cd12189

bifunctional lysine ketoglutarate reductase /saccharopine dehydrogenase enzyme

CDD entry
Member databaseCDD
CDD typedomain
Short nameLKR_SDH_like
SetNADB_Rossmann

Description

Bifunctional lysine ketoglutarate reductase /saccharopine dehydrogenase protein is a pair of enzymes linked on a single polypeptide chain that catalyze the initial, consecutive steps of lysine degradation. These proteins are related to the 2-domain saccharopine dehydrogenases. Along with formate dehydrogenase and similar enzymes, SDH consists paired domains resembling Rossmann folds in which the NAD-binding domain is inserted within the linear sequence of the catalytic domain. In this bifunctional enzyme, the LKR domain is N-terminal of the SDH domain. These proteins have a close match to the active site motif of SDHs, and an NAD-binding site motif that is a partial match to that found in SDH and other FDH-related proteins.
[2, 14, 1, 6, 10, 12, 8, 15, 4, 5, 9, 7, 13, 11, 3]

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

14.Structural and transcriptional analysis of plant genes encoding the bifunctional lysine ketoglutarate reductase saccharopine dehydrogenase enzyme. Anderson OD, Coleman-Derr D, Gu YQ, Heath S. BMC Plant Biol 10, 113, (2010). PMID: 20565711

15.Crystallization of the alanine dehydrogenase from Phormidium lapideum. Sedelnikova S, Rice DW, Shibata H, Sawa Y, Baker PJ. Acta Crystallogr D Biol Crystallogr 54, 407-8, (1998). PMID: 9761911

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