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Difference between revisions of "Talk:Glycoside Hydrolase Family 3"
(Created page with "Litzinger et al. (2010) suggested that the acid/base catalyst of 2 domain NagZs (and also 1 domain NagZs) is an Asp-His dyad in the (β/α)<sub>8</sub> domain. pmid: 208...") |
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+ | == Comment from [[User:Brian Mark|Brian Mark]], April 2013 == | ||
+ | The GH3 page has received a comprehensive update. The following comments have been addressed. Thank-you for the input! | ||
+ | |||
+ | == Comment from [[User:Shinya Fushinobu|Shinya Fushinobu]], Sept. 2011 == | ||
Litzinger et al. (2010) suggested that the acid/base catalyst of 2 domain NagZs (and also 1 domain NagZs) is an Asp-His dyad in the (β/α)<sub>8</sub> domain. pmid: 20826810. | Litzinger et al. (2010) suggested that the acid/base catalyst of 2 domain NagZs (and also 1 domain NagZs) is an Asp-His dyad in the (β/α)<sub>8</sub> domain. pmid: 20826810. | ||
+ | |||
+ | == Update to Catalytic Residues section needed? == | ||
+ | Given the growing amount of information about the identity of the GH3 catalytic residues - and in particular the acid/base - in different enzymes/subfamilies, I wonder if a update of this section isn't needed? | ||
+ | |||
+ | Here are some key acid/base ID references <cite>Thongpoo2012 Bacik2012 Litzinger2010 Pozzo2010 Yoshida2010 Li2006 Paal2004 Chir2002 Li2002</cite>, one of which also confirms the catalytic nucleophile <cite>Paal2004</cite>. These references are nucleophile-specific studies <cite>Vocadlo2000 Dan2000</cite>: | ||
+ | |||
+ | === References === | ||
+ | <biblio> | ||
+ | #Thongpoo2012 pmid=23201198 // Subfamily 4, 3-D homology model, mutagenesis, kinetic analysis, pH profile, azide rescue | ||
+ | #Bacik2012 pmid=23177201 // 1-domain Nag, experimental structure, ligand complex, mobile loop bearing acid/base | ||
+ | #Litzinger2010 pmid=20826810 // 2-domain Nag, strucuture, mutagenesis, kinetic analysis, pH profile, azide rescue unsuccessful | ||
+ | #Pozzo2010 pmid=20138890 // Subfamily 5, experimental structure, complexes, reduced Km for mutant with PNP-Glc | ||
+ | #Yoshida2010 pmid=20662765 // Subfamily 5, experimental structure, product complex | ||
+ | #Li2006 pmid=16717412 //Nag - relevant? Appears to be mis-identification. | ||
+ | #Paal2004 pmid=14561218 //Subfamily 5, kinetic analysis, pH profile, azide rescue | ||
+ | #Chir2002 pmid=11978178 // Subfamily 5, Glu-473 labelled by N-bromoacetyl-beta-d-glucosylamine | ||
+ | #Li2002 pmid=11851422 //Subfamily 5, kinetic analysis, pH profile, azide rescue | ||
+ | #Vocadlo2000 pmid=10625486 | ||
+ | #Dan2000 pmid=10671536 | ||
+ | </biblio> | ||
+ | |||
+ | |||
+ | [[User:Harry Brumer|Harry Brumer]] ([[User talk:Harry Brumer|talk]]) 17:55, 14 December 2012 (PST) |
Latest revision as of 13:10, 18 December 2021
Comment from Brian Mark, April 2013
The GH3 page has received a comprehensive update. The following comments have been addressed. Thank-you for the input!
Comment from Shinya Fushinobu, Sept. 2011
Litzinger et al. (2010) suggested that the acid/base catalyst of 2 domain NagZs (and also 1 domain NagZs) is an Asp-His dyad in the (β/α)8 domain. pmid: 20826810.
Update to Catalytic Residues section needed?
Given the growing amount of information about the identity of the GH3 catalytic residues - and in particular the acid/base - in different enzymes/subfamilies, I wonder if a update of this section isn't needed?
Here are some key acid/base ID references [1, 2, 3, 4, 5, 6, 7, 8, 9], one of which also confirms the catalytic nucleophile [7]. These references are nucleophile-specific studies [10, 11]:
References
- Thongpoo P, McKee LS, Araújo AC, Kongsaeree PT, and Brumer H. (2013). Identification of the acid/base catalyst of a glycoside hydrolase family 3 (GH3) beta-glucosidase from Aspergillus niger ASKU28. Biochim Biophys Acta. 2013;1830(3):2739-49. DOI:10.1016/j.bbagen.2012.11.014 |
Subfamily 4, 3-D homology model, mutagenesis, kinetic analysis, pH profile, azide rescue
- Bacik JP, Whitworth GE, Stubbs KA, Vocadlo DJ, and Mark BL. (2012). Active site plasticity within the glycoside hydrolase NagZ underlies a dynamic mechanism of substrate distortion. Chem Biol. 2012;19(11):1471-82. DOI:10.1016/j.chembiol.2012.09.016 |
1-domain Nag, experimental structure, ligand complex, mobile loop bearing acid/base
- Litzinger S, Fischer S, Polzer P, Diederichs K, Welte W, and Mayer C. (2010). Structural and kinetic analysis of Bacillus subtilis N-acetylglucosaminidase reveals a unique Asp-His dyad mechanism. J Biol Chem. 2010;285(46):35675-84. DOI:10.1074/jbc.M110.131037 |
2-domain Nag, strucuture, mutagenesis, kinetic analysis, pH profile, azide rescue unsuccessful
- Pozzo T, Pasten JL, Karlsson EN, and Logan DT. (2010). Structural and functional analyses of beta-glucosidase 3B from Thermotoga neapolitana: a thermostable three-domain representative of glycoside hydrolase 3. J Mol Biol. 2010;397(3):724-39. DOI:10.1016/j.jmb.2010.01.072 |
Subfamily 5, experimental structure, complexes, reduced Km for mutant with PNP-Glc
- Yoshida E, Hidaka M, Fushinobu S, Koyanagi T, Minami H, Tamaki H, Kitaoka M, Katayama T, and Kumagai H. (2010). Role of a PA14 domain in determining substrate specificity of a glycoside hydrolase family 3 β-glucosidase from Kluyveromyces marxianus. Biochem J. 2010;431(1):39-49. DOI:10.1042/BJ20100351 |
Subfamily 5, experimental structure, product complex
- Li H, Zhao G, Miyake H, Umekawa H, Kimura T, Ohmiya K, and Sakka K. (2006). Identification of a catalytic residue of Clostridium paraputrificum N-acetyl-beta-D-glucosaminidase Nag3A by site-directed mutagenesis. Biosci Biotechnol Biochem. 2006;70(5):1127-33. DOI:10.1271/bbb.70.1127 |
Nag - relevant? Appears to be mis-identification.
- Paal K, Ito M, and Withers SG. (2004). Paenibacillus sp. TS12 glucosylceramidase: kinetic studies of a novel sub-family of family 3 glycosidases and identification of the catalytic residues. Biochem J. 2004;378(Pt 1):141-9. DOI:10.1042/BJ20031028 |
Subfamily 5, kinetic analysis, pH profile, azide rescue
- Chir J, Withers S, Wan CF, and Li YK. (2002). Identification of the two essential groups in the family 3 beta-glucosidase from Flavobacterium meningosepticum by labelling and tandem mass spectrometric analysis. Biochem J. 2002;365(Pt 3):857-63. DOI:10.1042/BJ20020186 |
Subfamily 5, Glu-473 labelled by N-bromoacetyl-beta-d-glucosylamine
- Li YK, Chir J, Tanaka S, and Chen FY. (2002). Identification of the general acid/base catalyst of a family 3 beta-glucosidase from Flavobacterium meningosepticum. Biochemistry. 2002;41(8):2751-9. DOI:10.1021/bi016049e |
Subfamily 5, kinetic analysis, pH profile, azide rescue
- Vocadlo DJ, Mayer C, He S, and Withers SG. (2000). Mechanism of action and identification of Asp242 as the catalytic nucleophile of Vibrio furnisii N-acetyl-beta-D-glucosaminidase using 2-acetamido-2-deoxy-5-fluoro-alpha-L-idopyranosyl fluoride. Biochemistry. 2000;39(1):117-26. DOI:10.1021/bi991958d |
- Dan S, Marton I, Dekel M, Bravdo BA, He S, Withers SG, and Shoseyov O. (2000). Cloning, expression, characterization, and nucleophile identification of family 3, Aspergillus niger beta-glucosidase. J Biol Chem. 2000;275(7):4973-80. DOI:10.1074/jbc.275.7.4973 |
Harry Brumer (talk) 17:55, 14 December 2012 (PST)