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| - | [[Image:1oqm.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:1oqm.png|left|200px]] |
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| | {{STRUCTURE_1oqm| PDB=1oqm | SCENE= }} | | {{STRUCTURE_1oqm| PDB=1oqm | SCENE= }} |
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| - | '''A 1:1 complex between alpha-lactalbumin and beta1,4-galactosyltransferase in the presence of UDP-N-acetyl-galactosamine'''
| + | ===A 1:1 complex between alpha-lactalbumin and beta1,4-galactosyltransferase in the presence of UDP-N-acetyl-galactosamine=== |
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| - | ==Overview==
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| - | beta1,4-Galactosyltransferase I (Gal-T1) normally transfers Gal from UDP-Gal to GlcNAc in the presence of Mn(2+) ion. In the presence of alpha-lactalbumin (LA), the Gal acceptor specificity is altered from GlcNAc to Glc. Gal-T1 also transfers GalNAc from UDP-GalNAc to GlcNAc, but with only approximately 0.1% of Gal-T activity. To understand this low GalNAc-transferase activity, we have carried out the crystal structure analysis of the Gal-T1.LA complex with UDP-GalNAc at 2.1-A resolution. The crystal structure reveals that the UDP-GalNAc binding to Gal-T1 is similar to the binding of UDP-Gal to Gal-T1, except for an additional hydrogen bond formed between the N-acetyl group of GalNAc moiety with the Tyr-289 side chain hydroxyl group. Elimination of this additional hydrogen bond by mutating Tyr-289 residue to Leu, Ile, or Asn enhances the GalNAc-transferase activity. Although all three mutants exhibit enhanced GalNAc-transferase activity, the mutant Y289L exhibits GalNAc-transferase activity that is nearly 100% of its Gal-T activity, even while completely retaining its Gal-T activity. The steady state kinetic analyses on the Leu-289 mutant indicate that the K(m) for GlcNAc has increased compared to the wild type. On the other hand, the catalytic constant (k(cat)) in the Gal-T reaction is comparable with the wild type, whereas it is 3-5-fold higher in the GalNAc-T reaction. Interestingly, in the presence of LA, these mutants also transfer GalNAc to Glc instead of to GlcNAc. The present study demonstrates that, in the Gal-T family, the Tyr-289/Phe-289 residue largely determines the sugar donor specificity.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_11916963}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 11916963 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_11916963}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Beta1,4-galactosyltransferase]] | | [[Category: Beta1,4-galactosyltransferase]] |
| | [[Category: Udp-galnac]] | | [[Category: Udp-galnac]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 04:09:53 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 07:35:55 2008'' |
Revision as of 04:36, 29 July 2008
Template:STRUCTURE 1oqm
A 1:1 complex between alpha-lactalbumin and beta1,4-galactosyltransferase in the presence of UDP-N-acetyl-galactosamine
Template:ABSTRACT PUBMED 11916963
About this Structure
1OQM is a Protein complex structure of sequences from Bos taurus and Mus musculus. This structure supersedes the now removed PDB entry 1l7w. Full crystallographic information is available from OCA.
Reference
Structure-based design of beta 1,4-galactosyltransferase I (beta 4Gal-T1) with equally efficient N-acetylgalactosaminyltransferase activity: point mutation broadens beta 4Gal-T1 donor specificity., Ramakrishnan B, Qasba PK, J Biol Chem. 2002 Jun 7;277(23):20833-9. Epub 2002 Mar 26. PMID:11916963
Page seeded by OCA on Tue Jul 29 07:35:55 2008
