Open Access
I. The complete amino acid sequence of acyl carrier protein of Escherichia coli
T. C. Vanaman
- Vol. 29
TLDR
The complete amino acid sequence of the acyl carrier protein (ACP) from Escherichia coli has been established and contains 77 residues with NH2- terminal serine and COOH-terminal alanine.Abstract:
Abstract The complete amino acid sequence of the acyl carrier protein (ACP) from Escherichia coli has been established. It contains 77 residues with NH2-terminal serine and COOH-terminal alanine. The pantotheine prosthetic group of ACP is attached covalently to the hydroxyl group of serine at residue 36, which is 1 of 3 seryl residues in the molecule. This unique sequence was deduced by sequence analysis of the tryptic, peptic, and thermolysin peptides isolated from enzymic hydrolysates of ACP as described earlier. Important overlaps in sequence were also obtained by partial sequence analysis of one of the two unique peptides formed on cleavage of ACP with CNBr, and by sequence analysis of a single tryptic peptide isolated from tryptic digests of ACP modified at its single arginyl residue with 1,2-cyclohexanedione.read more
Citations
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Journal ArticleDOI
Similar Amino Acid Sequences: Chance or Common Ancestry?
TL;DR: The systemic comparison of every newly determined amino acid sequence with all other known sequences may allow a complete reconstruction of the evolutionary events leading to contemporary proteins, but sometimes the surviving similarities are so vague that even computer-based sequence comparisons procedures are unable to validate relationships.
Journal ArticleDOI
Posttranslational covalent modification of proteins
TL;DR: A brief consideration of the questions about where and when the derivatization reactions occur, how the specificity of the reactions is established, and how the posttranslational modifications can facilitate biological processes, reveal a need for more information on all these points.
Journal ArticleDOI
Structural and functional organization of the animal fatty acid synthase.
TL;DR: A revised model for the fatty acid synthase is suggested in which the two polypeptides are oriented such that head-to-tail contacts are formed both between and within subunits.
Journal ArticleDOI
The multifunctional 6-methylsalicylic acid synthase gene of Penicillium patulum. Its gene structure relative to that of other polyketide synthases.
TL;DR: The low similarity between the two P. patulum polyketide synthases, MSAS and FAS, possibly supports a convergent rather than a divergent evolution of both multienzyme proteins.
References
More filters
Journal ArticleDOI
Similar Amino Acid Sequences: Chance or Common Ancestry?
TL;DR: The systemic comparison of every newly determined amino acid sequence with all other known sequences may allow a complete reconstruction of the evolutionary events leading to contemporary proteins, but sometimes the surviving similarities are so vague that even computer-based sequence comparisons procedures are unable to validate relationships.
Journal ArticleDOI
Posttranslational covalent modification of proteins
TL;DR: A brief consideration of the questions about where and when the derivatization reactions occur, how the specificity of the reactions is established, and how the posttranslational modifications can facilitate biological processes, reveal a need for more information on all these points.
Journal ArticleDOI
Structural and functional organization of the animal fatty acid synthase.
TL;DR: A revised model for the fatty acid synthase is suggested in which the two polypeptides are oriented such that head-to-tail contacts are formed both between and within subunits.
Journal ArticleDOI
The multifunctional 6-methylsalicylic acid synthase gene of Penicillium patulum. Its gene structure relative to that of other polyketide synthases.
TL;DR: The low similarity between the two P. patulum polyketide synthases, MSAS and FAS, possibly supports a convergent rather than a divergent evolution of both multienzyme proteins.
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