EC |
2.4.1.67 |
Accepted name: |
galactinol—raffinose galactosyltransferase |
Reaction: |
α-D-galactosyl-(1→3)-1D-myo-inositol + raffinose = myo-inositol + stachyose |
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For diagram of stachyose biosynthesis, click here |
Glossary: |
raffinose = β-D-fructofuranosyl α-D-galactopyranosyl-(1→6)-α-D-glucopyranoside |
Other name(s): |
galactinol-raffinose galactosyltransferase; stachyose synthetase; α-D-galactosyl-(1→3)-myo-inositol:raffinose galactosyltransferase |
Systematic name: |
α-D-galactosyl-(1→3)-1D-myo-inositol:raffinose galactosyltransferase |
Comments: |
This enzyme also catalyses galactosyl transfer from stachyose to raffinose (shown by labelling) [4]. For synthesis of the substrate, see EC 2.4.1.123, inositol 3-α-galactosyltransferase. See also EC 2.4.1.82, galactinol—sucrose galactosyltransferase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37277-70-6 |
References: |
1. |
Tanner, W. Die Biosynthese der Stachyose. Ber. Dtsch. Bot. Ges. 80 (1967) 111. |
2. |
Tanner, W. and Kandler, O. Myo-inositol, a cofactor in the biosynthesis of stachyose. Eur. J. Biochem. 4 (1968) 233–239. [DOI] [PMID: 5655499] |
3. |
Lehle, L. and Tanner, W. The function of myo-inositol in the biosynthesis of raffinose. Purification and characterization of galactinol:sucrose 6-galactosyltransferase from Vicia faba seeds. Eur. J. Biochem. 38 (1973) 103–110. [DOI] [PMID: 4774118] |
4. |
Kandler, O. and Hopf, H. Occurrence, metabolism and function of oligosaccharides. In: Preiss, J. (Ed.), The Biochemistry of Plant, vol. 3, Academic Press, New York, 1980, pp. 221–270. |
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[EC 2.4.1.67 created 1972, modified 2003] |
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EC |
2.4.1.82 |
Accepted name: |
galactinol—sucrose galactosyltransferase |
Reaction: |
α-D-galactosyl-(1→3)-1D-myo-inositol + sucrose = myo-inositol + raffinose |
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For diagram of stachyose biosynthesis, click here |
Glossary: |
raffinose = β-D-fructofuranosyl α-D-galactopyranosyl-(1→6)-α-D-glucopyranoside |
Other name(s): |
1-α-D-galactosyl-myo-inositol:sucrose 6-α-D-galactosyltransferase; α-D-galactosyl-(1→3)-myo-inositol:sucrose 6-α-D-galactosyltransferase; raffinose synthase; RafS |
Systematic name: |
α-D-galactosyl-(1→3)-1D-myo-inositol:sucrose 6-α-D-galactosyltransferase |
Comments: |
4-Nitrophenyl α-D-galactopyranoside can also act as donor. The enzyme also catalyses an exchange reaction between raffinose and sucrose (cf. EC 2.4.1.123, inositol 3-α-galactosyltransferase). |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 62213-45-0 |
References: |
1. |
Lehle, L. and Tanner, W. The function of myo-inositol in the biosynthesis of raffinose. Purification and characterization of galactinol:sucrose 6-galactosyltransferase from Vicia faba seeds. Eur. J. Biochem. 38 (1973) 103–110. [DOI] [PMID: 4774118] |
2. |
Lehle, L., Tanner, W. and Kandler, O. Myo-inositol, a cofactor in the biosynthesis of raffinose. Hoppe-Seyler's Z. Physiol. Chem. 351 (1970) 1494–1498. [PMID: 5491608] |
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[EC 2.4.1.82 created 1976, modified 2003] |
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EC |
2.4.1.123 |
Accepted name: |
inositol 3-α-galactosyltransferase |
Reaction: |
UDP-α-D-galactose + myo-inositol = UDP + O-α-D-galactosyl-(1→3)-1D-myo-inositol |
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For diagram of stachyose biosynthesis, click here |
Glossary: |
O-α-D-galactosyl-(1→3)-1D-myo-inositol = galactinol |
Other name(s): |
UDP-D-galactose:inositol galactosyltransferase; UDP-galactose:myo-inositol 1-α-D-galactosyltransferase; UDPgalactose:myo-inositol 1-α-D-galactosyltransferase; galactinol synthase; inositol 1-α-galactosyltransferase; uridine diphosphogalactose-inositol galactosyltransferase; GolS; UDP-galactose:myo-inositol 3-α-D-galactosyltransferase |
Systematic name: |
UDP-α-D-galactose:myo-inositol 3-α-D-galactosyltransferase |
Comments: |
An enzyme from plants involved in the formation of raffinose and stachyose [cf. EC 2.4.1.67 (galactinol—raffinose galactosyltransferase) and EC 2.4.1.82 (galactinol—sucrose galactosyltransferase)]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 79955-89-8 |
References: |
1. |
Pharr, D.M., Sox, H.N., Locy, R.D. and Huber, S.C. Partial characterization of the galactinol forming enzyme from leaves of Cucumis sativus L. Plant Sci. Lett. 23 (1981) 25–33. |
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[EC 2.4.1.123 created 1984, modified 2003] |
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EC |
2.4.1.166 |
Accepted name: |
raffinose—raffinose α-galactosyltransferase |
Reaction: |
2 raffinose = 1F-α-D-galactosylraffinose + sucrose |
Glossary: |
raffinose = β-D-fructofuranosyl α-D-galactopyranosyl-(1→6)-α-D-glucopyranoside |
Other name(s): |
raffinose (raffinose donor) galactosyltransferase; raffinose:raffinose α-galactosyltransferase; raffinose—raffinose α-galactotransferase |
Systematic name: |
raffinose:raffinose α-D-galactosyltransferase |
Comments: |
The 3F position of raffinose can also act as galactosyl acceptor; the enzyme is involved in the accumulation of the tetrasaccharides lychnose and isolychnose in the leaves of Cerastium arvense and other plants of the family Caryophyllaceae during late autumn. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 93389-38-9 |
References: |
1. |
Hopf, H., Gruber, G., Zinn, A. and Kandler, O. Physiology and biosynthesis of lychnose in Cerastium arvense. Planta 162 (1984) 283–288. [PMID: 24253101] |
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[EC 2.4.1.166 created 1989] |
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EC
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3.6.3.18
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Transferred entry: | oligosaccharide-transporting ATPase. Now EC 7.5.2.2, ABC-type oligosaccharide transporter
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[EC 3.6.3.18 created 2000, deleted 2018] |
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EC |
7.5.2.2 |
Accepted name: |
ABC-type oligosaccharide transporter |
Reaction: |
ATP + H2O + oligosaccharide-[oligosaccharide-binding protein][side 1] = ADP + phosphate + oligosaccharide[side 2] + [oligosaccharide-binding protein][side 1] |
Other name(s): |
oligosaccharide-transporting ATPase |
Systematic name: |
ATP phosphohydrolase (ABC-type, oligosaccharide-importing) |
Comments: |
An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. The enzyme, found in bacteria, interacts with an extracytoplasmic substrate binding protein and mediates the import of lactose, melibiose and raffinose. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Higgins, C.F. ABC transporters: from microorganisms to man. Annu. Rev. Cell Biol. 8 (1992) 67–113. [DOI] [PMID: 1282354] |
2. |
Williams, S.G., Greenwood, J.A. and Jones, C.W. Molecular analysis of the lac operon encoding the binding-protein-dependent lactose transport system and β-galactosidase in Agrobacterium radiobacter. Mol. Microbiol. 6 (1992) 1755–1768. [DOI] [PMID: 1630315] |
3. |
Tam, R. and Saier, M.H., Jr. Structural, functional, and evolutionary relationships among extracellular solute-binding receptors of bacteria. Microbiol. Rev. 57 (1993) 320–346. [PMID: 8336670] |
4. |
Kuan, G., Dassa, E., Saurin, N., Hofnung, M. and Saier, M.H., Jr. Phylogenetic analyses of the ATP-binding constituents of bacterial extracytoplasmic receptor-dependent ABC-type nutrient uptake permeases. Res. Microbiol. 146 (1995) 271–278. [DOI] [PMID: 7569321] |
5. |
Saier, M.H., Jr. Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya. Adv. Microb. Physiol. 40 (1998) 81–136. [PMID: 9889977] |
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[EC 7.5.2.2 created 2000 as EC 3.6.3.18, transferred 2018 to EC 7.5.2.2] |
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