An Evolving Hierarchical Family Classification for Glycosyltransferases

Coutinho, Pedro M.; Deleury, Emeline; Davies, G.J.; Henrissat, Bernard

doi:10.1016/s0022-2836(03)00307-3

Cited by 1,027 publications

(853 citation statements)

References 49 publications

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“…These families are grouped into 14 clans or 'superfamilies' using the criteria of conservation of the protein fold, catalytic machinery and mechanism of glycosidic bond cleavage. A similar hierarchical classification exists for glycosyltransferases, with both the family and clan groupings predictive of functional and structural features of the members [39,40]. Although fold similarities between CBMs have been demonstrated, and the existence of superfamilies has been suggested [41,42], there are currently no formal 'super' groupings of the 39 CBM families.…”

Section: Fold Relationships Among Cbmsmentioning

confidence: 92%

Carbohydrate-binding modules: fine-tuning polysaccharide recognition

Boraston

Bolam

Gilbert

et al. 2004

Biochemical Journal

1,739

1,724

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The enzymic degradation of insoluble polysaccharides is one of the most important reactions on earth. Despite this, glycoside hydrolases attack such polysaccharides relatively inefficiently as their target glycosidic bonds are often inaccessible to the active site of the appropriate enzymes. In order to overcome these problems, many of the glycoside hydrolases that utilize insoluble substrates are modular, comprising catalytic modules appended to one or more non-catalytic CBMs (carbohydrate-binding modules). CBMs promote the association of the enzyme with the substrate. In view of the central role that CBMs play in the enzymic hydrolysis of plant structural and storage polysaccharides, the ligand specificity displayed by these protein modules and the mechanism by which they recognize their target carbohydrates have received considerable attention since their discovery almost 20 years ago. In the last few years, CBM research has harnessed structural, functional and bioinformatic approaches to elucidate the molecular determinants that drive CBM-carbohydrate recognition. The present review summarizes the impact structural biology has had on our understanding of the mechanisms by which CBMs bind to their target ligands.

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Section: Fold Relationships Among Cbmsmentioning

confidence: 92%

Carbohydrate-binding modules: fine-tuning polysaccharide recognition

Boraston

Bolam

Gilbert

et al. 2004

Biochemical Journal

1,739

1,724

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“…The near full-length cDNAs revealed that the HvCslF genes encode family GT2 glycosyl transferase enzymes (Coutinho et al, 2003; http://www.cazy.org/) with 810 to 947 amino acid residues. Amino acid sequence identity values range from 40% to 63% overall (Table I), although higher identity values are observed in some segments of the proteins (data not shown).…”

Section: Properties Of Proteins Encoded By the Hvcslf Genesmentioning

confidence: 99%

The Genetics and Transcriptional Profiles of the Cellulose Synthase-Like HvCslF Gene Family in Barley

Burton

Jobling²,

Harvey³

et al. 2008

Plant Physiol.

202

292

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“…The transfer of a sugar moiety from an activated donor to an acceptor molecule is generally catalysed by members of the superfamily of glycosyltransferases (GTs). The carbohydrate-active enzymes database (www.cazy.org) currently itemises 89 sequence-based families (Campbell et al 1997;Coutinho et al 2003) with over 20,000 entries. GTs belonging to Family 1 (UGTs) display a conserved amino acid motif near the C-terminus, use UDP-activated sugars (mainly UDP-glucose) as donors, and various types of low molecular-weight molecules as acceptors (Mackenzie et al 1997).…”

Section: Introductionmentioning

confidence: 99%

Recombinant expression and functional characterisation of regiospecific flavonoid glucosyltransferases from Hieracium pilosella L.

Witte

Moco

Vervoort

et al. 2009

Planta

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Five glucosyltransferases were cloned by RT-PCR ampliWcation using total RNA from Hieracium pilosella L. (Asteraceae) inXorescences as template. Expression was accomplished in Escherichia coli, and three of the HIS-tagged enzymes, UGT90A7, UGT95A1, and UGT72B11 were partially puriWed and functionally characterised as UDP-glucose:Xavonoid O-glucosyltransferases. Both UGT90A7 and UGT95A1 preferred luteolin as substrate, but possessed diVerent regiospeciWcity proWles. UGT95A1 established a new subgroup within the UGT family showing high regiospeciWcity towards the C-3Ј hydroxyl group of luteolin, while UGT90A7 primarily yielded the 4Ј-O-glucoside, but concomitantly catalysed also the formation of the 7-O-glucoside, which could account for this Xavones glucoside in H. pilosella Xower heads. Semi quantitative expression proWles revealed that UGT95A1 was expressed at all stages of inXorescence development as well as in leaf and stem tissue, whereas UGT90A7 transcript abundance was nearly limited to Xower tissue and started to develop with the pigmentation of closed buds. Other than these enzymes, UGT72B11 showed rather broad substrate acceptance, with highest activity towards Xavones and Xavonols which have not been reported from H. pilosella. As umbelliferone was also readily accepted, this enzyme could be involved in the glucosylation of coumarins and other metabolites.

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An Evolving Hierarchical Family Classification for Glycosyltransferases

Cited by 1,027 publications

References 49 publications

Carbohydrate-binding modules: fine-tuning polysaccharide recognition

Carbohydrate-binding modules: fine-tuning polysaccharide recognition

The Genetics and Transcriptional Profiles of the Cellulose Synthase-Like HvCslF Gene Family in Barley

Recombinant expression and functional characterisation of regiospecific flavonoid glucosyltransferases from Hieracium pilosella L.

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