EC |
2.4.2.51 |
Accepted name: |
anthocyanidin 3-O-glucoside 2′′′-O-xylosyltransferase |
Reaction: |
UDP-α-D-xylose + an anthocyanidin 3-O-β-D-glucoside = UDP + an anthocyanidin 3-O-β-D-sambubioside |
|
For diagram of anthocyanidin sambubioside biosynthesis, click here |
Glossary: |
anthocyanidin 3-O-β-D-sambubioside = anthocyanidin 3-O-(β-D-xylosyl-(1→2)-β-D-glucoside)
|
Other name(s): |
uridine 5′-diphosphate-xylose:anthocyanidin 3-O-glucose-xylosyltransferase; UGT79B1 |
Systematic name: |
UDP-α-D-xylose:anthocyanidin-3-O-β-D-glucoside 2′′′-O-xylosyltransferase |
Comments: |
Isolated from the plants Matthiola incana (stock) [1] and Arabidopsis thaliana (mouse-eared cress) [2]. The enzyme has similar activity with the 3-glucosides of pelargonidin, cyanidin, delphinidin, quercetin and kaempferol as well as with cyanidin 3-O-rhamnosyl-(1→6)-glucoside and cyanidin 3-O-(6-acylglucoside). There is no activity with other UDP-sugars or with cyanidin 3,5-diglucoside. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Teusch, M. Uridine 5′-diphosphate-xylose:anthocyanidin 3-O-glucose-xylosyltransferase from petals of Matthiola incana R.Br. Planta 169 (1986) 559–563. [PMID: 24232765] |
2. |
Yonekura-Sakakibara, K., Fukushima, A., Nakabayashi, R., Hanada, K., Matsuda, F., Sugawara, S., Inoue, E., Kuromori, T., Ito, T., Shinozaki, K., Wangwattana, B., Yamazaki, M. and Saito, K. Two glycosyltransferases involved in anthocyanin modification delineated by transcriptome independent component analysis in Arabidopsis thaliana. Plant J. 69 (2012) 154–167. [DOI] [PMID: 21899608] |
|
[EC 2.4.2.51 created 2013] |
|
|
|
|
EC |
2.4.2.52 |
Accepted name: |
triphosphoribosyl-dephospho-CoA synthase |
Reaction: |
ATP + 3′-dephospho-CoA = 2′-(5-triphospho-α-D-ribosyl)-3′-dephospho-CoA + adenine |
|
For diagram of holo-citrate-lyase biosynthesis, click here |
Other name(s): |
2′-(5′′-triphosphoribosyl)-3-dephospho-CoA synthase; ATP:dephospho-CoA 5-triphosphoribosyl transferase; CitG; ATP:dephospho-CoA 5′-triphosphoribosyl transferase; MdcB; ATP:3-dephospho-CoA 5′′-triphosphoribosyltransferase; MadG |
Systematic name: |
ATP:3′-dephospho-CoA 5-triphospho-α-D-ribosyltransferase |
Comments: |
ATP cannot be replaced by GTP, CTP, UTP, ADP or AMP. The reaction involves the formation of a new α (1′′→2′) glycosidic bond between the two ribosyl moieties, with concomitant displacement of the adenine moiety of ATP [1,4]. The 2′-(5-triphosphoribosyl)-3′-dephospho-CoA produced can be transferred by EC 2.7.7.61, citrate lyase holo-[acyl-carrier protein] synthase, to the apo-acyl-carrier protein subunit (γ-subunit) of EC 4.1.3.6, citrate (pro-3S) lyase, thus converting it from an apo-enzyme into a holo-enzyme [1,3]. Alternatively, it can be transferred to the apo-ACP subunit of malonate decarboxylase by the action of EC 2.7.7.66, malonate decarboxylase holo-[acyl-carrier protein] synthase [4]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 313345-38-9 |
References: |
1. |
Schneider, K., Dimroth, P. and Bott, M. Biosynthesis of the prosthetic group of citrate lyase. Biochemistry 39 (2000) 9438–9450. [DOI] [PMID: 10924139] |
2. |
Schneider, K., Dimroth, P. and Bott, M. Identification of triphosphoribosyl-dephospho-CoA as precursor of the citrate lyase prosthetic group. FEBS Lett. 483 (2000) 165–168. [DOI] [PMID: 11042274] |
3. |
Schneider, K., Kästner, C.N., Meyer, M., Wessel, M., Dimroth, P. and Bott, M. Identification of a gene cluster in Klebsiella pneumoniae which includes citX, a gene required for biosynthesis of the citrate lyase prosthetic group. J. Bacteriol. 184 (2002) 2439–2446. [DOI] [PMID: 11948157] |
4. |
Hoenke, S., Wild, M.R. and Dimroth, P. Biosynthesis of triphosphoribosyl-dephospho-coenzyme A, the precursor of the prosthetic group of malonate decarboxylase. Biochemistry 39 (2000) 13223–13232. [DOI] [PMID: 11052675] |
|
[EC 2.4.2.52 created 2002 as EC 2.7.8.25, modified 2008, transferred 2013 to EC 2.4.2.52] |
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|
|
|
EC |
2.4.2.53 |
Accepted name: |
undecaprenyl-phosphate 4-deoxy-4-formamido-L-arabinose transferase |
Reaction: |
UDP-4-deoxy-4-formamido-β-L-arabinopyranose + ditrans,octacis-undecaprenyl phosphate = UDP + 4-deoxy-4-formamido-α-L-arabinopyranosyl ditrans,octacis-undecaprenyl phosphate |
|
For diagram of UDP-4-amino-4-deoxy-β-L-arabinose biosynthesis, click here |
Other name(s): |
undecaprenyl-phosphate Ara4FN transferase; Ara4FN transferase; polymyxin resistance protein PmrF; UDP-4-amino-4-deoxy-α-L-arabinose:ditrans,polycis-undecaprenyl phosphate 4-amino-4-deoxy-α-L-arabinosyltransferase |
Systematic name: |
UDP-4-amino-4-deoxy-α-L-arabinose:ditrans,octacis-undecaprenyl phosphate 4-amino-4-deoxy-α-L-arabinosyltransferase |
Comments: |
The enzyme shows no activity with UDP-4-amino-4-deoxy-β-L-arabinose. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Breazeale, S.D., Ribeiro, A.A. and Raetz, C.R. Oxidative decarboxylation of UDP-glucuronic acid in extracts of polymyxin-resistant Escherichia coli. Origin of lipid a species modified with 4-amino-4-deoxy-L-arabinose. J. Biol. Chem. 277 (2002) 2886–2896. [DOI] [PMID: 11706007] |
2. |
Breazeale, S.D., Ribeiro, A.A., McClerren, A.L. and Raetz, C.R.H. A formyltransferase required for polymyxin resistance in Escherichia coli and the modification of lipid A with 4-amino-4-deoxy-L-arabinose. Identification and function of UDP-4-deoxy-4-formamido-L-arabinose. J. Biol. Chem. 280 (2005) 14154–14167. [DOI] [PMID: 15695810] |
|
[EC 2.4.2.53 created 2010 as EC 2.7.8.30, modified 2011, transferred 2013 to EC 2.4.2.53] |
|
|
|
|
EC |
2.4.2.54 |
Accepted name: |
β-ribofuranosylphenol 5′-phosphate synthase |
Reaction: |
5-phospho-α-D-ribose 1-diphosphate + 4-hydroxybenzoate = 4-(β-D-ribofuranosyl)phenol 5′-phosphate + CO2 + diphosphate |
|
For diagram of methanopterin biosynthesis (part 2), click here |
Other name(s): |
β-RFAP synthase (incorrect); β-RFA-P synthase (incorrect); AF2089 (gene name); MJ1427 (gene name); β-ribofuranosylhydroxybenzene 5′-phosphate synthase; 4-(β-D-ribofuranosyl)aminobenzene 5′-phosphate synthase (incorrect); β-ribofuranosylaminobenzene 5′-phosphate synthase (incorrect); 5-phospho-α-D-ribose 1-diphosphate:4-aminobenzoate 5-phospho-β-D-ribofuranosyltransferase (decarboxylating) (incorrect) |
Systematic name: |
5-phospho-α-D-ribose-1-diphosphate:4-hydroxybenzoate 5-phospho-β-D-ribofuranosyltransferase (decarboxylating) |
Comments: |
The enzyme is involved in biosynthesis of tetrahydromethanopterin in archaea. It can utilize both 4-hydroxybenzoate and 4-aminobenzoate as substrates, but only the former is known to be produced by methanogenic archaea [4]. The activity is dependent on Mg2+ or Mn2+ [1]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Rasche, M.E. and White, R.H. Mechanism for the enzymatic formation of 4-(β-D-ribofuranosyl)aminobenzene 5′-phosphate during the biosynthesis of methanopterin. Biochemistry 37 (1998) 11343–11351. [DOI] [PMID: 9698382] |
2. |
Scott, J.W. and Rasche, M.E. Purification, overproduction, and partial characterization of β-RFAP synthase, a key enzyme in the methanopterin biosynthesis pathway. J. Bacteriol. 184 (2002) 4442–4448. [DOI] [PMID: 12142414] |
3. |
Dumitru, R.V. and Ragsdale, S.W. Mechanism of 4-(β-D-ribofuranosyl)aminobenzene 5′-phosphate synthase, a key enzyme in the methanopterin biosynthetic pathway. J. Biol. Chem. 279 (2004) 39389–39395. [DOI] [PMID: 15262968] |
4. |
White, R.H. The conversion of a phenol to an aniline occurs in the biochemical formation of the 1-(4-aminophenyl)-1-deoxy-D-ribitol moiety in methanopterin. Biochemistry 50 (2011) 6041–6052. [DOI] [PMID: 21634403] |
5. |
Bechard, M.E., Farahani, P., Greene, D., Pham, A., Orry, A. and Rasche, M.E. Purification, kinetic characterization, and site-directed mutagenesis of Methanothermobacter thermautotrophicus RFAP synthase produced in Escherichia coli. AIMS Microbiol 5 (2019) 186–204. [DOI] [PMID: 31663056] |
|
[EC 2.4.2.54 created 2013, modified 2014, modified 2015] |
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|
|
|
EC |
2.4.2.55 |
Accepted name: |
nicotinate D-ribonucleotide:phenol phospho-D-ribosyltransferase |
Reaction: |
nicotinate D-ribonucleotide + phenol = nicotinate + phenyl 5-phospho-α-D-ribofuranoside |
Other name(s): |
ArsAB |
Systematic name: |
nicotinate D-ribonucleotide:phenol phospho-D-ribosyltransferase |
Comments: |
The enzyme is involved in the biosynthesis of phenolic cobamides in the Gram-positive bacterium Sporomusa ovata. It can also transfer the phospho-D-ribosyl group to 4-methylphenol and 5,6-dimethylbenzimidazole. The related EC 2.4.2.21, nicotinate-nucleotide dimethylbenzimidazole phosphoribosyltransferase, also transfers the phospho-D-ribosyl group from nicotinate D-ribonucleotide to 5,6-dimethylbenzimidazole, but shows no activity with 4-methylphenol or phenol. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Chan, C.H. and Escalante-Semerena, J.C. ArsAB, a novel enzyme from Sporomusa ovata activates phenolic bases for adenosylcobamide biosynthesis. Mol. Microbiol. 81 (2011) 952–967. [DOI] [PMID: 21696461] |
|
[EC 2.4.2.55 created 2013] |
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|
|
EC |
2.4.2.56 |
Accepted name: |
kaempferol 3-O-xylosyltransferase |
Reaction: |
UDP-α-D-xylose + kaempferol = UDP + kaempferol 3-O-β-D-xyloside |
|
For diagram of kaempferol biosynthesis, click here |
Other name(s): |
F3XT; UDP-D-xylose:flavonol 3-O-xylosyltransferase; flavonol 3-O-xylosyltransferase |
Systematic name: |
UDP-α-D-xylose:kaempferol 3-O-D-xylosyltransferase |
Comments: |
The enzyme from the plant Euonymus alatus also catalyses the 3-O-D-xylosylation of other flavonols (e.g. quercetin, isorhamnetin, rhamnetin, myricetin, fisetin) with lower activity. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Ishikura, N. and Yang, Z.Q. UDP-D-xylose: flavonol 3-O-xylosyltransferase from young leaves of Euonymus alatus f. ciliato-dentatus. Z. Naturforsch. C: Biosci. 46 (1991) 1003–1010. |
|
[EC 2.4.2.56 created 2013] |
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|
|
|
EC |
2.4.2.57 |
Accepted name: |
AMP phosphorylase |
Reaction: |
(1) AMP + phosphate = adenine + α-D-ribose 1,5-bisphosphate (2) CMP + phosphate = cytosine + α-D-ribose 1,5-bisphosphate (3) UMP + phosphate = uracil + α-D-ribose 1,5-bisphosphate |
|
For diagram of AMP catabolism, click here |
Other name(s): |
AMPpase; nucleoside monophosphate phosphorylase; deoA (gene name) |
Systematic name: |
AMP:phosphate α-D-ribosyl 5′-phosphate-transferase |
Comments: |
The enzyme from archaea is involved in AMP metabolism and CO2 fixation through type III RubisCO enzymes. The activity with CMP and UMP requires activation by cAMP [2]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Sato, T., Atomi, H. and Imanaka, T. Archaeal type III RuBisCOs function in a pathway for AMP metabolism. Science 315 (2007) 1003–1006. [DOI] [PMID: 17303759] |
2. |
Aono, R., Sato, T., Yano, A., Yoshida, S., Nishitani, Y., Miki, K., Imanaka, T. and Atomi, H. Enzymatic characterization of AMP phosphorylase and ribose-1,5-bisphosphate isomerase functioning in an archaeal AMP metabolic pathway. J. Bacteriol. 194 (2012) 6847–6855. [DOI] [PMID: 23065974] |
3. |
Nishitani, Y., Aono, R., Nakamura, A., Sato, T., Atomi, H., Imanaka, T. and Miki, K. Structure analysis of archaeal AMP phosphorylase reveals two unique modes of dimerization. J. Mol. Biol. 425 (2013) 2709–2721. [DOI] [PMID: 23659790] |
|
[EC 2.4.2.57 created 2014] |
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|
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|
EC |
2.4.2.58 |
Accepted name: |
hydroxyproline O-arabinosyltransferase |
Reaction: |
UDP-β-L-arabinofuranose + [protein]-trans-4-hydroxy-L-proline = UDP + [protein]-trans-4-(β-L-arabinofuranosyl)oxy-L-proline |
Glossary: |
trans-4-hydroxy-L-proline = (2S,4R)-4-hydroxyproline = (4R)-4-hydroxy-L-proline |
Other name(s): |
HPAT |
Systematic name: |
UDP-β-L-arabinofuranose:[protein]-trans-4-hydroxy-L-proline L-arabinofuranosyl transferase (configuration-retaining) |
Comments: |
The enzyme, found in plants and mosses, catalyses the O-arabinosylation of hydroxyprolines in hydroxyproline-rich glycoproteins. The enzyme acts on the first hydroxyproline in the motif Val-hydroxyPro-hydroxyPro-Ser. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Ogawa-Ohnishi, M., Matsushita, W. and Matsubayashi, Y. Identification of three hydroxyproline O-arabinosyltransferases in Arabidopsis thaliana. Nat. Chem. Biol. 9 (2013) 726–730. [DOI] [PMID: 24036508] |
|
[EC 2.4.2.58 created 2016] |
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|
|
|
EC |
2.4.2.59 |
Accepted name: |
sulfide-dependent adenosine diphosphate thiazole synthase |
Reaction: |
NAD+ + glycine + sulfide = nicotinamide + ADP-5-ethyl-4-methylthiazole-2-carboxylate + 3 H2O |
Other name(s): |
Thi4 (ambiguous) |
Systematic name: |
NAD+:glycine ADP-D-ribosyltransferase (sulfide-adding) |
Comments: |
This iron dependent enzyme, found in most archaea, is involved in the biosynthesis of thiamine phosphate. The homologous enzyme from plants and fungi (EC 2.4.2.60, cysteine-dependent adenosine diphosphate thiazole synthase) uses an intrinsic cysteine as sulfur donor and, unlike the archaeal enzyme, is a single turn-over enzyme. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Zhang, X., Eser, B.E., Chanani, P.K., Begley, T.P. and Ealick, S.E. Structural basis for iron-mediated sulfur transfer in archael and yeast thiazole synthases. Biochemistry 55 (2016) 1826–1838. [DOI] [PMID: 26919468] |
2. |
Eser, B.E., Zhang, X., Chanani, P.K., Begley, T.P. and Ealick, S.E. From suicide enzyme to catalyst: the iron-dependent sulfide transfer in Methanococcus jannaschii thiamin thiazole biosynthesis. J. Am. Chem. Soc. 138 (2016) 3639–3642. [DOI] [PMID: 26928142] |
|
[EC 2.4.2.59 created 2018] |
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|
|
|
EC |
2.4.2.60 |
Accepted name: |
cysteine-dependent adenosine diphosphate thiazole synthase |
Reaction: |
NAD+ + glycine + [ADP-thiazole synthase]-L-cysteine = nicotinamide + ADP-5-ethyl-4-methylthiazole-2-carboxylate + [ADP-thiazole synthase]-dehydroalanine + 3 H2O |
Other name(s): |
THI4 (gene name) (ambiguous); THI1 (gene name); ADP-thiazole synthase |
Systematic name: |
NAD+:glycine ADP-D-ribosyltransferase (dehydroalanine-producing) |
Comments: |
This iron dependent enzyme, found in fungi, plants, and some archaea, is involved in the thiamine phosphate biosynthesis pathway. It is a single turn-over enzyme since the cysteine residue is not regenerated in vivo [3]. The homologous enzyme in archaea (EC 2.4.2.59, sulfide-dependent adenosine diphosphate thiazole synthase) uses sulfide as sulfur donor. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Godoi, P.H., Galhardo, R.S., Luche, D.D., Van Sluys, M.A., Menck, C.F. and Oliva, G. Structure of the thiazole biosynthetic enzyme THI1 from Arabidopsis thaliana. J. Biol. Chem. 281 (2006) 30957–30966. [DOI] [PMID: 16912043] |
2. |
Chatterjee, A., Abeydeera, N.D., Bale, S., Pai, P.J., Dorrestein, P.C., Russell, D.H., Ealick, S.E. and Begley, T.P. Saccharomyces cerevisiae THI4p is a suicide thiamine thiazole synthase. Nature 478 (2011) 542–546. [DOI] [PMID: 22031445] |
3. |
Zhang, X., Eser, B.E., Chanani, P.K., Begley, T.P. and Ealick, S.E. Structural basis for iron-mediated sulfur transfer in archael and yeast thiazole synthases. Biochemistry 55 (2016) 1826–1838. [DOI] [PMID: 26919468] |
4. |
Hwang, S., Cordova, B., Chavarria, N., Elbanna, D., McHugh, S., Rojas, J., Pfeiffer, F. and Maupin-Furlow, J.A. Conserved active site cysteine residue of archaeal THI4 homolog is essential for thiamine biosynthesis in Haloferax volcanii. BMC Microbiol. 14:260 (2014). [PMID: 25348237] |
|
[EC 2.4.2.60 created 2018] |
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|
EC |
2.4.2.61 |
Accepted name: |
α-dystroglycan β1,4-xylosyltransferase |
Reaction: |
UDP-α-D-xylose + 3-O-[Rib-ol-P-Rib-ol-P-3-β-D-GalNAc-(1→3)-β-D-GlcNAc-(1→4)-O-6-P-α-D-Man]-Ser/Thr-[protein] = UDP + 3-O-[β-D-Xyl-(1→4)-Rib-ol-P-Rib-ol-P-3-β-D-GalNAc-(1→3)-β-D-GlcNAc-(1→4)-O-6-P-α-D-Man]-Ser/Thr-[protein] |
Other name(s): |
TMEM5 (gene name) |
Systematic name: |
UDP-α-D-xylose:3-O-[Rib-ol-P-Rib-ol-P-3-β-D-GalNAc-(1→3)-β-D-GlcNAc-(1→4)-O-6-P-α-D-Man]-Ser/Thr-[protein] xylosyltransferase |
Comments: |
This eukaryotic enzyme catalyses a step in the biosynthesis of the glycan moiety of the membrane protein α-dystroglycan. It is specific for the second ribitol 5-phosphate in the nascent glycan chain as acceptor. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Vuillaumier-Barrot, S., Bouchet-Seraphin, C., Chelbi, M., Devisme, L., Quentin, S., Gazal, S., Laquerriere, A., Fallet-Bianco, C., Loget, P., Odent, S., Carles, D., Bazin, A., Aziza, J., Clemenson, A., Guimiot, F., Bonniere, M., Monnot, S., Bole-Feysot, C., Bernard, J.P., Loeuillet, L., Gonzales, M., Socha, K., Grandchamp, B., Attie-Bitach, T., Encha-Razavi, F. and Seta, N. Identification of mutations in TMEM5 and ISPD as a cause of severe cobblestone lissencephaly. Am. J. Hum. Genet. 91 (2012) 1135–1143. [PMID: 23217329] |
2. |
Manya, H., Yamaguchi, Y., Kanagawa, M., Kobayashi, K., Tajiri, M., Akasaka-Manya, K., Kawakami, H., Mizuno, M., Wada, Y., Toda, T. and Endo, T. The muscular dystrophy gene TMEM5 encodes a ribitol β1,4-xylosyltransferase required for the functional glycosylation of dystroglycan. J. Biol. Chem. 291 (2016) 24618–24627. [PMID: 27733679] |
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[EC 2.4.2.61 created 2018] |
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|
|
EC |
2.4.2.62 |
Accepted name: |
xylosyl α-1,3-xylosyltransferase |
Reaction: |
UDP-α-D-xylose + [protein with EGF-like domain]-3-O-[α-D-xylosyl-(1→3)-β-D-glucosyl]-L-serine = UDP + [protein with EGF-like domain]-3-O-[α-D-xylosyl-(1→3)-α-D-xylosyl-(1→3)-β-D-glucosyl]-L-serine |
Other name(s): |
XXYLT1 (gene name) |
Systematic name: |
UDP-α-D-xylose:[EGF-like domain protein]-3-O-[α-D-xylosyl-(1→3)-β-D-glucosyl]-L-serine 3-α-D-xylosyltransferase (configuration-retaining) |
Comments: |
The enzyme, found in animals and insects, is involved in the biosynthesis of the α-D-xylosyl-(1→3)-α-D-xylosyl-(1→3)-β-D-glucosyl trisaccharide on epidermal growth factor-like (EGF-like) domains. When present on Notch proteins, the trisaccharide functions as a modulator of the signalling activity of this protein. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Minamida, S., Aoki, K., Natsuka, S., Omichi, K., Fukase, K., Kusumoto, S. and Hase, S. Detection of UDP-D-xylose: α-D-xyloside α 1-→3xylosyltransferase activity in human hepatoma cell line HepG2. J. Biochem. 120 (1996) 1002–1006. [PMID: 8982869] |
2. |
Sethi, M.K., Buettner, F.F., Ashikov, A., Krylov, V.B., Takeuchi, H., Nifantiev, N.E., Haltiwanger, R.S., Gerardy-Schahn, R. and Bakker, H. Molecular cloning of a xylosyltransferase that transfers the second xylose to O-glucosylated epidermal growth factor repeats of notch. J. Biol. Chem. 287 (2012) 2739–2748. [PMID: 22117070] |
3. |
Yu, H., Takeuchi, M., LeBarron, J., Kantharia, J., London, E., Bakker, H., Haltiwanger, R.S., Li, H. and Takeuchi, H. Notch-modifying xylosyltransferase structures support an SNi-like retaining mechanism. Nat. Chem. Biol. 11 (2015) 847–854. [PMID: 26414444] |
|
[EC 2.4.2.62 created 2020] |
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|
|
EC |
2.4.2.63 |
Accepted name: |
EGF-domain serine xylosyltransferase |
Reaction: |
UDP-α-D-xylose + [protein with EGF-like domain]-L-serine = UDP + [protein with EGF-like domain]-3-O-(β-D-xylosyl)-L-serine |
Other name(s): |
POGLUT1 (gene name) (ambiguous); rumi (gene name) (ambiguous) |
Systematic name: |
UDP-α-D-xylose:[protein with EGF-like domain]-L-serine O-β-xylosyltransferase (configuration-inverting) |
Comments: |
The enzyme, found in animals and insects, xylosylates at the serine in the C-X-S-X-P-C motif of epidermal growth factor-like (EGF-like) domains. The enzyme is bifunctional also being active with UDP-α-glucose as donor (EC 2.4.1.376, EGF-domain serine glucosyltransferase). |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Li, Z., Fischer, M., Satkunarajah, M., Zhou, D., Withers, S.G. and Rini, J.M. Structural basis of Notch O-glucosylation and O-xylosylation by mammalian protein-O-glucosyltransferase 1 (POGLUT1). Nat. Commun. 8:185 (2017). [PMID: 28775322] |
|
[EC 2.4.2.63 created 2020] |
|
|
|
|
EC |
2.4.2.64 |
Accepted name: |
tRNA-guanosine34 queuine transglycosylase |
Reaction: |
guanine34 in tRNA + queuine = queuine34 in tRNA + guanine |
|
For diagram of queuine biosynthesis, click here |
Glossary: |
queuine = base Q = 2-amino-5-({[(1S,4S,5R)-4,5-dihydroxycyclopent-2-en-1-yl]amino}methyl)-1,7-dihydropyrrolo[3,2-e]pyrimidin-4-one |
Other name(s): |
QTRT1 (gene name); QTRT2 (gene name); TGT (ambiguous); guanine insertion enzyme (ambiguous); tRNA transglycosylase (ambiguous); Q-insertase (ambiguous); queuine34 transfer ribonucleate ribosyltransferase; transfer ribonucleate glycosyltransferase (ambiguous); tRNA guanine34 transglycosidase (ambiguous); queuine tRNA-ribosyltransferase; [tRNA]-guanine34:queuine tRNA-D-ribosyltransferase; transfer ribonucleic acid guanine34 transglycosylase (ambiguous) |
Systematic name: |
tRNA-guanosine34:queuine tRNA-D-ribosyltransferase |
Comments: |
Certain prokaryotic and eukaryotic tRNAs contain the modified base queuine at position 34. In eukaryotes and a small number of prokaryotes queuine is salvaged and incorporated into tRNA directly via a base-exchange reaction, replacing guanine. cf. EC 2.4.2.29, tRNA-guanosine34 preQ1 transglycosylase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 72162-89-1 |
References: |
1. |
Howes, N.K. and Farkas, W.R. Studies with a homogeneous enzyme from rabbit erythrocytes catalyzing the insertion of guanine into tRNA. J. Biol. Chem. 253 (1978) 9082–9087. [PMID: 721832] |
2. |
Shindo-Okada, N., Okada, N., Ohgi, T., Goto, T. and Nishimura, S. Transfer ribonucleic acid guanine transglycosylase isolated from rat liver. Biochemistry 19 (1980) 395–400. [DOI] [PMID: 6986171] |
3. |
Boland, C., Hayes, P., Santa-Maria, I., Nishimura, S. and Kelly, V.P. Queuosine formation in eukaryotic tRNA occurs via a mitochondria-localized heteromeric transglycosylase. J. Biol. Chem. 284 (2009) 18218–18227. [DOI] [PMID: 19414587] |
4. |
Yuan, Y., Zallot, R., Grove, T.L., Payan, D.J., Martin-Verstraete, I., Sepic, S., Balamkundu, S., Neelakandan, R., Gadi, V.K., Liu, C.F., Swairjo, M.A., Dedon, P.C., Almo, S.C., Gerlt, J.A. and de Crecy-Lagard, V. Discovery of novel bacterial queuine salvage enzymes and pathways in human pathogens. Proc. Natl. Acad. Sci. USA 116 (2019) 19126–19135. [DOI] [PMID: 31481610] |
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[EC 2.4.2.64 created 2020 (EC 2.4.2.29 created 1984, modified 2007, modified 2012, part transferred 2020 to EC 2.4.2.64)] |
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