Glycoside Hydrolase Family 42

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• Author: ^^^Marco Moracci^^^
• Responsible Curator: ^^^Marco Moracci^^^

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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

The best known enzymatic activity for glycoside hydrolases in this family, at the current time, is b-galactosidase (EC 3.2.1.23), however, other commonly found activities are a-L-arabinosidase (EC 3.2.1.55) and b-D-fucosidase (EC 3.2.1.38) with both K_m and k_cat in the same order of magnitude for the different substrates [1, 2]. Apparently, these enzymes show strict specificity for axial C4-OH groups.

Interestingly, Family GH42 enzymes have been identified only in unicellular organisms, mainly from prokaryotes (in majority bacteria), and with few examples from archaea and fungi. GH42 enzymes are active on lactose [2, 3, 4, 5] and transgalactosylation was also observed with production of galactooligosaccharides [6]. However, several GH42 enzymes are extracted from diverse habitats where lactose would not be present and they are very active on galactooligosaccharides and galactans [1, 7, 8, 9], suggested that these enzymes would be involved in vivo in plant degradation. This function would be performed in cooperation with family GH53 galactanases, often encoded from genes adjacent to GH42 genes [9], and with cellulosome [1].

However, the activity of GH42 enzymes on lactose and also lactulose [2] has interesting applicative potential for the removal of the former from dairy products and to monitor lactulose concentration during heat treatment leading to UHT milk.

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 [3, 4]. You can even cite books using just the ISBN [5]. References that are not in PubMed can be typed in by hand [6].

Kinetics and Mechanism

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Catalytic Residues

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Three-dimensional structures

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Family Firsts

First sterochemistry determination

Cite some reference here, with a short (1-2 sentence) explanation [3].

First catalytic nucleophile identification

Cite some reference here, with a short (1-2 sentence) explanation [6].

First general acid/base residue identification

Cite some reference here, with a short (1-2 sentence) explanation [4].

First 3-D structure

Cite some reference here, with a short (1-2 sentence) explanation [5].

References

5. 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 |
7. 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 |
8. 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 |
9. 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 |
10. 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 |
11. 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 |
12. 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 |
13. 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 |
14. Shipkowski S and Brenchley JE. (2006). Bioinformatic, genetic, and biochemical evidence that some glycoside hydrolase family 42 beta-galactosidases are arabinogalactan type I oligomer hydrolases. Appl Environ Microbiol. 2006;72(12):7730-8. DOI:10.1128/AEM.01306-06 |
15. Hidaka M, Fushinobu S, Ohtsu N, Motoshima H, Matsuzawa H, Shoun H, and Wakagi T. (2002). Trimeric crystal structure of the glycoside hydrolase family 42 beta-galactosidase from Thermus thermophilus A4 and the structure of its complex with galactose. J Mol Biol. 2002;322(1):79-91. DOI:10.1016/s0022-2836(02)00746-5 |
16. Shaikh FA, Müllegger J, He S, and Withers SG. (2007). Identification of the catalytic nucleophile in Family 42 beta-galactosidases by intermediate trapping and peptide mapping: YesZ from Bacillus subtilis. FEBS Lett. 2007;581(13):2441-6. DOI:10.1016/j.febslet.2007.04.053 |

[[Category:Glycoside Hydrolase Families|GHnnn]]