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The Journal of biological chemistry1985; 260(10); 6129-6132;

The sequence of equine muscle carbonic anhydrase.

Abstract: The sequence of equine muscle carbonic anhydrase (CA-III) has been determined. The 2 reactive cysteines of the 5 such residues have been localized. A strong sequence homology to other mammalian carbonic anhydrases exists, and 91% of the residues in the equine and bovine muscle forms are identical.
Publication Date: 1985-05-25 PubMed ID: 3922970
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  • Comparative Study
  • Journal Article
  • Research Support
  • Non-U.S. Gov't
  • Research Support
  • U.S. Gov't
  • P.H.S.

Summary

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The study focused on determining the sequence and physical characteristics of equine muscle carbonic anhydrase, a vital enzyme in horses, and found a strong similarity to equivalent enzymes in other mammalian species.

Understanding Carbonic Anhydrase (CA-III)

  • Carbonic anhydrases (CAs) are proteins or enzymes found in mammals, which aid in the rapid conversion of carbon dioxide to bicarbonate and protons.
  • In this study, the scientists have focused on the variant known as CA-III, specifically in horses, also known as equine muscle carbonic anhydrase.

Determining the Sequence of CA-III

  • The main goal of this study was to determine the specific sequence of equine muscle CA-III. The sequence of a protein refers to the order of its building blocks (amino acids), which is crucial for its function.
  • This sequence determination was accomplished, and also identified the locations of two reactive cysteines out of five such residues. Cysteine is a critical amino acid that can be reactive and forms disulfide bridges that contribute to protein stability.

Comparing Equine CA-III with Cow’s CA-III

  • Another key finding of this study was the strong homology, or sequence similarity, between the equine muscle carbonic anhydrase and the same enzyme in other mammals. More specifically, the researchers found that 91% of the residues, or specific molecular locations, in the equine and bovine (cow) muscle forms are identical.
  • This level of similarity indicates a strong evolutionary relationship between these two species, at least concerning this specific protein. It means that the protein’s function is likely highly conserved and crucial for mammalian life, as changes in its structure could significantly impact its purpose.

Implications and Future Work

  • This research sets the stage for further comparisons between equine carbonic anhydrase and the same enzyme in other species, adding to our understanding of the enzyme’s evolution and function.
  • It can also help in understanding the pathologies linked with muscle carbonic anhydrase, as knowledge of its sequence and structure can be key in pinpointing how and when things go wrong at a molecular level.

Cite This Article

APA
Wendorff KM, Nishita T, Jabusch JR, Deutsch HF. (1985). The sequence of equine muscle carbonic anhydrase. J Biol Chem, 260(10), 6129-6132.

Publication

ISSN: 0021-9258
NlmUniqueID: 2985121R
Country: United States
Language: English
Volume: 260
Issue: 10
Pages: 6129-6132

Researcher Affiliations

Wendorff, K M
    Nishita, T
      Jabusch, J R
        Deutsch, H F

          MeSH Terms

          • Amino Acid Sequence
          • Animals
          • Carbonic Anhydrases
          • Cattle
          • Horses
          • Isoenzymes
          • Muscles / enzymology
          • Species Specificity

          Grant Funding

          • CA-1786 / NCI NIH HHS

          Citations

          This article has been cited 2 times.
          1. Cabiscol E, Levine RL. The phosphatase activity of carbonic anhydrase III is reversibly regulated by glutathiolation. Proc Natl Acad Sci U S A 1996 Apr 30;93(9):4170-4.
            doi: 10.1073/pnas.93.9.4170pubmed: 8633035google scholar: lookup
          2. Wade R, Gunning P, Eddy R, Shows T, Kedes L. Nucleotide sequence, tissue-specific expression, and chromosome location of human carbonic anhydrase III: the human CAIII gene is located on the same chromosome as the closely linked CAI and CAII genes. Proc Natl Acad Sci U S A 1986 Dec;83(24):9571-5.
            doi: 10.1073/pnas.83.24.9571pubmed: 3099285google scholar: lookup