The Enzyme Database

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EC 2.3.1.98     
Accepted name: chlorogenate—glucarate O-hydroxycinnamoyltransferase
Reaction: chlorogenate + glucarate = quinate + 2-O-caffeoylglucarate
Other name(s): chlorogenate:glucarate caffeoyltransferase; chlorogenic acid:glucaric acid O-caffeoyltransferase; chlorogenate:glucarate caffeoyltransferase
Systematic name: chlorogenate:glucarate O-(hydroxycinnamoyl)transferase
Comments: Galactarate can act as acceptor, more slowly. Involved with EC 2.3.1.99 quinate O-hydroxycinnamoyltransferase in the formation of caffeoylglucarate in tomato.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 126124-92-3
References:
1.  Strack, D. and Gross, W. Properties and activity changes of chlorogenic acid - glucaric acid caffeoyltransferase from tomato (Lycopersicon esculentum). Plant Physiol. 92 (1990) 41–47. [PMID: 16667263]
2.  Strack, D., Gross, W., Wray, V. and Grotjahn, L. Enzymatic-synthesis of caffeoylglucaric acid from chlorogenic acid and glucaric acid by a protein preparation from tomato cotyledons. Plant Physiol. 83 (1987) 475–478. [PMID: 16665274]
[EC 2.3.1.98 created 1989, modified 1990]
 
 
EC 2.3.1.130     
Accepted name: galactarate O-hydroxycinnamoyltransferase
Reaction: feruloyl-CoA + galactarate = CoA + O-feruloylgalactarate
Other name(s): galacturate hydroxycinnamoyltransferase
Systematic name: feruloyl-CoA:galactarate O-(hydroxycinnamoyl)transferase
Comments: Sinapoyl-CoA and 4-coumaroyl-CoA can also act as donors.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 112956-50-0
References:
1.  Strack, D., Keller, H. and Weissenböck, G. Enzymatic-synthesis of hydroxycinnamic acid-esters of sugar acids and hydroaromatic acids by protein preparations from rye (Secale cereale) primary leaves. J. Plant Physiol. 131 (1987) 61–73.
[EC 2.3.1.130 created 1990]
 
 
EC 2.7.1.165     
Accepted name: glycerate 2-kinase
Reaction: ATP + D-glycerate = ADP + 2-phospho-D-glycerate
For diagram of the Entner-Doudoroff pathway, click here
Other name(s): D-glycerate-2-kinase; glycerate kinase (2-phosphoglycerate forming); ATP:(R)-glycerate 2-phosphotransferase
Systematic name: ATP:D-glycerate 2-phosphotransferase
Comments: A key enzyme in the nonphosphorylative Entner-Doudoroff pathway in archaea [1,2]. In the bacterium Hyphomicrobium methylovorum GM2 the enzyme is involved in formaldehyde assimilation I (serine pathway) [5]. In Escherichia coli the enzyme is involved in D-glucarate/D-galactarate degradation [6]. The enzyme requires a divalent metal ion [1].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Liu, B., Wu, L., Liu, T., Hong, Y., Shen, Y. and Ni, J. A MOFRL family glycerate kinase from the thermophilic crenarchaeon, Sulfolobus tokodaii, with unique enzymatic properties. Biotechnol. Lett. 31 (2009) 1937–1941. [DOI] [PMID: 19690808]
2.  Reher, M., Bott, M. and Schonheit, P. Characterization of glycerate kinase (2-phosphoglycerate forming), a key enzyme of the nonphosphorylative Entner-Doudoroff pathway, from the thermoacidophilic euryarchaeon Picrophilus torridus. FEMS Microbiol. Lett. 259 (2006) 113–119. [DOI] [PMID: 16684110]
3.  Liu, B., Hong, Y., Wu, L., Li, Z., Ni, J., Sheng, D. and Shen, Y. A unique highly thermostable 2-phosphoglycerate forming glycerate kinase from the hyperthermophilic archaeon Pyrococcus horikoshii: gene cloning, expression and characterization. Extremophiles 11 (2007) 733–739. [DOI] [PMID: 17563835]
4.  Noh, M., Jung, J.H. and Lee, S.B. Purification and characterization of glycerate kinase from the thermoacidophilic archaeon Thermoplasma acidophilum: an enzyme belonging to the second glycerate kinase family. Biotechnol. Bioprocess Eng. 11 (2006) 344–350.
5.  Yoshida, T., Fukuta, K., Mitsunaga, T., Yamada, H. and Izumi, Y. Purification and characterization of glycerate kinase from a serine-producing methylotroph, Hyphomicrobium methylovorum GM2. Eur. J. Biochem. 210 (1992) 849–854. [DOI] [PMID: 1336459]
6.  Hubbard, B.K., Koch, M., Palmer, D.R., Babbitt, P.C. and Gerlt, J.A. Evolution of enzymatic activities in the enolase superfamily: characterization of the (D)-glucarate/galactarate catabolic pathway in Escherichia coli. Biochemistry 37 (1998) 14369–14375. [DOI] [PMID: 9772162]
[EC 2.7.1.165 created 2010]
 
 
EC 4.2.1.42     
Accepted name: galactarate dehydratase
Reaction: galactarate = (2R,3S)-2,3-dihydroxy-5-oxohexanedioate + H2O
Glossary: galactarate = (2R,3S,4R,5S)-2,3,4,5-tetrahydroxyhexanedioate
(2R,3S)-2,3-dihydroxy-5-oxohexanedioate = 3-deoxy-L-threo-hex-2-ulosarate
Other name(s): D-galactarate hydro-lyase; D-galactarate hydro-lyase (5-dehydro-4-deoxy-D-glucarate-forming); talrD (gene name)/galrD (gene name); galactarate dehydratase (L-threo-forming)
Systematic name: galactarate hydro-lyase (5-dehydro-4-deoxy-D-glucarate-forming)
Comments: The enzyme from the bacterium Escherichia coli is specific for galactarate [2], while the enzyme from Salmonella typhimurium also has activity with L-talarate (cf. EC 4.2.1.156, L-talarate dehydratase) [3]. cf. EC 4.2.1.158, galactarate dehydratase (D-threo-forming).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37290-78-1
References:
1.  Blumenthal, H.J. and Jepson, T. Galactarate dehydrase. Methods Enzymol. 9 (1966) 665–669.
2.  Hubbard, B.K., Koch, M., Palmer, D.R., Babbitt, P.C. and Gerlt, J.A. Evolution of enzymatic activities in the enolase superfamily: characterization of the (D)-glucarate/galactarate catabolic pathway in Escherichia coli. Biochemistry 37 (1998) 14369–14375. [DOI] [PMID: 9772162]
3.  Yew, W.S., Fedorov, A.A., Fedorov, E.V., Almo, S.C. and Gerlt, J.A. Evolution of enzymatic activities in the enolase superfamily: L-talarate/galactarate dehydratase from Salmonella typhimurium LT2. Biochemistry 46 (2007) 9564–9577. [DOI] [PMID: 17649980]
4.  Rakus, J.F., Kalyanaraman, C., Fedorov, A.A., Fedorov, E.V., Mills-Groninger, F.P., Toro, R., Bonanno, J., Bain, K., Sauder, J.M., Burley, S.K., Almo, S.C., Jacobson, M.P. and Gerlt, J.A. Computation-facilitated assignment of the function in the enolase superfamily: a regiochemically distinct galactarate dehydratase from Oceanobacillus iheyensis. Biochemistry 48 (2009) 11546–11558. [DOI] [PMID: 19883118]
[EC 4.2.1.42 created 1972, modified 2015]
 
 
EC 4.2.1.156     
Accepted name: L-talarate dehydratase
Reaction: L-altarate = 5-dehydro-4-deoxy-D-glucarate + H2O
Glossary: L-altrarate = L-talarate = (2R,3R,4S,5R)-2,3,4,5-tetrahydroxyhexanedioate
Other name(s): L-talarate hydro-lyase
Systematic name: L-altarate hydro-lyase (5-dehydro-4-deoxy-D-glucarate-forming)
Comments: Requires Mg2+. The enzyme, isolated from the bacteria Salmonella typhimurium and Polaromonas sp. JS666, also has activity with galactarate (cf. EC 4.2.1.42, galactarate dehydratase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Yew, W.S., Fedorov, A.A., Fedorov, E.V., Almo, S.C. and Gerlt, J.A. Evolution of enzymatic activities in the enolase superfamily: L-talarate/galactarate dehydratase from Salmonella typhimurium LT2. Biochemistry 46 (2007) 9564–9577. [DOI] [PMID: 17649980]
[EC 4.2.1.156 created 2015]
 
 
EC 4.2.1.158     
Accepted name: galactarate dehydratase (D-threo-forming)
Reaction: galactarate = (2S,3R)-2,3-dihydroxy-5-oxohexanedioate + H2O
Glossary: galactarate = (2R,3S,4R,5S)-2,3,4,5-tetrahydroxyhexanedioate
(2S,3R)-2,3-dihydroxy-5-oxohexanedioate = 3-deoxy-D-threo-hex-2-ulosarate
Systematic name: galactarate hydro-lyase (3-deoxy-D-threo-hex-2-ulosarate-forming)
Comments: The enzyme has been characterized from the bacterium Oceanobacillus iheyensis. cf. EC 4.2.1.42, galactarate dehydratase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Rakus, J.F., Kalyanaraman, C., Fedorov, A.A., Fedorov, E.V., Mills-Groninger, F.P., Toro, R., Bonanno, J., Bain, K., Sauder, J.M., Burley, S.K., Almo, S.C., Jacobson, M.P. and Gerlt, J.A. Computation-facilitated assignment of the function in the enolase superfamily: a regiochemically distinct galactarate dehydratase from Oceanobacillus iheyensis. Biochemistry 48 (2009) 11546–11558. [DOI] [PMID: 19883118]
[EC 4.2.1.158 created 2015]
 
 


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