Member database | CDD |
CDD type | domain |
Short name | LKR_SDH_like |
Set | NADB_Rossmann |
Description
References
1.LKR/SDH plays important roles throughout the tick life cycle including a long starvation period. Battur B, Boldbaatar D, Umemiya-Shirafuji R, Liao M, Battsetseg B, Taylor D, Baymbaa B, Fujisaki K. PLoS One 4, e7136, (2009). PMID: 19774086
2.Lysine degradation through the saccharopine pathway in mammals: involvement of both bifunctional and monofunctional lysine-degrading enzymes in mouse. Papes F, Kemper EL, Cord-Neto G, Langone F, Arruda P. Biochem J 344 Pt 2, 555-63, (1999). PMID: 10567240
3.Structure and regulation of the bifunctional enzyme lysine-oxoglutarate reductase-saccharopine dehydrogenase in maize. Kemper EL, Cord-Neto G, Capella AN, Goncalves-Butruile M, Azevedo RA, Arruda P. Eur. J. Biochem. 253, 720-9, (1998). View articlePMID: 9654071
4.Purification and characterization of alanine dehydrogenase from a cyanobacterium, Phormidium lapideum. Sawa Y, Tani M, Murata K, Shibata H, Ochiai H. J Biochem 116, 995-1000, (1994). PMID: 7896761
5.Evidence in support of lysine 77 and histidine 96 as acid-base catalytic residues in saccharopine dehydrogenase from Saccharomyces cerevisiae. Kumar VP, Thomas LM, Bobyk KD, Andi B, Cook PF, West AH. Biochemistry 51, 857-66, (2012). View articlePMID: 22243403
6.The activity of the Arabidopsis bifunctional lysine-ketoglutarate reductase/saccharopine dehydrogenase enzyme of lysine catabolism is regulated by functional interaction between its two enzyme domains. Zhu X, Tang G, Galili G. J Biol Chem 277, 49655-61, (2002). PMID: 12393892
7.Interdomain communications in bifunctional enzymes: how are different activities coordinated? Nagradova N. IUBMB Life 55, 459-66, (2003). View articlePMID: 14609201
8.Analysis of the structure and substrate binding of Phormidium lapideum alanine dehydrogenase. Baker PJ, Sawa Y, Shibata H, Sedelnikova SE, Rice DW. Nat. Struct. Biol. 5, 561-7, (1998). View articlePMID: 9665169
9.Crystal structures of ligand-bound saccharopine dehydrogenase from Saccharomyces cerevisiae. Andi B, Xu H, Cook PF, West AH. Biochemistry 46, 12512-21, (2007). View articlePMID: 17939687
10.Lysine catabolism, an effective versatile regulator of lysine level in plants. Stepansky A, Less H, Angelovici R, Aharon R, Zhu X, Galili G. Amino Acids 30, 121-5, (2006). PMID: 16525756
11.Lysine-ketoglutarate reductase and saccharopine dehydrogenase from Arabidopsis thaliana: nucleotide sequence and characterization. Epelbaum S, McDevitt R, Falco SC. Plant Mol. Biol. 35, 735-48, (1997). View articlePMID: 9426595
12.Lysine metabolism in higher plants. Azevedo RA, Lea PJ. Amino Acids 20, 261-79, (2001). View articlePMID: 11354603
13.A proposed proton shuttle mechanism for saccharopine dehydrogenase from Saccharomyces cerevisiae. Xu H, Alguindigue SS, West AH, Cook PF. Biochemistry 46, 871-82, (2007). PMID: 17223709