The amino acid sequence of glutamate dehydrogenase fromPyrococcus furiosus, a hyperthermophilic archaebacterium

1994 ◽  
Vol 13 (2) ◽  
pp. 253-259 ◽  
Author(s):  
Bruno Maras ◽  
Sofia Valiante ◽  
Roberta Chiaraluce ◽  
Valerio Consalvi ◽  
Laura Politi ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Glutamate Dehydrogenase

scholarly journals The gdhB Gene of Pseudomonas aeruginosaEncodes an Arginine-Inducible NAD+-Dependent Glutamate Dehydrogenase Which Is Subject to Allosteric Regulation

2001 ◽  
Vol 183 (2) ◽  
pp. 490-499 ◽  
Author(s):  
Chung-Dar Lu ◽  
Ahmed T. Abdelal
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Glutamate Dehydrogenase ◽  
Legionella Pneumophila ◽  
Caulobacter Crescentus ◽  
Sodium Dodecyl ◽  
Sequence Information ◽  
Saturation Curve ◽  
Moderate Degree ◽  
Amino Terminal

ABSTRACT The NAD+-dependent glutamate dehydrogenase (NAD-GDH) from Pseudomonas aeruginosa PAO1 was purified, and its amino-terminal amino acid sequence was determined. This sequence information was used in identifying and cloning the encodinggdhB gene and its flanking regions. The molecular mass predicted from the derived sequence for the encoded NAD-GDH was 182.6 kDa, in close agreement with that determined from sodium dodecyl sulfate-polyacrylamide gel electrophoresis of the purified enzyme (180 kDa). Cross-linking studies established that the native NAD-GDH is a tetramer of equal subunits. Comparison of the derived amino acid sequence of NAD-GDH from P. aeruginosa with the GenBank database showed the highest homology with hypothetical polypeptides from Pseudomonas putida, Mycobacterium tuberculosis, Rickettsia prowazakii, Legionella pneumophila, Vibrio cholerae, Shewanella putrefaciens, Sinorhizobium meliloti, andCaulobacter crescentus. A moderate degree of homology, primarily in the central domain, was observed with the smaller tetrameric NAD-GDH (protomeric mass of 110 kDa) fromSaccharomyces cerevisiae or Neurospora crassa. Comparison with the yet smaller hexameric GDH (protomeric mass of 48 to 55 kDa) of other prokaryotes yielded a low degree of homology that was limited to residues important for binding of substrates and for catalytic function. NAD-GDH was induced 27-fold by exogenous arginine and only 3-fold by exogenous glutamate. Primer extension experiments established that transcription of gdhB is initiated from an arginine-inducible promoter and that this induction is dependent on the arginine regulatory protein, ArgR, a member of the AraC/XyIS family of regulatory proteins. NAD-GDH was purified to homogeneity from a recombinant strain of P. aeruginosa and characterized. The glutamate saturation curve was sigmoid, indicating positive cooperativity in the binding of glutamate. NAD-GDH activity was subject to allosteric control by arginine and citrate, which function as positive and negative effectors, respectively. Both effectors act by influencing the affinity of the enzyme for glutamate. NAD-GDH from this organism differs from previously characterized enzymes with respect to structure, protomer mass, and allosteric properties indicate that this enzyme represents a novel class of microbial glutamate dehydrogenases.

scholarly journals Amino-Acid Sequence of NADP-Specific Glutamate Dehydrogenase of Neurospora crassa

1974 ◽  
Vol 71 (11) ◽  
pp. 4361-4365 ◽  
Author(s):  
J. C. Wootton ◽  
G. K. Chambers ◽  
A. A. Holder ◽  
A. J. Baron ◽  
J. G. Taylor ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Neurospora Crassa ◽  
Glutamate Dehydrogenase

scholarly journals The amino acid sequence of Neurospora NADP-specific glutamate dehydrogenase. The tryptic peptides

1975 ◽  
Vol 149 (3) ◽  
pp. 739-748 ◽  
Author(s):  
J C Wootton ◽  
J G Taylor ◽  
A A Jackson ◽  
G K Chambers ◽  
J R S. Fincham
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Neurospora Crassa ◽  
Glutamate Dehydrogenase ◽  
Polypeptide Chain ◽  
British Library ◽  
Tryptic Peptides

The NADP-specific glutamate dehydrogenase of Neurospora crassa was digested with trypsin, and peptides accounting for 441 out of the 452 residues of the polypeptide chain were isolated and substantially sequenced. Additional experimental detail has been deposited as Supplementary Publication SUP 50052 (11 pages) with the British Library (Lending Division), Boston Spa, Wetherby, W. Yorkshire LS23 7BQ, U.K., from whom copies may be obtained under the terms given in Biochem J. (1975) 145, 5.

scholarly journals Amino Acid Sequence of Chicken Liver Glutamate Dehydrogenase

1973 ◽  
Vol 248 (9) ◽  
pp. 3093-3107 ◽  
Author(s):  
Kenneth Moon ◽  
Dennis Piszkiewicz ◽  
Emil L. Smith
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Glutamate Dehydrogenase ◽  
Chicken Liver

scholarly journals The amino acid sequence of Neurospora NADP-specific glutamate dehydrogenase. Peptic and chymotryptic peptides and the complete sequence

1975 ◽  
Vol 149 (3) ◽  
pp. 757-773 ◽  
Author(s):  
A A Holder ◽  
J C Wootton ◽  
A J Baron ◽  
G K Chambers ◽  
J R S. Fincham
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Neurospora Crassa ◽  
Glutamate Dehydrogenase ◽  
Polypeptide Chain ◽  
Complete Sequence ◽  
British Library ◽  
Tryptic Peptides

Peptic and chymotryptic peptides were isolated form the NADP-specific glutamate dehydrogenase of Neurospora crassa and substantially sequenced. Out of 452 residues in the polypeptide chain, 265 were recovered in the peptic and 427 in the chymotryptic peptides. Together with the tryptic peptides [Wootton, J. C., Taylor, J. G., Jackson, A. A., Chambers, G. K. & Fincham, J. R. S. (1975) Biochem. J.149, 749-755], these establish the complete sequence of the chain, including the acid and amide assignments, except for seven places where overlaps are inadequate. These remaining alignments are deduced from information on the CNBr fragments obtained in another laboratory [Blumenthal, K. M., Moon, K. & Smith, E. L. (1975), J. Biol. Chem.250, 3644-3654]. Further information has been deposited as Supplementary Publication SUP 50054 (17 pages) with the British Library (Lending Division), Boston Spa, Wetherby, W. Yorkshire LS23 7BQ, U.K., from whom copies may be obtained under the terms given in Biochem. J. (1975) 145, 5.

Sign in / Sign up

Export Citation Format

Share Document