cd08295

Arabidopsis alkenal double bond reductase and leukotriene B4 12-hydroxydehydrogenase

CDD entry
Member databaseCDD
CDD typedomain
Short namedouble_bond_reductase_like
SetMDR

Description

This group includes proteins identified as the Arabidopsis alkenal double bond reductase and leukotriene B4 12-hydroxydehydrogenase. The Arabidopsis enzyme, a member of the medium chain dehydrogenase/reductase family, catalyzes the reduction of 7-8-double bond of phenylpropanal substrates as a plant defense mechanism. Prostaglandins and related eicosanoids (lipid mediators involved in host defense and inflamation) are metabolized by the oxidation of the 15(S)-hydroxyl group of the NAD+-dependent (type I 15-PGDH) 15-prostaglandin dehydrogenase (15-PGDH) followed by reduction by NADPH/NADH-dependent (type II 15-PGDH) delta-13 15-prostaglandin reductase (13-PGR) to 15-keto-13,14,-dihydroprostaglandins. 13-PGR is a bifunctional enzyme, since it also has leukotriene B(4) 12-hydroxydehydrogenase activity. Leukotriene B4 (LTB4) can be metabolized by LTB4 20-hydroxylase in inflamatory cells, and in other cells by bifunctional LTB4 12-HD/PGR. These 15-PGDH and related enzymes are members of the medium chain dehydrogenase/reductase family. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of an beta-alpha form and an N-terminal catalytic domain with distant homology to GroES.
[3, 9, 6, 2, 5, 1, 7, 4, 8]

References

1.Medium- and short-chain dehydrogenase/reductase gene and protein families : the MDR superfamily. Persson B, Hedlund J, Jornvall H. Cell. Mol. Life Sci. 65, 3879-94, (2008). View articlePMID: 19011751

2.Comparison of super-secondary structures in proteins. Rao ST, Rossmann MG. J. Mol. Biol. 76, 241-56, (1973). View articlePMID: 4737475

3.Structural basis of leukotriene B4 12-hydroxydehydrogenase/15-Oxo-prostaglandin 13-reductase catalytic mechanism and a possible Src homology 3 domain binding loop. Hori T, Yokomizo T, Ago H, Sugahara M, Ueno G, Yamamoto M, Kumasaka T, Shimizu T, Miyano M. J. Biol. Chem. 279, 22615-23, (2004). View articlePMID: 15007077

4.A super-family of medium-chain dehydrogenases/reductases (MDR). Sub-lines including zeta-crystallin, alcohol and polyol dehydrogenases, quinone oxidoreductase enoyl reductases, VAT-1 and other proteins. Persson B, Zigler JS Jr, Jornvall H. Eur J Biochem 226, 15-22, (1994). PMID: 7957243

5.Crystal structure of a putative NADPH-dependent oxidoreductase (GI: 18204011) from mouse at 2.10 A resolution. Levin I, Schwarzenbacher R, McMullan D, Abdubek P, Ambing E, Biorac T, Cambell J, Canaves JM, Chiu HJ, Dai X, Deacon AM, DiDonato M, Elsliger MA, Godzik A, Grittini C, Grzechnik SK, Hampton E, Jaroszewski L, Karlak C, Klock HE, Koesema E, Kreusch A, Kuhn P, Lesley SA, McPhillips TM, Miller MD, Morse A, Moy K, Ouyang J, Page R, Quijano K, Reyes R, Robb A, Sims E, Spraggon G, Stevens RC, van den Bedem H, Velasquez J, Vincent J, von Delft F, Wang X, West B, Wolf G, Xu Q, Hodgson KO, Wooley J, Wilson IA. Proteins 56, 629-33, (2004). View articlePMID: 15229897

6.NAD-binding domains of dehydrogenases. Lesk AM. Curr. Opin. Struct. Biol. 5, 775-83, (1995). View articlePMID: 8749365

7.Medium-chain dehydrogenases/reductases (MDR). Family characterizations including genome comparisons and active site modeling. Nordling E, Jornvall H, Persson B. Eur. J. Biochem. 269, 4267-76, (2002). View articlePMID: 12199705

8.Merging protein, gene and genomic data: the evolution of the MDR-ADH family. Gonzalez-Duarte R, Albalat R. Heredity (Edinb) 95, 184-97, (2005). PMID: 16121213

9.Mechanistic and structural studies of apoform, binary, and ternary complexes of the Arabidopsis alkenal double bond reductase At5g16970. Youn B, Kim SJ, Moinuddin SG, Lee C, Bedgar DL, Harper AR, Davin LB, Lewis NG, Kang C. J. Biol. Chem. 281, 40076-88, (2006). View articlePMID: 17028190

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