Difference between revisions of "Glycoside Hydrolase Family 36"

Revision as of 12:25, 27 May 2007

Glycoside Hydrolase Family GH36
Clan	GH-D
Mechanism	retaining
Active site residues	known
CAZy DB link
http://www.cazy.org/fam/GH36.html

Substrate specificities

Alpha-galactosidase and alpha-N-acetylgalactosaminidase activity has been demonstrated in archaeal, bacterial, and eukaryotic members of this family. Additionally, certain plant members of this family possess stachyose synthase or raffinose synthase activity.

Kinetics and Mechanism

Family GH36 alpha-galactosidases are anomeric configuration-retaining enzymes, as first shown by NMR studies on the alpha-galactosidase GalA from Thermotoga maritima [1]. Correspondingly, GH36 enzymes use a classical Koshland double-displacement mechanism [2], like their Glycoside Hydrolase Family GH27 (GH27) relatives in Clan GH-D.

Catalytic Residues

Three-dimensional structures

Family Firsts

First sterochemistry determination: Thermotoga maritima alpha-galactosidase, by NMR [1].
First catalytic nucleophile identification: Sulfolobus solfataricus alpha-galactosidase GalS, by sequence homology with GH27 enzymes and mutagenesis [3]. Subsequently confirmed in Thermotoga maritima alpha-galactosidase by structural homology, mutagenesis, and azide rescue [1].
First general acid/base residue identification: Sulfolobus solfataricus alpha-galactosidase GalS, by sequence homology with GH27 enzymes and mutagenesis [3]. Subsequently confirmed in Thermotoga maritima alpha-galactosidase by structural homology, mutagenesis, and azide rescue [1].
First 3-D structure: Thermotoga maritima alpha-galactosidase by X-ray crystallography. Coordinates (PDB 1zy9) deposited in 2005 as part of a high-throughput functional genomics project [4], first structural analysis reported in 2007 [1].

References

Error fetching PMID 12193646:
Error fetching PMID 16547025:

Comfort DA, Bobrov KS, Ivanen DR, Shabalin KA, Harris JM, Kulminskaya AA, Brumer H, and Kelly RM. (2007). Biochemical analysis of Thermotoga maritima GH36 alpha-galactosidase (TmGalA) confirms the mechanistic commonality of clan GH-D glycoside hydrolases. Biochemistry. 2007;46(11):3319-30. DOI:10.1021/bi061521n | PubMed ID:17323919 [1]
Sinnott, M.L. (1990) Catalytic mechanisms of enzymatic glycosyl transfer. Chem. Rev. 90, 1171-1202. DOI: 10.1021/cr00105a006
[4]
Error fetching PMID 16547025: [3]
Error fetching PMID 12193646: [2]

All Medline abstracts: PubMed

@@ Line 36: / Line 36: @@
 ;First catalytic nucleophile identification: ''Sulfolobus solfataricus'' alpha-galactosidase GalS, by sequence homology with GH27 enzymes and mutagenesis <cite>3</cite>.  Subsequently confirmed in ''Thermotoga maritima'' alpha-galactosidase by structural homology, mutagenesis, and azide rescue <cite>1</cite>.
 ;First general acid/base residue identification: ''Sulfolobus solfataricus'' alpha-galactosidase GalS, by sequence homology with GH27 enzymes and mutagenesis <cite>3</cite>.  Subsequently confirmed in ''Thermotoga maritima'' alpha-galactosidase by structural homology, mutagenesis, and azide rescue <cite>1</cite>.
-;First 3-D structure: ''Thermotoga maritima'' alpha-galactosidase.  Coordinates first reported as part of a high-throughput functional genomics project <cite>2</cite>, structural analysis reported in ref. <cite>1</cite>.
+;First 3-D structure: ''Thermotoga maritima'' alpha-galactosidase by X-ray crystallography.  Coordinates ([http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=1zy9 PDB 1zy9]) deposited in 2005 as part of a high-throughput functional genomics project <cite>2</cite>, first structural analysis reported in 2007 <cite>1</cite>.
 == References ==