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MetaCyc Enzyme: multifunctional protein MFP III

Synonyms: tetrafunctional protein, multifunctional protein, 2-enoyl-CoA hydratase I

Species: Cucumis sativus

Summary:
At least three forms of multifunctional protein (MFP) have been purified from cucumber peroxisome. multifunctional protein MFP I (74 kDa) is a trifunctional enzyme possessing 2-enoyl-CoA hydratase (L-3-hydroxyacyl-CoA hydro-lyase), D-3-hydroxyacyl-CoA epimerase and L-3-hydroxyacyl-CoA dehydrogenase activities. multifunctional protein MFP II (76.5 kDa) and multifunctional protein MFP III (81 kDa) are tetrafunctional enzymes having delta-3, delta2-enoyl-CoA isomerase, 2-enoyl-CoA hydratase (L-3-hydroxyacyl-CoA hydro-lyase), D-3-hydroxyacyl-CoA epimerase and L-3-hydroxyacyl-CoA dehydrogenase activities.

In addition, a fourth cDNA clone, known as MFP a, was reported to encode a tetrafunctional MFP that differs from MFP II and MFP III. Expressing the cDNA in Escherichia coli and characterization of the purified recombinant protein revealed four activities: delta-3, delta2-enoyl-CoA isomerase, 2-enoyl-CoA hydratase (L-3-hydroxyacyl-CoA hydro-lyase), D-3-hydroxyacyl-CoA epimerase and L-3-hydroxyacyl-CoA dehydrogenase. The ratio of the four activities is 1:4000:3:20 [PreisigMuller94].

Molecular Weight of Polypeptide: 81 kD (experimental) [GuhnemannSchafe95 ]

Gene-Reaction Schematic: ?

Instance reaction of [a cis-3-enoyl-CoA ↔ a trans-2-enoyl-CoA] (5.3.3.8):
i1: 3-cis-dodecenoyl-CoA → 2-trans-dodecenoyl-CoA (5.3.3.8)

Instance reactions of [a (3S)-3-hydroxyacyl-CoA ← a trans-2-enoyl-CoA + H2O] (4.2.1.17):
i9: (3R)-3-hydroxy-lignoceroyl-CoA → trans-lignocer-2-enoyl-CoA + H2O (4.2.1.134)

i10: (S)-3-hydroxybutanoyl-CoA ↔ crotonyl-CoA + H2O (4.2.1.150)

i11: (S)-3-hydroxydecanoyl-CoA ← trans-Δ2-decenoyl-CoA + H2O (4.2.1.17)

i12: (S)-3-hydroxyhexanoyl-CoA → trans-hex-2-enoyl-CoA + H2O (4.2.1.74)

Instance reactions of [a (3S)-3-hydroxyacyl-CoA + NAD+ ↔ a 3-oxoacyl-CoA + NADH + H+] (1.1.1.35):
i2: 3-hydroxy-5-cis-tetradecenoyl-CoA + NAD+ = 3-keto-5-cis-tetradecenoyl-CoA + NADH + H+ (1.1.1.211)

i3: (S)-3-hydroxytetradecanoyl-CoA + NAD+ = 3-oxo-myristoyl-CoA + NADH + H+ (no EC#)

i4: (S)-3-hydroxyhexadecanoyl-CoA + NAD+ = 3-oxo-palmitoyl-CoA + NADH + H+ (1.1.1.211)

i5: (S)-3-hydroxybutanoyl-CoA + NAD+ ↔ acetoacetyl-CoA + NADH + H+ (1.1.1.35)

i6: (S)-3-hydroxyoctanoyl-CoA + NAD+ = 3-oxooctanoyl-CoA + NADH + H+ (1.1.1.35)

i7: (S)-3-hydroxydecanoyl-CoA + NAD+ → 3-oxodecanoyl-CoA + NADH + H+ (1.1.1.35)

i8: (S)-3-hydroxyhexanoyl-CoA + NAD+ ← 3-oxohexanoyl-CoA + NADH + H+ (1.1.1.35)


Enzymatic reaction of: enoyl-CoA isomerase (multifunctional protein MFP III)

Synonyms: δ-3, δ-2-enoyl-CoA isomerase

a cis-3-enoyl-CoA <=> a trans-2-enoyl-CoA

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

This reaction is reversible.

In Pathways: fatty acid β-oxidation III (unsaturated, odd number)


Enzymatic reaction of: 3-hydroxyacyl-CoA epimerase (multifunctional protein MFP III)

Synonyms: D-3-hydroxyacyl-CoA epimerase

a (3R)-3-hydroxyacyl-CoA <=> a (3S)-3-hydroxyacyl-CoA

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

This reaction is reversible.

In Pathways: unsaturated, even numbered fatty acid β-oxidation


Enzymatic reaction of: (3R)-3-hydroxyacyl-CoA hydro-lyase (multifunctional protein MFP III)

Synonyms: 2-enoyl-CoA hydratase, L-3-hydroxyacyl-CoA hydro-lyase

EC Number: 4.2.1.17

a (3R)-3-hydroxyacyl-CoA <=> a cis-2-enoyl-CoA + H2O

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is favored in the opposite direction.

In Pathways: unsaturated, even numbered fatty acid β-oxidation


Enzymatic reaction of: trans-enoyl-CoA isomerase (multifunctional protein MFP III)

Synonyms: δ-3, δ-2-enoyl-CoA isomerase

a trans-3-enoyl-CoA <=> a trans-2-enoyl-CoA

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

This reaction is reversible.

In Pathways: unsaturated, even numbered fatty acid β-oxidation


Enzymatic reaction of: (S)-3-hydroxyacyl-CoA:NAD+ oxidoreductase (multifunctional protein MFP III)

Synonyms: L-3-hydroxyacyl-CoA dehydrogenase

EC Number: 1.1.1.35

a (3S)-3-hydroxyacyl-CoA + NAD+ <=> a 3-oxoacyl-CoA + NADH + H+

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is physiologically favored in the direction shown.

In Pathways: fatty acid β-oxidation II (peroxisome)


Enzymatic reaction of: (3S)-3-hydroxyacyl-CoA hydro-lyase (multifunctional protein MFP III)

Synonyms: 2-enoyl-CoA hydratase, L-3-hydroxyacyl-CoA hydro-lyase

EC Number: 4.2.1.17

a (3S)-3-hydroxyacyl-CoA <=> a trans-2-enoyl-CoA + H2O

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is physiologically favored in the opposite direction.

In Pathways: unsaturated, even numbered fatty acid β-oxidation , fatty acid β-oxidation II (peroxisome)


References

Allenbach00: Allenbach L, Poirier Y (2000). "Analysis of the alternative pathways for the beta-oxidation of unsaturated fatty acids using transgenic plants synthesizing polyhydroxyalkanoates in peroxisomes." Plant Physiol 124(3);1159-68. PMID: 11080293

GuhnemannSchafe95: Guhnemann-Schafer K, Kindl H (1995). "Fatty acid beta-oxidation in glyoxysomes. Characterization of a new tetrafunctional protein (MFP III)." Biochim Biophys Acta 1256(2);181-6. PMID: 7766696

PreisigMuller94: Preisig-Muller R, Guhnemann-Schafer K, Kindl H (1994). "Domains of the tetrafunctional protein acting in glyoxysomal fatty acid beta-oxidation. Demonstration of epimerase and isomerase activities on a peptide lacking hydratase activity." J Biol Chem 269(32);20475-81. PMID: 8051146


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 18.5 on Wed Nov 26, 2014, BIOCYC14B.