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Ligand 1,2-dihydroxy-5-(methylthio)pent-1-en-3-one

Basic Ligand Information

Molecular Structure

Show all BRENDA pathways known for 1,2-dihydroxy-5-(methylthio)pent-1-en-3-one

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (4 results)

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Show Natural Substrate (4 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.13.11.53

1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + O2 = 3-(methylthio)-2-oxobutanoate + formate

725214

-

1.13.11.53

1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + O2 = 3-(methylthio)propanoate + formate + CO

661058, 662101, 661942, 662933

-

1.13.11.54

1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + O2 = 3-(methylthio)propanoate + formate + CO

661058

-

1.13.11.54

1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + O2 = 4-(methylthio)-2-oxobutanoate + formate

725214, 725438, 662101

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1.13.11.53

2 entries

1.13.11.54

2 entries

In Vivo Product in Enzyme-catalyzed Reactions (2 results)

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Show Natural Product (2 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

3.1.3.87

2-hydroxy-5-methylthio-pent-1-ene-3-one phosphate + H2O = 1,2-dihydroxy-5-methylthio-pent-1-ene-3-one + phosphate

-

-

3.1.3.87

5-methylthio-2,3-dioxopentyl phosphate + H2O = 1,2-dihydroxy-5-methylthio-pent-1-ene-3-one + phosphate

-

-

3.1.3.87

2 entries

Substrate in Enzyme-catalyzed Reactions (7 results)

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Show Substrate (7 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.13.11.53

1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + O2 = 3-(methylthio)-2-oxobutanoate + formate

725214

-

1.13.11.53

1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + O2 = 3-(methylthio)propanoate + formate + CO

673849, 661942, 662101, 663098, 677051, 725214, 674007, 674006, 662933, 662095, 662091, 662049, 661058, 673852

-

1.13.11.53

1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + O2 = 4-methylthio-2-ketobutyrate + formate + CO

675408

-

1.13.11.54

1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + O2 = 2-keto-4-methyl thiobutyrate + formate

673849

-

1.13.11.54

1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + O2 = 3-(methylthio)propanoate + formate

675408

-

1.13.11.54

1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + O2 = 3-(methylthio)propanoate + formate + CO

661058

-

1.13.11.54

1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + O2 = 4-(methylthio)-2-oxobutanoate + formate

725214, 725438, 662101, 661058

-

1.13.11.53

3 entries

1.13.11.54

4 entries

Product in Enzyme-catalyzed Reactions (2 results)

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Show Product (2 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

3.1.3.87

2-hydroxy-5-methylthio-pent-1-ene-3-one phosphate + H2O = 1,2-dihydroxy-5-methylthio-pent-1-ene-3-one + phosphate

-

-

3.1.3.87

5-methylthio-2,3-dioxopentyl phosphate + H2O = 1,2-dihydroxy-5-methylthio-pent-1-ene-3-one + phosphate

-

-

3.1.3.87

2 entries

Enzyme Kinetic Parameters

K_M Value (3 results)

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Show KM Value (3 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.13.11.53

0.044

-

-

663098

1.13.11.53

500

-

-

662101

1.13.11.53

2 entries

1.13.11.54

210

-

-

662101

References & Links

Literature References (16)

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Show Reference (16 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

661058

11371200

Mechanistic studies of two dioxygenases in the methionine salvage pathway of Klebsiella pneumoniae

2001

Dai, Y.; Pochapsky, T.C.; Abeles, R.H.

Biochemistry

40

6379-6387

661942

16332057

Aliphatic carbon-carbon bond cleavage reactivity of a mononuclear Ni(II) cis-beta-keto-enolate complex in the presence of base and O2: a model reaction for acireductone dioxygenase (ARD)

2005

Szajna, E.; Arif, A.M.; Berreau, L.M.

J. Am. Chem. Soc.

127

17186-17187

662049

2838472

Intermediates in the conversion of 5'-S-methylthioadenosine to methionine in Klebsiella pneumonia

1988

Furfine, E.S.; Abeles, R.H.

J. Bacteriol.

263

9598-9606

662091

8407993

A bacterial enzyme that catalyzes formation of carbon monoxide

1993

Wray, J.W.; Abeles, R.H.

J. Biol. Chem.

268

21466-21469

662095

7852397

The methionine salvage pathway in Klebsiella pneumoniae and rat liver

1995

Wray, J.W.; Abeles, R.B.

J. Biol. Chem.

270

3147-3153

662101

9880484

One protein, two enzymes

1999

Dai, Y.; Wensink, P.C.; Abeles, R.H.

J. Biol. Chem.

274

1193-1195

662933

12402029

Modeling and experiment yields the structure of acireductone dioxygenase from Klebsiella pneumoniae

2002

Pochapsky, T.C.; Pochapsky, S.S.; Ju, T.; Mo, H.; Al-Mjeni, F.; Maroney, M.J.

Nat. Struct. Biol.

9

966-972

663098

16297065

The immediate-early ethylene response gene OsARD1 encodes an acireductone dioxygenase involved in recycling of the ethylene precursor S-adenosylmethionine

2005

Sauter, M.; Lorbiecke, R.; Ouyang, B.; Pochapsky, T.C.; Rzewuski, G.

Plant J.

44

718-729

673849

15938715

Membrane-type 1 matrix metalloproteinase cytoplasmic tail binding protein-1 (MTCBP-1) acts as an eukaryotic aci-reductone dioxygenase (ARD) in the methionine salvage pathway

2005

Hirano, W.; Gotoh, I.; Uekita, T.; Seiki, M.

Genes Cells

10

565-574

673852

17212658

Regulated nucleo-cytoplasmic shuttling of human aci-reductone dioxygenase (hADI1) and its potential role in mRNA processing

2007

Gotoh, I.; Uekita, T.; Seiki, M.

Genes Cells

12

105-117

674006

17288413

Carboxylate coordination chemistry of a mononuclear Ni(II) center in a hydrophobic or hydrogen bond donor secondary environment: Relevance to acireductone dioxygenase

2007

Szajna-Fuller, E.; Chambers, B.M.; Arif, A.M.; Berreau, L.M.

Inorg. Chem.

46

5486-5498

674007

17295469

Acireductone dioxygenase-(ARD-) type reactivity of a nickel(II) complex having monoanionic coordination of a model substrate: Product identification and comparisons to unreactive analogues

2007

Szajna-Fuller, E.; Rudzka, K.; Arif, A.M.; Berreau, L.M.

Inorg. Chem.

46

5499-5507

675408

16989860

One protein, two enzymes revisited: A structural entropy switch interconverts the two isoforms of acireductone dioxygenase

2006

Ju, T.; Goldsmith, R.B.; Chai, S.C.; Maroney, M.J.; Pochapsky, S.S.; Pochapsky, T.C.

J. Mol. Biol.

363

823-834

677051

16783794

Crystal structure of acireductone dioxygenase (ARD) from Mus musculus at 2.06 A resolution

2006

Xu Q.; Schwarzenbacher R.; Krishna SS.; McMullan D.; Agarwalla S.; Quijano K.; Abdubek P.; Ambing E.; Axelrod H.; Biorac T.; Canaves JM.; Chiu HJ.; Elsliger MA.; Grittini C.; Grzechnik SK.; DiDonato M.; Hale J.; Hampton E.; Han GW.; Haugen J.; Hornsby M.; Jaroszewski L.; Klock H.E.; Knuth MW.; Koesema E.; Kreusch A.; Kuhn P.; Miller M.D.; Moy K.; Nigoghossian E.; Paulsen J.; Reyes R.; Rife C.; Spraggon G.; Stevens RC.; van den Bedem H.; Velasquez J.; White A.; Wolf G.; Hodgson K.O.; Wooley J.; Deacon A.M.; Godzik A.; Lesley SA.; Wilson I.A.

Proteins

64

808-813

725214

23214721

Regioselective aliphatic carbon-carbon bond cleavage by a model system of relevance to iron-containing acireductone dioxygenase

2013

Allpress, C.J.; Grubel, K.; Szajna-Fuller, E.; Arif, A.M.; Berreau, L.M.

J. Am. Chem. Soc.

135

659-668

725438

21712381

Acireductone dioxygenase 1 (ARD1) is an effector of the heterotrimeric G protein beta subunit in Arabidopsis

2011

Friedman, E.; Wang, H.; Jiang, K.; Perovic, I.; Deshpande, A.; Pochapsky, T.; Temple, B.; Hicks, S.; Harden, T.; Jones, A.

J. Biol. Chem.

286

30107-30118

Links to other databases for 1,2-dihydroxy-5-(methylthio)pent-1-en-3-one

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ChEBI

PubChem

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