Sequence Similarities and Evolutionary Relationships of Microbial, Plant and Animal α‐amylases
Amino acid sequence comparison of 37 α‐amylases from microbial, plant and animal sources was performed to identify their mutual sequence similarities in addition to the five already described conserved regions. These sequence regions were examined from structure/function and evolutionary perspective...
Published in: | European Journal of Biochemistry |
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Online Access: | http://dx.doi.org/10.1111/j.1432-1033.1994.00519.x https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1111%2Fj.1432-1033.1994.00519.x https://febs.onlinelibrary.wiley.com/doi/pdf/10.1111/j.1432-1033.1994.00519.x |
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crwiley:10.1111/j.1432-1033.1994.00519.x 2024-06-02T07:57:11+00:00 Sequence Similarities and Evolutionary Relationships of Microbial, Plant and Animal α‐amylases Janeček, Štefan 1994 http://dx.doi.org/10.1111/j.1432-1033.1994.00519.x https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1111%2Fj.1432-1033.1994.00519.x https://febs.onlinelibrary.wiley.com/doi/pdf/10.1111/j.1432-1033.1994.00519.x en eng Wiley http://onlinelibrary.wiley.com/termsAndConditions#vor European Journal of Biochemistry volume 224, issue 2, page 519-524 ISSN 0014-2956 1432-1033 journal-article 1994 crwiley https://doi.org/10.1111/j.1432-1033.1994.00519.x 2024-05-03T11:29:55Z Amino acid sequence comparison of 37 α‐amylases from microbial, plant and animal sources was performed to identify their mutual sequence similarities in addition to the five already described conserved regions. These sequence regions were examined from structure/function and evolutionary perspectives. An unrooted evolutionary tree of α‐amylases was constructed on a subset of 55 residues from the alignment of sequence similarities along with conserved regions. The most important new information extracted from the tree was as follows: (a) the close evolutionary relationship of Alteromonas haloplanctis α‐amylase (thermolabile enzyme from an antarctic psychrotroph) with the already known group of homologous α‐amylases from streptomycetes, Thermomonospora curvata , insects and mammals, and (b) the remarkable 40.1% identity between starch‐saccharifying Bacillus subtilis α‐amylase and the enzyme from the ruminal bacterium Butyrivibrio fibrisolvens , an α‐amylase with an unusually large polypeptide chain (943 residues in the mature enzyme). Due to a very high degree of similarity, the whole amino acid sequences of three groups of α‐amylases, namely (a) fungi and yeasts, (b) plants, and (c) A. haloplanctis , streptomycetes, T. curvata , insects and mammals, were aligned independently and their unrooted distance trees were calculated using these alignments. Possible rooting of the trees was also discussed. Based on the knowledge of the location of the five disulfide bonds in the structure of pig pancreatic α‐amylase, the possible disulfide bridges were established for each of these groups of homologous α‐amylases. Article in Journal/Newspaper Antarc* Antarctic Wiley Online Library Antarctic European Journal of Biochemistry 224 2 519 524 |
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Wiley Online Library |
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crwiley |
language |
English |
description |
Amino acid sequence comparison of 37 α‐amylases from microbial, plant and animal sources was performed to identify their mutual sequence similarities in addition to the five already described conserved regions. These sequence regions were examined from structure/function and evolutionary perspectives. An unrooted evolutionary tree of α‐amylases was constructed on a subset of 55 residues from the alignment of sequence similarities along with conserved regions. The most important new information extracted from the tree was as follows: (a) the close evolutionary relationship of Alteromonas haloplanctis α‐amylase (thermolabile enzyme from an antarctic psychrotroph) with the already known group of homologous α‐amylases from streptomycetes, Thermomonospora curvata , insects and mammals, and (b) the remarkable 40.1% identity between starch‐saccharifying Bacillus subtilis α‐amylase and the enzyme from the ruminal bacterium Butyrivibrio fibrisolvens , an α‐amylase with an unusually large polypeptide chain (943 residues in the mature enzyme). Due to a very high degree of similarity, the whole amino acid sequences of three groups of α‐amylases, namely (a) fungi and yeasts, (b) plants, and (c) A. haloplanctis , streptomycetes, T. curvata , insects and mammals, were aligned independently and their unrooted distance trees were calculated using these alignments. Possible rooting of the trees was also discussed. Based on the knowledge of the location of the five disulfide bonds in the structure of pig pancreatic α‐amylase, the possible disulfide bridges were established for each of these groups of homologous α‐amylases. |
format |
Article in Journal/Newspaper |
author |
Janeček, Štefan |
spellingShingle |
Janeček, Štefan Sequence Similarities and Evolutionary Relationships of Microbial, Plant and Animal α‐amylases |
author_facet |
Janeček, Štefan |
author_sort |
Janeček, Štefan |
title |
Sequence Similarities and Evolutionary Relationships of Microbial, Plant and Animal α‐amylases |
title_short |
Sequence Similarities and Evolutionary Relationships of Microbial, Plant and Animal α‐amylases |
title_full |
Sequence Similarities and Evolutionary Relationships of Microbial, Plant and Animal α‐amylases |
title_fullStr |
Sequence Similarities and Evolutionary Relationships of Microbial, Plant and Animal α‐amylases |
title_full_unstemmed |
Sequence Similarities and Evolutionary Relationships of Microbial, Plant and Animal α‐amylases |
title_sort |
sequence similarities and evolutionary relationships of microbial, plant and animal α‐amylases |
publisher |
Wiley |
publishDate |
1994 |
url |
http://dx.doi.org/10.1111/j.1432-1033.1994.00519.x https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1111%2Fj.1432-1033.1994.00519.x https://febs.onlinelibrary.wiley.com/doi/pdf/10.1111/j.1432-1033.1994.00519.x |
geographic |
Antarctic |
geographic_facet |
Antarctic |
genre |
Antarc* Antarctic |
genre_facet |
Antarc* Antarctic |
op_source |
European Journal of Biochemistry volume 224, issue 2, page 519-524 ISSN 0014-2956 1432-1033 |
op_rights |
http://onlinelibrary.wiley.com/termsAndConditions#vor |
op_doi |
https://doi.org/10.1111/j.1432-1033.1994.00519.x |
container_title |
European Journal of Biochemistry |
container_volume |
224 |
container_issue |
2 |
container_start_page |
519 |
op_container_end_page |
524 |
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1800739601137008640 |