author_facet FISCHER, Stephan
TSUGITA, Akira
FISCHER, Stephan
TSUGITA, Akira
author FISCHER, Stephan
TSUGITA, Akira
spellingShingle FISCHER, Stephan
TSUGITA, Akira
European Journal of Biochemistry
Amino Acid Sequence around the Active Site of Two Class I Fructose‐1,6‐Bisphosphate Aldolases from Staphylococci
Biochemistry
author_sort fischer, stephan
spelling FISCHER, Stephan TSUGITA, Akira 0014-2956 1432-1033 Wiley Biochemistry http://dx.doi.org/10.1111/j.1432-1033.1982.tb06970.x <jats:p>The amino acid sequences of a 26‐residue segment containing the active‐site lysyl residue of the class I fructose‐1,6‐bisphosphate aldolases from <jats:italic>Staphylococcus aureus</jats:italic> and <jats:italic>Staphylococcus epidermidis</jats:italic> have been determined. The sequence homology within the active sites between these enzymes and those from several eucaryotic class I aldolases showed a maximum of 21%. The similarity may indicate the origin of both procaryotic and eucaryotic class I aldolases from a common ancestor.</jats:p> Amino Acid Sequence around the Active Site of Two Class I Fructose‐1,6‐Bisphosphate Aldolases from Staphylococci European Journal of Biochemistry
doi_str_mv 10.1111/j.1432-1033.1982.tb06970.x
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series European Journal of Biochemistry
source_id 49
title Amino Acid Sequence around the Active Site of Two Class I Fructose‐1,6‐Bisphosphate Aldolases from Staphylococci
title_unstemmed Amino Acid Sequence around the Active Site of Two Class I Fructose‐1,6‐Bisphosphate Aldolases from Staphylococci
title_full Amino Acid Sequence around the Active Site of Two Class I Fructose‐1,6‐Bisphosphate Aldolases from Staphylococci
title_fullStr Amino Acid Sequence around the Active Site of Two Class I Fructose‐1,6‐Bisphosphate Aldolases from Staphylococci
title_full_unstemmed Amino Acid Sequence around the Active Site of Two Class I Fructose‐1,6‐Bisphosphate Aldolases from Staphylococci
title_short Amino Acid Sequence around the Active Site of Two Class I Fructose‐1,6‐Bisphosphate Aldolases from Staphylococci
title_sort amino acid sequence around the active site of two class i fructose‐1,6‐bisphosphate aldolases from staphylococci
topic Biochemistry
url http://dx.doi.org/10.1111/j.1432-1033.1982.tb06970.x
publishDate 1982
physical 343-348
description <jats:p>The amino acid sequences of a 26‐residue segment containing the active‐site lysyl residue of the class I fructose‐1,6‐bisphosphate aldolases from <jats:italic>Staphylococcus aureus</jats:italic> and <jats:italic>Staphylococcus epidermidis</jats:italic> have been determined. The sequence homology within the active sites between these enzymes and those from several eucaryotic class I aldolases showed a maximum of 21%. The similarity may indicate the origin of both procaryotic and eucaryotic class I aldolases from a common ancestor.</jats:p>
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author FISCHER, Stephan, TSUGITA, Akira
author_facet FISCHER, Stephan, TSUGITA, Akira, FISCHER, Stephan, TSUGITA, Akira
author_sort fischer, stephan
container_issue 2-3
container_start_page 343
container_title European Journal of Biochemistry
container_volume 128
description <jats:p>The amino acid sequences of a 26‐residue segment containing the active‐site lysyl residue of the class I fructose‐1,6‐bisphosphate aldolases from <jats:italic>Staphylococcus aureus</jats:italic> and <jats:italic>Staphylococcus epidermidis</jats:italic> have been determined. The sequence homology within the active sites between these enzymes and those from several eucaryotic class I aldolases showed a maximum of 21%. The similarity may indicate the origin of both procaryotic and eucaryotic class I aldolases from a common ancestor.</jats:p>
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id ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTExMS9qLjE0MzItMTAzMy4xOTgyLnRiMDY5NzAueA
imprint Wiley, 1982
imprint_str_mv Wiley, 1982
institution DE-14, DE-105, DE-Ch1, DE-L229, DE-D275, DE-Bn3, DE-Brt1, DE-Zwi2, DE-D161, DE-Zi4, DE-Gla1, DE-15, DE-Pl11, DE-Rs1
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source_id 49
spelling FISCHER, Stephan TSUGITA, Akira 0014-2956 1432-1033 Wiley Biochemistry http://dx.doi.org/10.1111/j.1432-1033.1982.tb06970.x <jats:p>The amino acid sequences of a 26‐residue segment containing the active‐site lysyl residue of the class I fructose‐1,6‐bisphosphate aldolases from <jats:italic>Staphylococcus aureus</jats:italic> and <jats:italic>Staphylococcus epidermidis</jats:italic> have been determined. The sequence homology within the active sites between these enzymes and those from several eucaryotic class I aldolases showed a maximum of 21%. The similarity may indicate the origin of both procaryotic and eucaryotic class I aldolases from a common ancestor.</jats:p> Amino Acid Sequence around the Active Site of Two Class I Fructose‐1,6‐Bisphosphate Aldolases from Staphylococci European Journal of Biochemistry
spellingShingle FISCHER, Stephan, TSUGITA, Akira, European Journal of Biochemistry, Amino Acid Sequence around the Active Site of Two Class I Fructose‐1,6‐Bisphosphate Aldolases from Staphylococci, Biochemistry
title Amino Acid Sequence around the Active Site of Two Class I Fructose‐1,6‐Bisphosphate Aldolases from Staphylococci
title_full Amino Acid Sequence around the Active Site of Two Class I Fructose‐1,6‐Bisphosphate Aldolases from Staphylococci
title_fullStr Amino Acid Sequence around the Active Site of Two Class I Fructose‐1,6‐Bisphosphate Aldolases from Staphylococci
title_full_unstemmed Amino Acid Sequence around the Active Site of Two Class I Fructose‐1,6‐Bisphosphate Aldolases from Staphylococci
title_short Amino Acid Sequence around the Active Site of Two Class I Fructose‐1,6‐Bisphosphate Aldolases from Staphylococci
title_sort amino acid sequence around the active site of two class i fructose‐1,6‐bisphosphate aldolases from staphylococci
title_unstemmed Amino Acid Sequence around the Active Site of Two Class I Fructose‐1,6‐Bisphosphate Aldolases from Staphylococci
topic Biochemistry
url http://dx.doi.org/10.1111/j.1432-1033.1982.tb06970.x