On the Evidence for Partial Gene Duplication from Amino Acid Sequence of Bovine Glutamate Dehydrogenase

Nature ◽  
1974 ◽  
Vol 247 (5442) ◽  
pp. 556-557 ◽  
Author(s):  
J. WILLIAMS ◽  
A. G. WILKINS
Keyword(s):  
Amino Acid ◽  
Gene Duplication ◽  
Amino Acid Sequence ◽  
Glutamate Dehydrogenase ◽  
Partial Gene Duplication

Human and Bovine Prothrombin: Sequence Homology

1975 ◽  
Author(s):  
D. A. Walz ◽  
D. Hewett-Emmett ◽  
J. Reuterby ◽  
L. E. McCoy ◽  
W. H. Seegers
Keyword(s):  
Amino Acid ◽  
Gene Duplication ◽  
Amino Acid Sequence ◽  
Molecular Size ◽  
Factor Ix ◽  
Factor X ◽  
Initial Sequence ◽  
Human Thrombin ◽  
Prothrombin Gene ◽  
A Chain

Bovine and human prothrombins can be selectively activated to release PR fragment and 0 fragment. In addition, the generation of human thrombin is accompanied by the loss of a 13 residue peptide, designated Al. We have determined the complete amino acid sequence of the non-thrombin portion of bovine prothrombin and have established regions of significant internal homology. A region of bovine PR fragment (66-128) is homologous to a region of the bovine 0 fragment (15-77). In addition, residues 1-14 of the 0 fragment and residues 17-30 of the A chain of thrombin are homologous. A theoretical primordial prothrombin gene can be proposed: chromosomal misalignment and an unequal crossover of this gene would account for the internal homology and for the molecular size of prothrombin which is approximately 16,000 daltons greater than its related molecules, autoprothrombin III (Factor X) and Factor IX. Preliminary structure work on human prothrombin supports this gene duplication hypothesis. The initial sequence of human PR fragment is nearly identical to that of bovine PR fragment, presumably due to the functionally important modified glutamic acid residues. The 0 fragment and A chain of human prothrombin are also homologous.

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

Gene action in the human haptoglobins. IV. Amino acid sequence studies on the haptoglobin α chains

1970 ◽  
Vol 48 (1) ◽  
pp. 133-146 ◽  
Author(s):  
J. A. Black ◽  
G. H. Dixon
Keyword(s):  
Amino Acid ◽  
Sequence Analysis ◽  
Amino Acid Sequence ◽  
Amino Acid Sequences ◽  
Dansyl Amino Acids ◽  
Tryptic Peptides ◽  
Specific Chemical ◽  
Chloromethyl Ketone ◽  
Partial Gene Duplication ◽  
Arginyl Residues

Alpha chains of human haptoglobin have been prepared from whole haptoglobin of genetic type Hp 2–1 purified from the ascites fluid of a single patient. Amino acid sequence analysis has been carried out on these light chains which represent the products α1S and α2(F,S) of the single genes Hp1S and Hp2(F,S), and are, respectively, 83 and 142 residues in length. The data reported here concern the sequence analysis of two series of tryptic peptides, one obtained by unlimited cleavage of the chains by p-toluene sulfonamido-phenylethyl chloromethyl ketone - trypsin, and the second following limitation of trypsin cleavage to arginyl residues after modification of lysyl residues by trifluoracetylation. The major technique for sequence analysis of these peptides was a modification of the p-dimethylaminonaphthalene-sulfonyl-Edman (dansyl-Edman) procedure employing a new thin-layer chromatographic separation of the dansyl-amino acids. The sequences of these tryptic peptides in conjunction with those of the chymotryptic peptides allowed the unequivocal deduction of portions of the sequence, but the final overlaps were provided by fragments obtained by specific chemical cleavage of the chain at aspartyl residues. The amino acid sequences deduced have documented the occurrence of a partial gene duplication in the gene product α2(F,S) of the Hp2(F,S) gene.

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.

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
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