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Difference between revisions of "Glycoside Hydrolase Family 42"

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<biblio>
 
<biblio>
 
#Kosugi2002 pmid=12446636
 
#Kosugi2002 pmid=12446636
#pmid=18068682
+
#DiLauro2008 pmid=18068682
 
#Ohtsu1998 pmid=9757561
 
#Ohtsu1998 pmid=9757561
 
#Kang2005 pmid=15748760
 
#Kang2005 pmid=15748760

Revision as of 06:18, 3 November 2009

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This page is currently under construction. This means that the Responsible Curator has deemed that the page's content is not quite up to CAZypedia's standards for full public consumption. All information should be considered to be under revision and may be subject to major changes.


Glycoside Hydrolase Family GH42
Clan GH-A
Mechanism retaining
Active site residues known
CAZy DB link
http://www.cazy.org/fam/GH42.html


Substrate specificities

Content is to be added here.

This is an example of how to make references to a journal article [1]. (See the References section below). Multiple references can go in the same place like this [2, 3]. You can even cite books using just the ISBN [4]. References that are not in PubMed can be typed in by hand [5].


Kinetics and Mechanism

Content is to be added here.


Catalytic Residues

Content is to be added here.


Three-dimensional structures

Content is to be added here.


Family Firsts

First sterochemistry determination
Cite some reference here, with a short (1-2 sentence) explanation [2].
First catalytic nucleophile identification
Cite some reference here, with a short (1-2 sentence) explanation [5].
First general acid/base residue identification
Cite some reference here, with a short (1-2 sentence) explanation [3].
First 3-D structure
Cite some reference here, with a short (1-2 sentence) explanation [4].

References

  1. Kosugi A, Murashima K, and Doi RH. (2002). Characterization of two noncellulosomal subunits, ArfA and BgaA, from Clostridium cellulovorans that cooperate with the cellulosome in plant cell wall degradation. J Bacteriol. 2002;184(24):6859-65. DOI:10.1128/JB.184.24.6859-6865.2002 | PubMed ID:12446636 [Kosugi2002]
  2. Di Lauro B, Strazzulli A, Perugino G, La Cara F, Bedini E, Corsaro MM, Rossi M, and Moracci M. (2008). Isolation and characterization of a new family 42 beta-galactosidase from the thermoacidophilic bacterium Alicyclobacillus acidocaldarius: identification of the active site residues. Biochim Biophys Acta. 2008;1784(2):292-301. DOI:10.1016/j.bbapap.2007.10.013 | PubMed ID:18068682 [DiLauro2008]
  3. Ohtsu N, Motoshima H, Goto K, Tsukasaki F, and Matsuzawa H. (1998). Thermostable beta-galactosidase from an extreme thermophile, Thermus sp. A4: enzyme purification and characterization, and gene cloning and sequencing. Biosci Biotechnol Biochem. 1998;62(8):1539-45. DOI:10.1271/bbb.62.1539 | PubMed ID:9757561 [Ohtsu1998]
  4. Kang SK, Cho KK, Ahn JK, Bok JD, Kang SH, Woo JH, Lee HG, You SK, and Choi YJ. (2005). Three forms of thermostable lactose-hydrolase from Thermus sp. IB-21: cloning, expression, and enzyme characterization. J Biotechnol. 2005;116(4):337-46. DOI:10.1016/j.jbiotec.2004.07.019 | PubMed ID:15748760 [Kang2005]
  5. Yuan T, Yang P, Wang Y, Meng K, Luo H, Zhang W, Wu N, Fan Y, and Yao B. (2008). Heterologous expression of a gene encoding a thermostable beta-galactosidase from Alicyclobacillus acidocaldarius. Biotechnol Lett. 2008;30(2):343-8. DOI:10.1007/s10529-007-9551-y | PubMed ID:17914606 [Yuan2008]
  6. Møller PL, Jørgensen F, Hansen OC, Madsen SM, and Stougaard P. (2001). Intra- and extracellular beta-galactosidases from Bifidobacterium bifidum and B. infantis: molecular cloning, heterologous expression, and comparative characterization. Appl Environ Microbiol. 2001;67(5):2276-83. DOI:10.1128/AEM.67.5.2276-2283.2001 | PubMed ID:11319112 [Moller2001]
  7. Van Laere KM, Abee T, Schols HA, Beldman G, and Voragen AG. (2000). Characterization of a novel beta-galactosidase from Bifidobacterium adolescentis DSM 20083 active towards transgalactooligosaccharides. Appl Environ Microbiol. 2000;66(4):1379-84. DOI:10.1128/AEM.66.4.1379-1384.2000 | PubMed ID:10742215 [VanLaere2000]
  8. Hinz SW, van den Brock LA, Beldman G, Vincken JP, and Voragen AG. (2004). beta-galactosidase from Bifidobacterium adolescentis DSM20083 prefers beta(1,4)-galactosides over lactose. Appl Microbiol Biotechnol. 2004;66(3):276-84. DOI:10.1007/s00253-004-1745-9 | PubMed ID:15480628 [Hinz2004]

All Medline abstracts: PubMed

[[Category:Glycoside Hydrolase Families|GHnnn]]