DOI: 10.1111/j.1432-1033.1989.tb15202.x. Evolutionary relationships among aminotransferases

Evolutionary relationships among aminotransferases

10.1111/j.1432-1033.1989.tb15202.x

Crossref journal-article

Wiley

European Journal of Biochemistry (311)

Abstract

A data base was compiled containing the amino acid sequences of 12 aspartate aminotransferases and 11 other aminotransferases. A comparison of these sequences by a standard alignment method confirmed the previously reported homology of all aspartate aminotransferases and Escherichia coli tyrosine aminotransferase. However, no significant similarity between these proteins and any of the other aminotransferases was detected. A more rigorous analysis, focusing on short sequence segments rather than the total polypeptide chain, revealed that rat tyrosine aminotransferase and Saccharomyces cerevisiae and Escherichia coli histidinol‐phosphate aminotransferase share several homologous sequence segments with aspartate aminotransferases. For comparison of the complete sequences, a multiple sequence editor was developed to display the whole set of amino acid sequences in parallel on a single work‐sheet. The editor allows gaps in individual sequences or a set of sequences to be introduced and thus facilitates their parallel analysis and alignment. Several clusters of invariant residues at corresponding positions in the amino acid sequences became evident, clearly establishing that the cytosolic and the mitochondrial isoenzyme of vertebrate aspartate aminotransferase, E. coli aspartate aminotransferase, rat and E. coli tyrosine aminotransferase, and S. cerevisiae and E. coli histidinol‐phosphate aminotransferase are homologous proteins. Only 12 amino acid residues out of a total of about 400 proved to be invariant in all sequences compared; they are either involved in the binding of pyridoxal 5′‐phosphate and the substrate, or appear to be essential for the conformation of the enzymes.

Bibliography

MEHTA, P. K., HALE, T. I., & CHRISTEN, P. (1989). Evolutionary relationships among aminotransferases. European Journal of Biochemistry, 186(1â2), 249â253. Portico.

Authors 3

Perdeep K. MEHTA (first)
Terence I. HALE (additional)
Philipp CHRISTEN (additional)

References 39 Referenced 113

{'key': 'e_1_2_3_2_2', 'volume-title': 'Transaminases', 'author': 'Christen P.', 'year': '1985'} / Transaminases by Christen P. (1985)
{'key': 'e_1_2_3_3_2', 'first-page': '123', 'volume': '61', 'author': 'Christen P.', 'year': '1989', 'journal-title': 'Nova Acta Leopold.'} / Nova Acta Leopold. by Christen P. (1989)
10.1042/bj2340593
10.1016/S0021-9258(17)31222-X
10.1016/S0021-9258(19)81634-4
10.1111/j.1432-1033.1987.tb13597.x
10.1016/S0021-9258(17)38826-9
10.1073/pnas.83.5.1203
10.1093/oxfordjournals.jbchem.a135176
10.1042/bj2340049
10.1016/S0021-9258(17)42677-9
10.1126/science.2983426
10.1016/0022-2836(70)90057-4
{'key': 'e_1_2_3_15_2', 'first-page': '101', 'volume-title': 'Atlas of protein sequence and structure', 'author': 'Barker W. C.', 'year': '1972'} / Atlas of protein sequence and structure by Barker W. C. (1972)
10.1073/pnas.80.3.726
10.1016/S0021-9258(18)32129-X / J. Biol. Chem. by Graf‐Hausner U. (1983)
10.1093/oxfordjournals.jbchem.a122464
10.1016/0014-5793(73)80008-0
10.1016/0014-5793(79)80537-2
10.1016/S0021-9258(18)43714-3 / J. Biol. Chem. by Kagamiyama H. (1980)
10.1007/BF02100642
10.1007/978-3-0348-9308-4_7
10.1093/oxfordjournals.jbchem.a133543
10.1016/S0021-9258(19)75987-0
10.1016/0167-4838(85)90172-4
10.1093/oxfordjournals.jbchem.a135173
10.1016/0022-2836(85)90386-9
10.1007/BF00330437
10.1128/jb.164.3.1317-1323.1985 / J. Bacteriol. by Grisolia V. (1985)
{'key': 'e_1_2_3_31_2', 'author': 'Martinez‐Carrion M.', 'year': '1989', 'journal-title': 'Ann. NY Acad. Sci.'} / Ann. NY Acad. Sci. by Martinez‐Carrion M. (1989)
{'key': 'e_1_2_3_32_2', 'first-page': '187', 'volume-title': 'Active sites of enzymes', 'author': 'Jansonius J. N.', 'year': '1987'} / Active sites of enzymes by Jansonius J. N. (1987)
10.1073/pnas.77.5.2559
10.1016/0022-2836(84)90333-4
10.1073/pnas.71.10.3888
10.1016/S0021-9258(18)34493-4 / J. Biol. Chem. by Sandmeier E. (1982)
10.1101/SQB.1987.052.01.046
{'key': 'e_1_2_3_38_2', 'first-page': '109', 'volume-title': 'Transaminases', 'author': 'Jansonius J. N.', 'year': '1985'} / Transaminases by Jansonius J. N. (1985)
10.1038/scientificamerican1085-88
10.1093/oxfordjournals.jbchem.a122600

Dates

Type	When
Created	20 years, 6 months ago (March 3, 2005, 11:05 p.m.)
Deposited	2 years ago (Aug. 31, 2023, 3:41 p.m.)
Indexed	1 month ago (Aug. 5, 2025, 8:57 a.m.)
Issued	35 years, 9 months ago (Dec. 1, 1989)
Published	35 years, 9 months ago (Dec. 1, 1989)
Published Online	20 years, 6 months ago (March 3, 2005)
Published Print	35 years, 9 months ago (Dec. 1, 1989)

Funders 0

None

BibTeX

@article{MEHTA_1989, title={Evolutionary relationships among aminotransferases: Tyrosine aminotransferase, histidinol‐phosphate aminotransferase, and aspartate aminotransferase are homologous proteins}, volume={186}, ISSN={1432-1033}, url={http://dx.doi.org/10.1111/j.1432-1033.1989.tb15202.x}, DOI={10.1111/j.1432-1033.1989.tb15202.x}, number={1–2}, journal={European Journal of Biochemistry}, publisher={Wiley}, author={MEHTA, Perdeep K. and HALE, Terence I. and CHRISTEN, Philipp}, year={1989}, month=dec, pages={249–253} }

JSON

{
  "indexed": {
    "date-parts": [
      [
        2025,
        8,
        5
      ]
    ],
    "date-time": "2025-08-05T12:57:16Z",
    "timestamp": 1754398636260
  },
  "reference-count": 39,
  "publisher": "Wiley",
  "issue": "1-2",
  "license": [
    {
      "start": {
        "date-parts": [
          [
            2005,
            3,
            3
          ]
        ],
        "date-time": "2005-03-03T00:00:00Z",
        "timestamp": 1109808000000
      },
      "content-version": "vor",
      "delay-in-days": 5571,
      "URL": "http://onlinelibrary.wiley.com/termsAndConditions#vor"
    }
  ],
  "content-domain": {
    "domain": [],
    "crossmark-restriction": false
  },
  "published-print": {
    "date-parts": [
      [
        1989,
        12
      ]
    ]
  },
  "abstract": "<jats:p>A data base was compiled containing the amino acid sequences of 12 aspartate aminotransferases and 11 other aminotransferases. A comparison of these sequences by a standard alignment method confirmed the previously reported homology of all aspartate aminotransferases and <jats:italic>Escherichia coli</jats:italic> tyrosine aminotransferase. However, no significant similarity between these proteins and any of the other aminotransferases was detected. A more rigorous analysis, focusing on short sequence segments rather than the total polypeptide chain, revealed that rat tyrosine aminotransferase and <jats:italic>Saccharomyces cerevisiae</jats:italic> and <jats:italic>Escherichia coli</jats:italic> histidinol\u2010phosphate aminotransferase share several homologous sequence segments with aspartate aminotransferases. For comparison of the complete sequences, a multiple sequence editor was developed to display the whole set of amino acid sequences in parallel on a single work\u2010sheet. The editor allows gaps in individual sequences or a set of sequences to be introduced and thus facilitates their parallel analysis and alignment. Several clusters of invariant residues at corresponding positions in the amino acid sequences became evident, clearly establishing that the cytosolic and the mitochondrial isoenzyme of vertebrate aspartate aminotransferase, <jats:italic>E. coli</jats:italic> aspartate aminotransferase, rat and <jats:italic>E. coli</jats:italic> tyrosine aminotransferase, and S. cerevisiae and <jats:italic>E. coli</jats:italic> histidinol\u2010phosphate aminotransferase are homologous proteins. Only 12 amino acid residues out of a total of about 400 proved to be invariant in all sequences compared; they are either involved in the binding of pyridoxal 5\u2032\u2010phosphate and the substrate, or appear to be essential for the conformation of the enzymes.</jats:p>",
  "DOI": "10.1111/j.1432-1033.1989.tb15202.x",
  "type": "journal-article",
  "created": {
    "date-parts": [
      [
        2005,
        3,
        4
      ]
    ],
    "date-time": "2005-03-04T04:05:19Z",
    "timestamp": 1109909119000
  },
  "page": "249-253",
  "source": "Crossref",
  "is-referenced-by-count": 113,
  "title": "Evolutionary relationships among aminotransferases",
  "prefix": "10.1111",
  "volume": "186",
  "author": [
    {
      "given": "Perdeep K.",
      "family": "MEHTA",
      "sequence": "first",
      "affiliation": []
    },
    {
      "given": "Terence I.",
      "family": "HALE",
      "sequence": "additional",
      "affiliation": []
    },
    {
      "given": "Philipp",
      "family": "CHRISTEN",
      "sequence": "additional",
      "affiliation": []
    }
  ],
  "member": "311",
  "published-online": {
    "date-parts": [
      [
        2005,
        3,
        3
      ]
    ]
  },
  "reference": [
    {
      "key": "e_1_2_3_2_2",
      "volume-title": "Transaminases",
      "author": "Christen P.",
      "year": "1985"
    },
    {
      "key": "e_1_2_3_3_2",
      "first-page": "123",
      "volume": "61",
      "author": "Christen P.",
      "year": "1989",
      "journal-title": "Nova Acta Leopold."
    },
    {
      "key": "e_1_2_3_4_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1042/bj2340593"
    },
    {
      "key": "e_1_2_3_5_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1016/S0021-9258(17)31222-X"
    },
    {
      "key": "e_1_2_3_6_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1016/S0021-9258(19)81634-4"
    },
    {
      "key": "e_1_2_3_7_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1111/j.1432-1033.1987.tb13597.x"
    },
    {
      "key": "e_1_2_3_8_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1016/S0021-9258(17)38826-9"
    },
    {
      "key": "e_1_2_3_9_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1073/pnas.83.5.1203"
    },
    {
      "key": "e_1_2_3_10_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1093/oxfordjournals.jbchem.a135176"
    },
    {
      "key": "e_1_2_3_11_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1042/bj2340049"
    },
    {
      "key": "e_1_2_3_12_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1016/S0021-9258(17)42677-9"
    },
    {
      "key": "e_1_2_3_13_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1126/science.2983426"
    },
    {
      "key": "e_1_2_3_14_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1016/0022-2836(70)90057-4"
    },
    {
      "key": "e_1_2_3_15_2",
      "first-page": "101",
      "volume-title": "Atlas of protein sequence and structure",
      "author": "Barker W. C.",
      "year": "1972"
    },
    {
      "key": "e_1_2_3_16_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1073/pnas.80.3.726"
    },
    {
      "key": "e_1_2_3_17_2",
      "doi-asserted-by": "crossref",
      "first-page": "8813",
      "DOI": "10.1016/S0021-9258(18)32129-X",
      "volume": "258",
      "author": "Graf\u2010Hausner U.",
      "year": "1983",
      "journal-title": "J. Biol. Chem."
    },
    {
      "key": "e_1_2_3_18_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1093/oxfordjournals.jbchem.a122464"
    },
    {
      "key": "e_1_2_3_19_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1016/0014-5793(73)80008-0"
    },
    {
      "key": "e_1_2_3_20_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1016/0014-5793(79)80537-2"
    },
    {
      "key": "e_1_2_3_21_2",
      "doi-asserted-by": "crossref",
      "first-page": "6153",
      "DOI": "10.1016/S0021-9258(18)43714-3",
      "volume": "255",
      "author": "Kagamiyama H.",
      "year": "1980",
      "journal-title": "J. Biol. Chem."
    },
    {
      "key": "e_1_2_3_22_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1007/BF02100642"
    },
    {
      "key": "e_1_2_3_23_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1007/978-3-0348-9308-4_7"
    },
    {
      "key": "e_1_2_3_24_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1093/oxfordjournals.jbchem.a133543"
    },
    {
      "key": "e_1_2_3_25_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1016/S0021-9258(19)75987-0"
    },
    {
      "key": "e_1_2_3_26_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1016/0167-4838(85)90172-4"
    },
    {
      "key": "e_1_2_3_27_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1093/oxfordjournals.jbchem.a135173"
    },
    {
      "key": "e_1_2_3_28_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1016/0022-2836(85)90386-9"
    },
    {
      "key": "e_1_2_3_29_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1007/BF00330437"
    },
    {
      "key": "e_1_2_3_30_2",
      "doi-asserted-by": "crossref",
      "first-page": "1317",
      "DOI": "10.1128/jb.164.3.1317-1323.1985",
      "volume": "164",
      "author": "Grisolia V.",
      "year": "1985",
      "journal-title": "J. Bacteriol."
    },
    {
      "key": "e_1_2_3_31_2",
      "author": "Martinez\u2010Carrion M.",
      "year": "1989",
      "journal-title": "Ann. NY Acad. Sci."
    },
    {
      "key": "e_1_2_3_32_2",
      "first-page": "187",
      "volume-title": "Active sites of enzymes",
      "author": "Jansonius J. N.",
      "year": "1987"
    },
    {
      "key": "e_1_2_3_33_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1073/pnas.77.5.2559"
    },
    {
      "key": "e_1_2_3_34_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1016/0022-2836(84)90333-4"
    },
    {
      "key": "e_1_2_3_35_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1073/pnas.71.10.3888"
    },
    {
      "key": "e_1_2_3_36_2",
      "doi-asserted-by": "crossref",
      "first-page": "6745",
      "DOI": "10.1016/S0021-9258(18)34493-4",
      "volume": "257",
      "author": "Sandmeier E.",
      "year": "1982",
      "journal-title": "J. Biol. Chem."
    },
    {
      "key": "e_1_2_3_37_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1101/SQB.1987.052.01.046"
    },
    {
      "key": "e_1_2_3_38_2",
      "first-page": "109",
      "volume-title": "Transaminases",
      "author": "Jansonius J. N.",
      "year": "1985"
    },
    {
      "key": "e_1_2_3_39_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1038/scientificamerican1085-88"
    },
    {
      "key": "e_1_2_3_40_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1093/oxfordjournals.jbchem.a122600"
    }
  ],
  "container-title": "European Journal of Biochemistry",
  "original-title": [],
  "language": "en",
  "link": [
    {
      "URL": "https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1111%2Fj.1432-1033.1989.tb15202.x",
      "content-type": "unspecified",
      "content-version": "vor",
      "intended-application": "text-mining"
    },
    {
      "URL": "https://febs.onlinelibrary.wiley.com/doi/pdf/10.1111/j.1432-1033.1989.tb15202.x",
      "content-type": "unspecified",
      "content-version": "vor",
      "intended-application": "similarity-checking"
    }
  ],
  "deposited": {
    "date-parts": [
      [
        2023,
        8,
        31
      ]
    ],
    "date-time": "2023-08-31T19:41:57Z",
    "timestamp": 1693510917000
  },
  "score": 1,
  "resource": {
    "primary": {
      "URL": "https://febs.onlinelibrary.wiley.com/doi/10.1111/j.1432-1033.1989.tb15202.x"
    }
  },
  "subtitle": [
    "Tyrosine aminotransferase, histidinol\u2010phosphate aminotransferase, and aspartate aminotransferase are homologous proteins"
  ],
  "short-title": [],
  "issued": {
    "date-parts": [
      [
        1989,
        12
      ]
    ]
  },
  "references-count": 39,
  "journal-issue": {
    "issue": "1-2",
    "published-print": {
      "date-parts": [
        [
          1989,
          12
        ]
      ]
    }
  },
  "alternative-id": [
    "10.1111/j.1432-1033.1989.tb15202.x"
  ],
  "URL": "http://dx.doi.org/10.1111/j.1432-1033.1989.tb15202.x",
  "relation": {},
  "ISSN": [
    "0014-2956",
    "1432-1033"
  ],
  "subject": [],
  "container-title-short": "European Journal of Biochemistry",
  "published": {
    "date-parts": [
      [
        1989,
        12
      ]
    ]
  }
}