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Ligand 4-methylpentanal

Basic Ligand Information

Molecular Structure

Show all BRENDA pathways known for 4-methylpentanal

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Roles as Enzyme Ligand

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

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Show Natural Product (4 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.14.15.6

(20R,22R)-20,22-dihydroxy-cholesterol + 2 reduced adrenodoxin + O2 = pregnenolone + 4-methylpentanal + 2 oxidized adrenodoxin + 2 H2O

0

-

1.14.15.6

cholesterol + 6 reduced adrenodoxin + 3 O2 = pregnenolone + 4-methylpentanal + 6 oxidized adrenodoxin + 4 H2O

285425, 285429, 285430, 285432, 285433, 285431, 285412, 285415, 285417, 285418, 285420, 285421, 285422, 285423, 285428, 285426, 0

-

1.14.15.6

cholesterol + reduced adrenal ferredoxin + O2 = pregnenolone + 4-methylpentanal + oxidized adrenal ferredoxin

0

-

1.14.15.6

cholesterol + reduced ferredoxin + O2 = pregnenolone + 4-methylpentanal + oxidized ferredoxin

0

-

1.14.15.6

4 entries

Substrate in Enzyme-catalyzed Reactions (2 results)

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Show Substrate (2 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.149

isocaproaldehyde + NADPH + H+ = ?

740126

-

1.1.1.21

isocaproaldehyde + NADPH + H+ = ?

695881

-

Product in Enzyme-catalyzed Reactions (12 results)

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Show Product (12 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.1

4-methyl-1-pentanol + NAD+ = 4-methyl-1-pentanal + NADH

0

-

1.1.1.245

4-methyl-1-pentanol + NAD+ = 4-methylpentanal + NADH

0

-

1.1.1.80

4-methyl-1-pentanol + NAD+ = 4-methyl-1-pentanal + NADH

0

-

1.1.1.80

4-methyl-1-pentanol + NADP+ = 4-methyl-1-pentanal + NADPH

0

-

1.14.15.6

(20R,22R)-20,22-dihydroxy-cholesterol + 2 reduced adrenodoxin + O2 = pregnenolone + 4-methylpentanal + 2 oxidized adrenodoxin + 2 H2O

0

-

1.14.15.6

20alpha-hydroxycholesterol + reduced adrenodoxin + O2 = pregnenolone + 4-methylpentanal + oxidized adrenodoxin + H2O

285418, 0

-

1.14.15.6

cholesterol + 6 reduced adrenodoxin + 3 O2 = pregnenolone + 4-methylpentanal + 6 oxidized adrenodoxin + 4 H2O

285425, 285429, 285430, 285432, 285433, 285431, 285412, 285415, 285417, 285418, 285420, 285421, 285422, 285423, 285428, 285426, 0

-

1.14.15.6

cholesterol + 6 reduced adrenodoxin mutant S112W + 3 O2 = pregnenolone + 4-methylpentanal + 6 oxidized adrenodoxin mutant S112W + 4 H2O

0

-

1.14.15.6

cholesterol + reduced adrenal ferredoxin + O2 = pregnenolone + 4-methylpentanal + oxidized adrenal ferredoxin

0

-

1.14.15.6

cholesterol + reduced adrenodoxin + O2 + H+ = pregnenolone + 4-methylpentanal + oxidized adrenodoxin + H2O

0

-

1.14.15.6

cholesterol + reduced adrenodoxin + O2 = pregnenolone + 4-methylpentanal + oxidized adrenodoxin + H2O

0, 285412, 285413, 285414, 285415, 285419, 285420, 285423, 285424, 285426, 285427, 285428, 285429, 285430, 285431, 285432, 285433, 285422, 285421, 285425, 285416, 285418, 285417

-

1.14.15.6

cholesterol + reduced ferredoxin + O2 = pregnenolone + 4-methylpentanal + oxidized ferredoxin

0

-

1.1.1.80

2 entries

1.14.15.6

8 entries

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (2 results)

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Show Turnover Number (2 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.1.1.149

0.023

-

at pH 7.4 and 37°C

740126

1.1.1.21

1.43

-

in 0.1 M potassium phosphate, pH 7.4, at 25°C

695881

K_M Value (2 results)

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Show KM Value (2 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.1.1.149

0.068

-

at pH 7.4 and 37°C

740126

1.1.1.21

0.056

-

in 0.1 M potassium phosphate, pH 7.4, at 25°C

695881

References & Links

Literature References (24)

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Show Reference (24 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

285412

6766943

Mitochondrial cytochrome P-450sec. Mechanism of electron transport by adrenodoxin

1980

Hanukoglu, I.; Jefcoate, C.R.

J. Biol. Chem.

255

3057-3061

285413

7217084

Adrenal mitochondrial cytochrome P-450scc. Cholesterol and adrenodoxin interactions at equilibrium and during turnover

1981

Hanukoglu, I.; Spitsberg, V.; Bumpus, J.A.; Dus, K.M.; Jefcoate, C.R.

J. Biol. Chem.

256

4321-4328

285414

6783659

Mechanisms of ionic activation of adrenal mitochondrial cytochromes P-450scc and P-45011beta

1981

Hanukoglu, I.; Privalle, C.T.; Jefcoate, C.R.

J. Biol. Chem.

256

4329-4335

285415

184090

Purification and characterization of adrenal cortex mitochondrial cytochrome P-450 specific for cholesterol side chain cleavage activity

1976

Wang, H.P.; Kimura, T.

J. Biol. Chem.

251

6068-6074

285416

444237

Binding of Triton X-100 to purified cytochrome P-450scc and enhancement of the cholesterol side chain cleavage activity

1979

Nakajin, S.; Ishii, Y.; Shinoda, M.

Biochem. Biophys. Res. Commun.

87

524-531

285417

6723652

The catalytic cycle of cytochrome P-450scc and intermediates in the conversion of cholesterol to pregnenolone

1984

Hume, R.; Kelly, R.W.; Taylor, P.L.; Boyd, G.S.

Eur. J. Biochem.

140

583-591

285418

4723901

Cytochrome P-450 from bovine adrenocortical mitochondria: an enzyme for the side chain cleavage of cholesterol. I. Purification and properties

1973

Shikita, M.; Hall, P.F.

J. Biol. Chem.

248

5598-5604

285419

1131251

Purification of cytochrome P-450 from bovine adrenocortical mitochondria by an aniline-Sepharose and the properties

1975

Takemori, S.; Sukara, K.; Hashimoto, K.; Hashimoto, M.; Sato, H.; Gomi, T.; Katagiri, M.

Biochem. Biophys. Res. Commun.

63

588-593

285420

2605191

Cholesterol metabolism by purified cytochrome P-450scc is highly stimulated by octyl glucoside and stearic acid exclusively in large unilamellar phospholipid vesicles

1989

Dhariwal, M.S.; Jefcoate, C.R.

Biochemistry

28

8397-8402

285421

4019455

Cytochrome P-450scc-adrenodoxin interactions. Ionic effects on binding, and regulation of cytochrome reduction by bound steroid substrates

1985

Lambeth, J.D.; Kriengsiri, S.

J. Biol. Chem.

260

8810-8816

285422

3968069

Competitive inhibition of cytochrome P-450scc by (22R)- and (22S)-22-aminocholesterol. Side-chain stereochemical requirements for C-22 amine coordination to the active-site heme

1985

Nagahisa, A.; Foo, T.; Gut, M.; Orme-Johnson, W.H.

J. Biol. Chem.

260

846-851

285423

6244284

Purification and characterization of mitochondrial cytochrome P-450 associated with cholesterol side chain cleavage from bovine corpus luteum

1980

Kashiwagi, K.; Dafeldecker, W.P.; Salhanick, H.A.

J. Biol. Chem.

255

2606-2611

285424

6688621

Active site-directed inhibitors of cytochrome P-450scc. Structural and mechanistic implications of a side chain-substituted series of amino-steroids

1983

Sheets, J.J.; Vickery, L.E.

J. Biol. Chem.

258

11446-11452

285425

6822531

C-22-Substituted steroid derivatives as substrate analogues and inhibitors of cytochrome P-450scc

1983

Sheets, J.J.; Vickery, L.E.

J. Biol. Chem.

258

1720-1725

285426

6572949

Modulation of the kinetics of cholesterol side-chain cleavage by an activator and by an inhibitor isolated from the cytosol of the cortex of bovine adrenals

1983

Warne, P.A.; Greenfield, N.J.; Lieberman, S.

Proc. Natl. Acad. Sci. USA

80

1877-1881

285427

4723902

Cytochrome P-450 from bovine adrenocortical mitochondria: an enzyme for the side chain cleavage of cholesterol. II. Subunit structure

1973

Shikita, M.; Hall, P.F.

J. Biol. Chem.

248

5605-5609

285428

7599132

Cytochrome P-450scc-mediated oxidation of (20S)-22-thiacholesterol: Characterization of mechanism-based inhibition

1995

Miao, E.; Joardar, S.; Zuo, C.; Cloutier, N.J.; Nagahisa, A.; Byon, C.; Wilson, S.R.; Orme-Johnson, W.H.

Biochemistry

34

8415-8421

285429

8662703

alpha-Branched 1,2-diacyl phosphatidylcholines as effectors of activity of cytochrome P450SCC (CYP11A1). Modeling the structure of the fatty acyl chain region of cardiolipin

1996

Schwarz, D.; Kisselev, P.; Wessel, R.; Jueptner, O.; Schmid, R.D.

J. Biol. Chem.

271

12840-12846

285430

11173513

Site-directed mutagenesis of cytochrome P450scc (CYP11A1). Effect of lysine residue substitution on its structural and functional properties

2000

Lepesheva, G.I.; Azeva, T.N.; Strushkevich, N.V.; Gilep, A.A.; Usanov, S.A.

Biochemistry (Moscow)

65

1409-1418

285431

10924360

The use of the novel substrate-heme complex approach in the derivation of a representation of the active site of the enzyme cholesterol side chain cleavage

2000

Ahmed, S.

Biochem. Biophys. Res. Commun.

274

821-824

285432

8431464

Substrate-binding region of cytochrome P-450scc (P-450 XIA1). Identification and primary structure of the cholesterol binding region in cytochrome P-450scc

1993

Tsujita, M.; Ichikawa, Y.

Biochim. Biophys. Acta

1161

124-130

285433

12081479

Probing the interaction of bovine cytochrome P450scc (CYP11A1) with adrenodoxin: evaluating site-directed mutations by molecular modeling

2002

Usanov, S.A.; Graham, S.E.; Lepesheva, G.I.; Azeva, T.N.; Strushkevich, N.V.; Gilep, A.A.; Estabrook, R.W.; Peterson, J.

Biochemistry

41

8310-8320

695881

19464995

Kinetic studies of AKR1B10, human aldose reductase-like protein: endogenous substrates and inhibition by steroids

2009

Endo, S.; Matsunaga, T.; Mamiya, H.; Ohta, C.; Soda, M.; Kitade, Y.; Tajima, K.; Zhao, H.T.; El-Kabbani, O.; Hara, A.

Arch. Biochem. Biophys.

487

1-9

740126

23995665

Substrate specificity and inhibitor sensitivity of rabbit 20alpha-hydroxysteroid dehydrogenase

2013

Endo, S.; Arai, Y.; Hara, A.; Kitade, Y.; Bunai, Y.; El-Kabbani, O.; Matsunaga, T.

Biol. Pharm. Bull.

36

1514-1518

Links to other databases for 4-methylpentanal

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ChEBI

PubChem