 1993) 3 (7): 693–705. doi:10.1016/S0969-2126(01)00204-0. PMID 8591046.  edit

This article incorporates text from the public domain Pfam and InterPro IPR006096

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

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Glu/Leu/Phe/Val dehydrogenase, dimerisation domain Provide feedback

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Literature references

  1. Baker PJ, Turnbull AP, Sedelnikova SE, Stillman TJ, Rice DW; , Structure 1995;3:693-705.: A role for quaternary structure in the substrate specificity of leucine dehydrogenase. PUBMED:8591046 EPMC:8591046


External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR006097

Glutamate, leucine, phenylalanine and valine dehydrogenases are structurally and functionally related. They contain a Gly-rich region containing a conserved Lys residue, which has been implicated in the catalytic activity, in each case a reversible oxidative deamination reaction.

Glutamate dehydrogenases (EC, EC, and EC) (GluDH) are enzymes that catalyse the NAD- and/or NADP-dependent reversible deamination of L-glutamate into alpha-ketoglutarate [PUBMED:1358610, PUBMED:8315654]. GluDH isozymes are generally involved with either ammonia assimilation or glutamate catabolism. Two separate enzymes are present in yeasts: the NADP-dependent enzyme, which catalyses the amination of alpha-ketoglutarate to L-glutamate; and the NAD-dependent enzyme, which catalyses the reverse reaction [PUBMED:2989290] - this form links the L-amino acids with the Krebs cycle, which provides a major pathway for metabolic interconversion of alpha-amino acids and alpha- keto acids [PUBMED:3368458].

Leucine dehydrogenase (EC) (LeuDH) is a NAD-dependent enzyme that catalyses the reversible deamination of leucine and several other aliphatic amino acids to their keto analogues [PUBMED:3069133]. Each subunit of this octameric enzyme from Bacillus sphaericus contains 364 amino acids and folds into two domains, separated by a deep cleft. The nicotinamide ring of the NAD+ cofactor binds deep in this cleft, which is thought to close during the hydride transfer step of the catalytic cycle.

Phenylalanine dehydrogenase (EC) (PheDH) is na NAD-dependent enzyme that catalyses the reversible deamidation of L-phenylalanine into phenyl-pyruvate [PUBMED:1880121].

Valine dehydrogenase (EC) (ValDH) is an NADP-dependent enzyme that catalyses the reversible deamidation of L-valine into 3-methyl-2-oxobutanoate [PUBMED:8320231].

This entry represents the dimerisation region of these enzymes.

Gene Ontology

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Domain organisation

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(262)
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(6065)
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(4625)
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(1317)
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(538)
RP35
(1003)
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(1309)
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(1526)
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  Seed
(262)
Full
(6065)
Representative proteomes NCBI
(4625)
Meta
(1317)
RP15
(538)
RP35
(1003)
RP55
(1309)
RP75
(1526)
Alignment:
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  Seed
(262)
Full
(6065)
Representative proteomes NCBI
(4625)
Meta
(1317)
RP15
(538)
RP35
(1003)
RP55
(1309)
RP75
(1526)
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Curation and family details

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Seed source: Prosite
Previous IDs: E_L_F_V_dh; GLFV_dehydrog_N;
Type: Domain
Author: Finn RD, Griffiths-Jones SR
Number in seed: 262
Number in full: 6065
Average length of the domain: 125.30 aa
Average identity of full alignment: 45 %
Average coverage of the sequence by the domain: 30.51 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 25.3 25.3
Trusted cut-off 25.4 25.5
Noise cut-off 25.2 25.0
Model length: 131
Family (HMM) version: 13
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Interactions

There are 2 interactions for this family. More...

ELFV_dehydrog_N ELFV_dehydrog

Structures

For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the ELFV_dehydrog_N domain has been found. There are 213 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.

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