Beta-galactosidase
Details
- Name
- Beta-galactosidase
- Synonyms
- 3.2.1.23
- Beta-gal
- Lactase
- Gene Name
- lacZ
- Organism
- Escherichia coli (strain K12)
- Amino acid sequence
>lcl|BSEQ0019112|Beta-galactosidase MTMITDSLAVVLQRRDWENPGVTQLNRLAAHPPFASWRNSEEARTDRPSQQLRSLNGEWR FAWFPAPEAVPESWLECDLPEADTVVVPSNWQMHGYDAPIYTNVTYPITVNPPFVPTENP TGCYSLTFNVDESWLQEGQTRIIFDGVNSAFHLWCNGRWVGYGQDSRLPSEFDLSAFLRA GENRLAVMVLRWSDGSYLEDQDMWRMSGIFRDVSLLHKPTTQISDFHVATRFNDDFSRAV LEAEVQMCGELRDYLRVTVSLWQGETQVASGTAPFGGEIIDERGGYADRVTLRLNVENPK LWSAEIPNLYRAVVELHTADGTLIEAEACDVGFREVRIENGLLLLNGKPLLIRGVNRHEH HPLHGQVMDEQTMVQDILLMKQNNFNAVRCSHYPNHPLWYTLCDRYGLYVVDEANIETHG MVPMNRLTDDPRWLPAMSERVTRMVQRDRNHPSVIIWSLGNESGHGANHDALYRWIKSVD PSRPVQYEGGGADTTATDIICPMYARVDEDQPFPAVPKWSIKKWLSLPGETRPLILCEYA HAMGNSLGGFAKYWQAFRQYPRLQGGFVWDWVDQSLIKYDENGNPWSAYGGDFGDTPNDR QFCMNGLVFADRTPHPALTEAKHQQQFFQFRLSGQTIEVTSEYLFRHSDNELLHWMVALD GKPLASGEVPLDVAPQGKQLIELPELPQPESAGQLWLTVRVVQPNATAWSEAGHISAWQQ WRLAENLSVTLPAASHAIPHLTTSEMDFCIELGNKRWQFNRQSGFLSQMWIGDKKQLLTP LRDQFTRAPLDNDIGVSEATRIDPNAWVERWKAAGHYQAEAALLQCTADTLADAVLITTA HAWQHQGKTLFISRKTYRIDGSGQMAITVDVEVASDTPHPARIGLNCQLAQVAERVNWLG LGPQENYPDRLTAACFDRWDLPLSDMYTPYVFPSENGLRCGTRELNYGPHQWRGDFQFNI SRYSQQQLMETSHRHLLHAEEGTWLNIDGFHMGIGGDDSWSPSVSAEFQLSAGRYHYQLV WCQK
- Number of residues
- 1024
- Molecular Weight
- 116482.045
- Theoretical pI
- 5.2
- GO Classification
- Functionsalkali metal ion binding / beta-galactosidase activity / carbohydrate binding / magnesium ion bindingProcesseslactose catabolic processComponentsbeta-galactosidase complex
- General Function
- Magnesium ion binding
- Specific Function
- Not Available
- Pfam Domain Function
- Transmembrane Regions
- Not Available
- Cellular Location
- Cytoplasmic
- Gene sequence
>lcl|BSEQ0019113|Beta-galactosidase (lacZ) ATGACCATGATTACGGATTCACTGGCCGTCGTTTTACAACGTCGTGACTGGGAAAACCCT GGCGTTACCCAACTTAATCGCCTTGCAGCACATCCCCCTTTCGCCAGCTGGCGTAATAGC GAAGAGGCCCGCACCGATCGCCCTTCCCAACAGTTGCGCAGCCTGAATGGCGAATGGCGC TTTGCCTGGTTTCCGGCACCAGAAGCGGTGCCGGAAAGCTGGCTGGAGTGCGATCTTCCT GAGGCCGATACTGTCGTCGTCCCCTCAAACTGGCAGATGCACGGTTACGATGCGCCCATC TACACCAACGTGACCTATCCCATTACGGTCAATCCGCCGTTTGTTCCCACGGAGAATCCG ACGGGTTGTTACTCGCTCACATTTAATGTTGATGAAAGCTGGCTACAGGAAGGCCAGACG CGAATTATTTTTGATGGCGTTAACTCGGCGTTTCATCTGTGGTGCAACGGGCGCTGGGTC GGTTACGGCCAGGACAGTCGTTTGCCGTCTGAATTTGACCTGAGCGCATTTTTACGCGCC GGAGAAAACCGCCTCGCGGTGATGGTGCTGCGCTGGAGTGACGGCAGTTATCTGGAAGAT CAGGATATGTGGCGGATGAGCGGCATTTTCCGTGACGTCTCGTTGCTGCATAAACCGACT ACACAAATCAGCGATTTCCATGTTGCCACTCGCTTTAATGATGATTTCAGCCGCGCTGTA CTGGAGGCTGAAGTTCAGATGTGCGGCGAGTTGCGTGACTACCTACGGGTAACAGTTTCT TTATGGCAGGGTGAAACGCAGGTCGCCAGCGGCACCGCGCCTTTCGGCGGTGAAATTATC GATGAGCGTGGTGGTTATGCCGATCGCGTCACACTACGTCTGAACGTCGAAAACCCGAAA CTGTGGAGCGCCGAAATCCCGAATCTCTATCGTGCGGTGGTTGAACTGCACACCGCCGAC GGCACGCTGATTGAAGCAGAAGCCTGCGATGTCGGTTTCCGCGAGGTGCGGATTGAAAAT GGTCTGCTGCTGCTGAACGGCAAGCCGTTGCTGATTCGAGGCGTTAACCGTCACGAGCAT CATCCTCTGCATGGTCAGGTCATGGATGAGCAGACGATGGTGCAGGATATCCTGCTGATG AAGCAGAACAACTTTAACGCCGTGCGCTGTTCGCATTATCCGAACCATCCGCTGTGGTAC ACGCTGTGCGACCGCTACGGCCTGTATGTGGTGGATGAAGCCAATATTGAAACCCACGGC ATGGTGCCAATGAATCGTCTGACCGATGATCCGCGCTGGCTACCGGCGATGAGCGAACGC GTAACGCGAATGGTGCAGCGCGATCGTAATCACCCGAGTGTGATCATCTGGTCGCTGGGG AATGAATCAGGCCACGGCGCTAATCACGACGCGCTGTATCGCTGGATCAAATCTGTCGAT CCTTCCCGCCCGGTGCAGTATGAAGGCGGCGGAGCCGACACCACGGCCACCGATATTATT TGCCCGATGTACGCGCGCGTGGATGAAGACCAGCCCTTCCCGGCTGTGCCGAAATGGTCC ATCAAAAAATGGCTTTCGCTACCTGGAGAGACGCGCCCGCTGATCCTTTGCGAATACGCC CACGCGATGGGTAACAGTCTTGGCGGTTTCGCTAAATACTGGCAGGCGTTTCGTCAGTAT CCCCGTTTACAGGGCGGCTTCGTCTGGGACTGGGTGGATCAGTCGCTGATTAAATATGAT GAAAACGGCAACCCGTGGTCGGCTTACGGCGGTGATTTTGGCGATACGCCGAACGATCGC CAGTTCTGTATGAACGGTCTGGTCTTTGCCGACCGCACGCCGCATCCAGCGCTGACGGAA GCAAAACACCAGCAGCAGTTTTTCCAGTTCCGTTTATCCGGGCAAACCATCGAAGTGACC AGCGAATACCTGTTCCGTCATAGCGATAACGAGCTCCTGCACTGGATGGTGGCGCTGGAT GGTAAGCCGCTGGCAAGCGGTGAAGTGCCTCTGGATGTCGCTCCACAAGGTAAACAGTTG ATTGAACTGCCTGAACTACCGCAGCCGGAGAGCGCCGGGCAACTCTGGCTCACAGTACGC GTAGTGCAACCGAACGCGACCGCATGGTCAGAAGCCGGGCACATCAGCGCCTGGCAGCAG TGGCGTCTGGCGGAAAACCTCAGTGTGACGCTCCCCGCCGCGTCCCACGCCATCCCGCAT CTGACCACCAGCGAAATGGATTTTTGCATCGAGCTGGGTAATAAGCGTTGGCAATTTAAC CGCCAGTCAGGCTTTCTTTCACAGATGTGGATTGGCGATAAAAAACAACTGCTGACGCCG CTGCGCGATCAGTTCACCCGTGCACCGCTGGATAACGACATTGGCGTAAGTGAAGCGACC CGCATTGACCCTAACGCCTGGGTCGAACGCTGGAAGGCGGCGGGCCATTACCAGGCCGAA GCAGCGTTGTTGCAGTGCACGGCAGATACACTTGCTGATGCGGTGCTGATTACGACCGCT CACGCGTGGCAGCATCAGGGGAAAACCTTATTTATCAGCCGGAAAACCTACCGGATTGAT GGTAGTGGTCAAATGGCGATTACCGTTGATGTTGAAGTGGCGAGCGATACACCGCATCCG GCGCGGATTGGCCTGAACTGCCAGCTGGCGCAGGTAGCAGAGCGGGTAAACTGGCTCGGA TTAGGGCCGCAAGAAAACTATCCCGACCGCCTTACTGCCGCCTGTTTTGACCGCTGGGAT CTGCCATTGTCAGACATGTATACCCCGTACGTCTTCCCGAGCGAAAACGGTCTGCGCTGC GGGACGCGCGAATTGAATTATGGCCCACACCAGTGGCGCGGCGACTTCCAGTTCAACATC AGCCGCTACAGTCAACAGCAACTGATGGAAACCAGCCATCGCCATCTGCTGCACGCGGAA GAAGGCACATGGCTGAATATCGACGGTTTCCATATGGGGATTGGTGGCGACGACTCCTGG AGCCCGTCAGTATCGGCGGAATTCCAGCTGAGCGCCGGTCGCTACCATTACCAGTTGGTC TGGTGTCAAAAATAA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P00722 UniProtKB Entry Name BGAL_ECOLI GenBank Protein ID 146577 GenBank Gene ID J01636 - General References
- Kalnins A, Otto K, Ruther U, Muller-Hill B: Sequence of the lacZ gene of Escherichia coli. EMBO J. 1983;2(4):593-7. [Article]
- Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [Article]
- Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [Article]
- Fowler AV, Zabin I: Amino acid sequence of beta-galactosidase. XI. Peptide ordering procedures and the complete sequence. J Biol Chem. 1978 Aug 10;253(15):5521-5. [Article]
- Calos MP, Miller JH: Molecular consequences of deletion formation mediated by the transposon Tn9. Nature. 1980 May 1;285(5759):38-41. [Article]
- Buchel DE, Gronenborn B, Muller-Hill B: Sequence of the lactose permease gene. Nature. 1980 Feb 7;283(5747):541-5. [Article]
- Jobe A, Bourgeois S: lac Repressor-operator interaction. VI. The natural inducer of the lac operon. J Mol Biol. 1972 Aug 28;69(3):397-408. [Article]
- Huber RE, Parfett C, Woulfe-Flanagan H, Thompson DJ: Interaction of divalent cations with beta-galactosidase (Escherichia coli). Biochemistry. 1979 Sep 18;18(19):4090-5. [Article]
- Fowler AV, Smith PJ: The active site regions of lacZ and ebg beta-galactosidases are homologous. J Biol Chem. 1983 Sep 10;258(17):10204-7. [Article]
- Herrchen M, Legler G: Identification of an essential carboxylate group at the active site of lacZ beta-galactosidase from Escherichia coli. Eur J Biochem. 1984 Feb 1;138(3):527-31. [Article]
- Gebler JC, Aebersold R, Withers SG: Glu-537, not Glu-461, is the nucleophile in the active site of (lac Z) beta-galactosidase from Escherichia coli. J Biol Chem. 1992 Jun 5;267(16):11126-30. [Article]
- Martinez-Bilbao M, Gaunt MT, Huber RE: E461H-beta-galactosidase (Escherichia coli): altered divalent metal specificity and slow but reversible metal inactivation. Biochemistry. 1995 Oct 17;34(41):13437-42. [Article]
- Roth NJ, Huber RE: The beta-galactosidase (Escherichia coli) reaction is partly facilitated by interactions of His-540 with the C6 hydroxyl of galactose. J Biol Chem. 1996 Jun 14;271(24):14296-301. [Article]
- VanBogelen RA, Abshire KZ, Moldover B, Olson ER, Neidhardt FC: Escherichia coli proteome analysis using the gene-protein database. Electrophoresis. 1997 Aug;18(8):1243-51. [Article]
- Roth NJ, Rob B, Huber RE: His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and helps to mediate catalysis. Biochemistry. 1998 Jul 14;37(28):10099-107. [Article]
- Huber RE, Hlede IY, Roth NJ, McKenzie KC, Ghumman KK: His-391 of beta-galactosidase (Escherichia coli) promotes catalyses by strong interactions with the transition state. Biochem Cell Biol. 2001;79(2):183-93. [Article]
- Huber RE, Hakda S, Cheng C, Cupples CG, Edwards RA: Trp-999 of beta-galactosidase (Escherichia coli) is a key residue for binding, catalysis, and synthesis of allolactose, the natural lac operon inducer. Biochemistry. 2003 Feb 18;42(6):1796-803. [Article]
- Xu J, McRae MA, Harron S, Rob B, Huber RE: A study of the relationships of interactions between Asp-201, Na+ or K+, and galactosyl C6 hydroxyl and their effects on binding and reactivity of beta-galactosidase. Biochem Cell Biol. 2004 Apr;82(2):275-84. [Article]
- Matthews BW: The structure of E. coli beta-galactosidase. C R Biol. 2005 Jun;328(6):549-56. [Article]
- Sutendra G, Wong S, Fraser ME, Huber RE: Beta-galactosidase (Escherichia coli) has a second catalytically important Mg2+ site. Biochem Biophys Res Commun. 2007 Jan 12;352(2):566-70. Epub 2006 Nov 20. [Article]
- Jacobson RH, Zhang XJ, DuBose RF, Matthews BW: Three-dimensional structure of beta-galactosidase from E. coli. Nature. 1994 Jun 30;369(6483):761-6. [Article]
- Juers DH, Jacobson RH, Wigley D, Zhang XJ, Huber RE, Tronrud DE, Matthews BW: High resolution refinement of beta-galactosidase in a new crystal form reveals multiple metal-binding sites and provides a structural basis for alpha-complementation. Protein Sci. 2000 Sep;9(9):1685-99. [Article]
- Juers DH, Heightman TD, Vasella A, McCarter JD, Mackenzie L, Withers SG, Matthews BW: A structural view of the action of Escherichia coli (lacZ) beta-galactosidase. Biochemistry. 2001 Dec 11;40(49):14781-94. [Article]
- Juers DH, Hakda S, Matthews BW, Huber RE: Structural basis for the altered activity of Gly794 variants of Escherichia coli beta-galactosidase. Biochemistry. 2003 Nov 25;42(46):13505-11. [Article]
Drug Relations
- Drug Relations
DrugBank ID Name Drug group Pharmacological action? Actions Details DB01862 Isopropyl beta-D-thiogalactopyranoside experimental unknown Details DB01885 D-Galctopyranosyl-1-On experimental unknown Details DB01920 1-O-[O-Nitrophenyl]-Beta-D-Galactopyranose experimental unknown Details DB02228 2-deoxy-2-fluoro-β-D-galactose experimental unknown Details DB02294 (5R,6S,7S,8S)-5-hydroxymethyl-6,7,8-trihydroxy-tetrazolo[1,5-A]piperidine experimental unknown Details DB02632 4-nitrophenyl-beta-D-galactoside experimental unknown Details DB04116 Allolactose experimental unknown Details DB04155 2-Fluoro-2-Deoxy-Beta-D-Galactopyranosyl-Beta-D-Glucopyranose experimental unknown Details DB04382 2-Deoxy-alpha-D-galactopyranose experimental unknown Details DB04465 Lactose approved, experimental, investigational unknown Details DB04530 S,S-(2-Hydroxyethyl)Thiocysteine experimental unknown Details DB13503 Tyrothricin approved unknown inhibitor Details