Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:Q07644 (polypeptide)
 72,197 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The amino acid sequences of one of the dimeric hemoglobin components, CTT-X, of Chironomus thummi thummi (Diptera) are given. The sequences were determined by automatic Edman degradation of tryptic peptides and peptides obtained by specific chemical cleavages. CTT-X has two different polypeptide chains, each with 151 amino acid residues. The two polypeptide chains differ only in one amino acid. The sequences are discussed in the light of the sequences of other related heme-proteins.
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PMID:Hemoglobins, XXIX. Sequence analysis of a dimeric hemoglobin (erythrocruorin), CTT-X, of Chironomus thummi thummi (Diptera). 49 57

Peptides corresponding to the N- and C-extremities of the adenovirus 2 fibre polypeptide were synthesized, coupled to tetanus toxoid and injected into rabbits. Two sera were obtained: the anti-NTT serum and the anti-CTT serum. These sera and an anti-native-fibre serum were used to study fragments generated by hydrochloric acid cleavage of the fibre. The 44-Kd fragment corresponding to the 2/3 N-terminal part of the molecule retained its antigenic reactivity. This is consistent with a shaft structure for this part of the fibre. The anti-peptide sera were used to orientate the fibre, i.e., to determine the site of anchorage of this protein in the penton base. First, immunorevelation of blots of enzymatic digests of native or dissociated penton suggested that the N-extremity of the fibre was involved in the assembly of this protein in the penton base. Second, attempts were made to determine the accessibility of the fibre ends in the penton structure by ELISA assays and by immunorevelation of penton in Western blots. The results agreed with the proposed orientation derived from study of the enzymatic digests. Since the 2 anti-peptide sera and the peptides were unable to affect viral adsorption, it was not possible to determine how the fibre is orientated with respect to the cell receptor. However, the anti-peptide sera were found to inhibit viral production slightly.
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PMID:Structural study of adenovirus type 2 fibre using anti-fibre and anti-peptide sera. 315

The nucleotide sequence of a segment of the mtDNA molecule of Drosophila yakuba has been determined, within which have been identified the genes for tRNAleuUUR, cytochrome c oxidase subunit II (COII), tRNAlys, tRNAasp, URFA6L, ATPase subunit 6 (ATPase6), cytochrome c oxidase subunit III (COIII) and tRNAgly. The genes are arranged in the order given and all are transcribed from the same strand of the molecule in a direction opposite to that in which replication proceeds around the molecule. The tRNAlys gene is unusual among mitochondrial tRNAlys genes in that it contains a CTT anticodon. The triplet AGA is used to specify an amino acid in all of the COII, COIII, ATPase6, and URFA6L genes. However, the AGA codons found in these four polypeptide genes correspond in position to codons which specify nine different amino acids, but never arginine, in the equivalent polypeptide gene which have been sequenced from mtDNAs of mouse, yeast and Zea mays.
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PMID:Nucleotide sequence of a segment of Drosophila mitochondrial DNA that contains the genes for cytochrome c oxidase subunits II and III and ATPase subunit 6. 630 79

Comparison of the high-field 1H-NMR spectra of the met-cyano complexes of allosteric haemoglobins III and IV of the insect larva Chironomus thummi thummi (CTT-III and CTT-IV) shows that, in addition to the molecular heterogeneity previously described for both Hbs as due to haem orientational disorder [La Mar et al. (1980) J. Biol. Chem. 255, 66-70], CTT-III but not CTT-IV exhibits a second heterogeneity as evidenced by splitting of numerous signals. Reconstitution of CTT-III with modified haems alters the populations of the two haem rotational isomers but leaves the secondary heterogeneity unaffected. This argues directly for locating this secondary heterogeneity solely within the polypeptide chain rather than the result of protein-haem interaction. We assign this secondary heterogeneity found solely in Hb-III to a point mutation in the haem cavity, 57E6 (Ile/Thr); CTT-IV is chemically homogeneous. The observation of significant hyperfine shift differences for the alternative substitution at 57E6, particularly for non-haem single-proton resonances thought to arise from distal residues, indicates some structural consequences in the haem cavity due to the point mutation. While a difference in the allosteric properties cannot be detected in that the point mutation appears to leave the pK for the allosteric transition unaltered, subtle influences on the function of the protein in both affinity states cannot be ruled out at this time.
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PMID:High-resolution proton NMR as indicator of a silent mutation in the haem cavity of a monomeric allosteric haemoglobin. 661 56

The sequence analysis of the monomeric hemoglobin CTT I (erythrocruorin) of Chironomus thummi thummi is given. The tryptic peptides were separated and sequenced by automatic Edman degradation. The alignment was established with help of some peptic peptides. In CTT I two polypeptide chains are present. They differ in position 98, where we found alanine and threonine in the ratio 1:1. CTT I is compared with human myoglobin and the monomeric component CTT III. The dimeric components of CTT are also included into the discussion, because CTT I seems to have an enlarged heme pocket like them. We particularly compare the amino acid residues involved in the heme contacts. The lack of a Bohr effect is discussed.
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PMID:[Hemoglobin, XXXI. Analysis or the primary structure of the monomeric hemoglobin CTT I (erythrocruorin) of Chironomus thummi thummi, Diptera]. 738 Mar 86

The 11.3 kb plasmid pSE101 integrates into the chromosome of Saccharopolyspora erythraea at a specific attB site and into the chromosome of Streptomyces lividans at many sites. Multisite integration in S. lividans was also observed when a 1.9 kb segment of pSE101 containing attP and adjacent plasmid sequence was used to transform a pSE101- S. lividans host. Nucleotide sequencing of this segment revealed the presence of a complete open reading frame (ORF) designated int, encoding a putative polypeptide of 448 amino acids that shows similarities to site-specific recombinases of the integrase family. Sequencing of the 1.3 kb segment upstream of int revealed the presence of three additional ORFs: the one most distal to int encodes a putative 76 amino acid basic polypeptide analogous to the Xis proteins of a number of bacteriophages. Nucleotide sequencing of attP, and the attB, attL and attR sites from Sac. erythraea revealed a 46 bp sequence common to all sites with no duplications of chromosomal sequences in the integrated state. A putative structural gene for a tRNA(Thr) was found to overlap the 46 bp common sequence at attB. Sequencing of four pSE101 integration sites (attB') and corresponding attL' and attR' sites in S. lividans showed that the 46 bp sequence was present at each attR' site, whereas only the first three bases, CTT, were retained at each attL' and attB' site. A feature common to the four attB' sites and to attB is a highly conserved 21 bp segment with inverted repeats flanking the CTT sequence.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Characterization of the genes and attachment sites for site-specific integration of plasmid pSE101 in Saccharopolyspora erythraea and Streptomyces lividans. 815 69

Proteus mirabilis urease, a nickel-containing enzyme, has been established as a critical virulence determinant in urinary tract infection. An amino acid sequence (residues 308 to 327: TVDEHLDMLMVCHHLDPSIP) within the large urease subunit, UreC, is highly conserved for every urease examined thus far and has been suggested to reside within the enzyme active site. Histidine residues have been postulated to play a role in catalysis by coordinating Ni2+ ions. To test this hypothesis, oligonucleotide-directed mutagenesis was used to change amino acid His-320 to Leu-320 within UreC. The base change (CAT for His-320 to CTT for Leu-320) was confirmed by DNA sequencing. The recombinant and mutant proteins were expressed at similar levels in Escherichia coli as detected by Western blotting (immunoblotting) of denaturing and nondenaturing gels. Specific activities of the enzymes were quantitated after partial purification. Strains expressing the mutant enzyme showed no detectable activity, whereas strains expressing the recombinant enzyme hydrolyzed urea at 149 mumol of NH3 per min per mg of protein. In addition, the mutant enzyme was able to incorporate only about one-half (58%) of the amount of 63Ni2+ incorporated by the active recombinant enzyme. While the mutation of His-320 to Leu-320 within UreC does not affect expression or assembly of urease polypeptide subunits UreA, UreB, and UreC His-320 of UreC is required for urea hydrolysis and proper incorporation of Ni2+ into apoenzyme.
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PMID:Proteus mirabilis urease: histidine 320 of UreC is essential for urea hydrolysis and nickel ion binding within the native enzyme. 850 Aug 94