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2.4.1.195

Accepted name:

N-hydroxythioamide S-β-glucosyltransferase

Reaction:

(1) UDP-α-D-glucose + (Z)-2-phenyl-1-thioacetohydroximate = UDP + desulfoglucotropeolin
(2) UDP-α-D-glucose + an (E)-ω-(methylsulfanyl)alkyl-thiohydroximate = UDP + an aliphatic desulfoglucosinolate
(3) UDP-α-D-glucose + (E)-2-(1H-indol-3-yl)-1-thioacetohydroximate = UDP + desulfoglucobrassicin

For diagram of glucotropeolin biosynthesis, click here

Glossary:

an aliphatic desulfoglucosinolate = an ω-(methylsulfanyl)alkylhydroximate S-glucoside

Other name(s):

UGT74B1 (gene name); desulfoglucosinolate-uridine diphosphate glucosyltransferase; uridine diphosphoglucose-thiohydroximate glucosyltransferase; thiohydroximate β-D-glucosyltransferase; UDPG:thiohydroximate glucosyltransferase; thiohydroximate S-glucosyltransferase; thiohydroximate glucosyltransferase; UDP-glucose:thiohydroximate S-β-D-glucosyltransferase; UDP-glucose:N-hydroxy-2-phenylethanethioamide S-β-D-glucosyltransferase

Systematic name:

UDP-α-D-glucose:N-hydroxy-2-phenylethanethioamide S-β-D-glucosyltransferase

Comments:

The enzyme specifically glucosylates the thiohydroximate functional group. It is involved in the biosynthesis of glucosinolates in cruciferous plants, and acts on aliphatic, aromatic, and indolic substrates.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9068-14-8

References:

1.	Jain, J.C., Reed, D.W., Groot Wassink, J.W.D. and Underhill, E.W. A radioassay of enzymes catalyzing the glucosylation and sulfation steps of glucosinolate biosynthesis in Brassica species. Anal. Biochem. 178 (1989) 137–140. [DOI] [PMID: 2524977]
2.	Reed, D.W., Davin, L., Jain, J.C., Deluca, V., Nelson, L. and Underhill, E.W. Purification and properties of UDP-glucose:thiohydroximate glucosyltransferase from Brassica napus L. seedlings. Arch. Biochem. Biophys. 305 (1993) 526–532. [DOI] [PMID: 8373190]
3.	Marillia, E.F., MacPherson, J.M., Tsang, E.W., Van Audenhove, K., Keller, W.A. and GrootWassink, J.W. Molecular cloning of a Brassica napus thiohydroximate S-glucosyltransferase gene and its expression in Escherichia coli. Physiol. Plant. 113 (2001) 176–184. [PMID: 12060294]
4.	Fahey, J.W., Zalcmann, A.T. and Talalay, P. The chemical diversity and distribution of glucosinolates and isothiocyanates among plants. Phytochemistry 56 (2001) 5–51. [DOI] [PMID: 11198818]
5.	Grubb, C.D., Zipp, B.J., Ludwig-Muller, J., Masuno, M.N., Molinski, T.F. and Abel, S. Arabidopsis glucosyltransferase UGT74B1 functions in glucosinolate biosynthesis and auxin homeostasis. Plant J. 40 (2004) 893–908. [DOI] [PMID: 15584955]

[EC 2.4.1.195 created 1992, modified 2006, modified 2018]

2.8.2.24

Accepted name:

aromatic desulfoglucosinolate sulfotransferase

Reaction:

(1) 3′-phosphoadenylyl sulfate + desulfoglucotropeolin = adenosine 3′,5′-bisphosphate + glucotropeolin
(2) 3′-phosphoadenylyl sulfate + indolylmethyl-desulfoglucosinolate = adenosine 3′,5′-bisphosphate + glucobrassicin

For diagram of glucotropeolin biosynthesis, click here

Glossary:

3′-phosphoadenylyl sulfate = PAPS

Other name(s):

desulfoglucosinolate sulfotransferase (ambiguous); PAPS-desulfoglucosinolate sulfotransferase (ambiguous); 3′-phosphoadenosine-5′-phosphosulfate:desulfoglucosinolate sulfotransferase (ambiguous); 3′-phosphoadenylyl-sulfate:aromatic desulfoglucosinolate sulfotransferase

Systematic name:

3′-phosphoadenylyl-sulfate:aromatic desulfoglucosinolate sulfonotransferase

Comments:

This enzyme, characterized from cruciferous plants, catalyses the last step in the biosynthesis of tryptophan- and phenylalanine-derived glucosinolates. cf. EC 2.8.2.38, aliphatic desulfoglucosinolate sulfotransferase.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 121479-85-4

References:

1.	Jain, J.C., Reed, D.W., Groot Wassink, J.W.D. and Underhill, E.W. A radioassay of enzymes catalyzing the glucosylation and sulfation steps of glucosinolate biosynthesis in Brassica species. Anal. Biochem. 178 (1989) 137–140. [DOI] [PMID: 2524977]
2.	Klein, M., Reichelt, M., Gershenzon, J. and Papenbrock, J. The three desulfoglucosinolate sulfotransferase proteins in Arabidopsis have different substrate specificities and are differentially expressed. FEBS J. 273 (2006) 122–136. [DOI] [PMID: 16367753]
3.	Klein, M. and Papenbrock, J. Kinetics and substrate specificities of desulfo-glucosinolate sulfotransferases in Arabidopsis thaliana. Physiol. Plant. 135 (2009) 140–149. [DOI] [PMID: 19077143]

[EC 2.8.2.24 created 1992, modified 2017]

2.8.2.38

Accepted name:

aliphatic desulfoglucosinolate sulfotransferase

Reaction:

3′-phosphoadenylyl sulfate + an aliphatic desulfoglucosinolate = adenosine 3′,5′-bisphosphate + an aliphatic glucosinolate

Other name(s):

SOT17 (gene name); SOT18 (gene name); 3′-phosphoadenylyl-sulfate:aliphatic desulfoglucosinolate sulfotransferase

Systematic name:

3′-phosphoadenylyl-sulfate:aliphatic desulfoglucosinolate sulfonotransferase

Comments:

The enzyme catalyses the last step in the biosynthesis of aliphatic glucosinolate core structures. cf. EC 2.8.2.24, aromatic desulfoglucosinolate sulfotransferase.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB

References:

1.	Piotrowski, M., Schemenewitz, A., Lopukhina, A., Muller, A., Janowitz, T., Weiler, E.W. and Oecking, C. Desulfoglucosinolate sulfotransferases from Arabidopsis thaliana catalyze the final step in the biosynthesis of the glucosinolate core structure. J. Biol. Chem. 279 (2004) 50717–50725. [DOI] [PMID: 15358770]
2.	Klein, M., Reichelt, M., Gershenzon, J. and Papenbrock, J. The three desulfoglucosinolate sulfotransferase proteins in Arabidopsis have different substrate specificities and are differentially expressed. FEBS J. 273 (2006) 122–136. [DOI] [PMID: 16367753]
3.	Klein, M. and Papenbrock, J. Kinetics and substrate specificities of desulfo-glucosinolate sulfotransferases in Arabidopsis thaliana. Physiol. Plant. 135 (2009) 140–149. [DOI] [PMID: 19077143]

[EC 2.8.2.38 created 2017]