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, PDB |
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, PDB, 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, PDB |
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, PDB |
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] |
|
|
|
|