scholarly journals Glutamate-1-semialdehyde aminotransferase from Sulfolobus solfataricus*

1996 ◽  
Vol 320 (2) ◽  
pp. 541-545 ◽  
Author(s):  
Gianna PALMIERI ◽  
Michela DI PALO ◽  
Andrea SCALONI ◽  
Stefania ORRÙ ◽  
Gennaro MARINO ◽  
...  
Keyword(s):  
Absorption Spectrum ◽  
Sulfolobus Solfataricus ◽  
Active Form ◽  
Thermophilic Bacterium ◽  
Aminotransferase Activity ◽  
Terminal Amino Acid ◽  
Significant Similarity ◽  
Terminal Amino ◽  
C5 Pathway ◽  
Terminal Amino Acid Sequence

Glutamate-1-semialdehyde aminotransferase (GSA-AT) from the extremely thermophilic bacterium Sulfolobus solfataricus has been purified to homogeneity and characterized. GSA-AT is the last enzyme in the C5 pathway for the conversion of glutamate into the tetrapyrrole precursor Δ-aminolaevulinate (ALA) in plants, algae and several bacteria. The active form of GSA-AT from S. solfataricus seems to be a homodimer with a molecular mass of 87 kDa. The absorption spectrum of the purified aminotransferase is indicative of the presence of pyridoxamine 5´-phosphate (PMP) cofactor, and the catalytic activity of the enzyme is further stimulated by addition of PMP. 3-Amino-2,3-dihydrobenzoic acid is an inhibitor of the aminotransferase activity. The N-terminal amino acid sequence of GSA-AT from S. solfataricus was found to share significant similarity with the eukaryotic and eubacterial enzymes. Evidence is provided that ALA synthesis in S. solfataricus follows the C5 pathway characteristic of plants, algae, cyanobacteria and many other bacteria.

scholarly journals Production of Native-Type Streptoverticillium mobaraense Transglutaminase in Corynebacterium glutamicum

2003 ◽  
Vol 69 (5) ◽  
pp. 3011-3014 ◽  
Author(s):  
Masayo Date ◽  
Kei-ichi Yokoyama ◽  
Yukiko Umezawa ◽  
Hiroshi Matsui ◽  
Yoshimi Kikuchi
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Corynebacterium Glutamicum ◽  
Cleavage Site ◽  
Active Form ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Terminal Amino Acid ◽  
Terminal Amino ◽  
Terminal Amino Acid Sequence

ABSTRACT We previously observed secretion of active-form transglutaminase in Corynebacterium glutamicum by coexpressing the subtilisin-like protease SAM-P45 from Streptomyces albogriseolus to process the prodomain. However, the N-terminal amino acid sequence of the transglutaminase differed from that of the native Streptoverticillium mobaraense enzyme. In the present work we have used site-directed mutagenesis to generate an optimal SAM-P45 cleavage site in the C-terminal region of the prodomain. As a result, native-type transglutaminase was secreted.

scholarly journals The NADP-Dependent Methylene Tetrahydromethanopterin Dehydrogenase in Methylobacterium extorquens AM1

1998 ◽  
Vol 180 (20) ◽  
pp. 5351-5356 ◽  
Author(s):  
Julia A. Vorholt ◽  
Ludmila Chistoserdova ◽  
Mary E. Lidstrom ◽  
Rudolf K. Thauer
Keyword(s):  
Specific Activity ◽  
Catalytic Efficiency ◽  
Methanogenic Archaea ◽  
Methylobacterium Extorquens ◽  
Terminal Amino Acid ◽  
Significant Similarity ◽  
Apparent Homogeneity ◽  
Formaldehyde Oxidation ◽  
Terminal Amino ◽  
Terminal Amino Acid Sequence

ABSTRACT An NADP-dependent methylene tetrahydromethanopterin (H4MPT) dehydrogenase has recently been proposed to be involved in formaldehyde oxidation to CO2 inMethylobacterium extorquens AM1. We report here on the purification of this novel enzyme to apparent homogeneity. Via the N-terminal amino acid sequence, it was identified to be themtdA gene product. The purified enzyme catalyzed the dehydrogenation of methylene H4MPT with NADP+rather than with NAD+, with a specific activity of approximately 400 U/mg of protein. It also catalyzed the dehydrogenation of methylene tetrahydrofolate (methylene H4F) with NADP+. With methylene H4F as the substrate, however, the specific activity (26 U/mg) and the catalytic efficiency (V max/Km ) were approximately 20-fold lower than with methylene H4MPT. Whereas the dehydrogenation of methylene H4MPT (E0 = −390 mV) with NADP+ (E0 = −320 mV) proceeded essentially irreversibly, the dehydrogenation of methylene H4F (E0 = −300 mV) was fully reversible. Comparison of the primary structure of the NADP-dependent dehydrogenase fromM. extorquens AM1 with those of methylene H4F dehydrogenases from other bacteria and eucarya and with those of methylene H4MPT dehydrogenases from methanogenic archaea revealed only marginally significant similarity (<15%).

C-Terminal amino acid sequence of chicken pepsinogen and its homology with sequences of other acid proteases

1980 ◽  
Vol 45 (4) ◽  
pp. 1144-1154 ◽  
Author(s):  
Miroslav Baudyš ◽  
Helena Keilová ◽  
Vladimír Kostka
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
The Other ◽  
Terminal Sequence ◽  
Terminal Part ◽  
Terminal Amino Acid ◽  
Tryptic Peptides ◽  
Terminal Amino ◽  
High Degree ◽  
Terminal Amino Acid Sequence

To determine the primary structure of the C-terminal part of the molecule of chicken pepsinogen the tryptic, chymotryptic and thermolytic digest of the protein were investigated and peptides derived from this region were sought. These peptides permitted the following 21-residue C-terminal sequence to be determined: ...Ile-Arg-Glu-Tyr-Tyr-Val-Ile-Phe-Asp-Arg-Ala-Asn-Asn-Lys-Val-Gly-Leu-Ser-Pro-Leu-Ser.COOH. A comparison of this structure with the C-terminal sequential regions of the other acid proteases shows a high degree of homology between chicken pepsinogen and these proteases (e.g., the degree of homology with respect to hog pepsinogen and calf prochymosin is about 66%). Additional tryptic peptides, derived from the N-terminal part of the zymogen molecule whose amino acid sequence has been reported before, were also obtained in this study. This sequence was extended by two residues using an overlapping peptide. An ancillary result of this study was the isolation of tryptic peptides derived from other regions of the zymogen molecule.

scholarly journals The NH2- and COOH-terminal amino acid sequence of nuclear protein A24.

1976 ◽  
Vol 251 (19) ◽  
pp. 5901-5903 ◽  
Author(s):  
M O Olson ◽  
I L Goldknopf ◽  
K A Guetzow ◽  
G T James ◽  
T C Hawkins ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Nuclear Protein ◽  
Terminal Amino Acid ◽  
Terminal Amino ◽  
Terminal Amino Acid Sequence
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