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MetaCyc Enzyme: fatty acid oxidation complex, α component

Gene: fadB Accession Numbers: EG10279 (MetaCyc), b3846, ECK3838

Synonyms: oldB

Species: Escherichia coli K-12 substr. MG1655

Component of: aerobic fatty acid oxidation complex

Subunit composition of fatty acid oxidation complex, α component = [FadB]2
         dodecenoyl-CoA δ-isomerase, enoyl-CoA hydratase, 3-hydroxybutyryl-CoA epimerase, 3-hydroxyacyl-CoA dehydrogenase = FadB

Summary:
The alpha subunit has four enzymatic activities associated with it. It is part of a multienzyme complex. Two of the activities, enoyl-CoA hydratase (EC 4.2.1.17) and 3-OHacyl-CoA epimerase (EC 5.1.2.3) are carried out by the same N terminal active site. [Yang93]

Locations: cytosol

Map Position: [4,028,782 <- 4,030,971]

Molecular Weight of Polypeptide: 79.594 kD (from nucleotide sequence)

pI: 6.16

Unification Links: ASAP:ABE-0012564, CGSC:793, DIP:DIP-9560N, EchoBASE:EB0275, EcoGene:EG10279, EcoliWiki:b3846, ModBase:P21177, OU-Microarray:b3846, PortEco:fadB, Pride:P21177, Protein Model Portal:P21177, RefSeq:NP_418288, RegulonDB:EG10279, SMR:P21177, String:511145.b3846, Swiss-Model:P21177, UniProt:P21177

Relationship Links: InterPro:IN-FAMILY:IPR001753, InterPro:IN-FAMILY:IPR006108, InterPro:IN-FAMILY:IPR006176, InterPro:IN-FAMILY:IPR006180, InterPro:IN-FAMILY:IPR008927, InterPro:IN-FAMILY:IPR012799, InterPro:IN-FAMILY:IPR013328, InterPro:IN-FAMILY:IPR016040, InterPro:IN-FAMILY:IPR018376, InterPro:IN-FAMILY:IPR029045, Pfam:IN-FAMILY:PF00378, Pfam:IN-FAMILY:PF00725, Pfam:IN-FAMILY:PF02737, Prosite:IN-FAMILY:PS00067, Prosite:IN-FAMILY:PS00166

Gene-Reaction Schematic

Expand/Contract the Schematic connections:

Gene-Reaction Schematic

Instance reaction of [a cis-3-enoyl-CoA ↔ a trans-2-enoyl-CoA] (5.3.3.8):
i40: 3-cis-dodecenoyl-CoA ↔ trans-dodec-2-enoyl-CoA (5.3.3.8)

Instance reactions of [a (3S)-3-hydroxyacyl-CoA ← a trans-2-enoyl-CoA + H2O] (4.2.1.17):
i26: (S)-3-hydroxy-(5Z)-dodecenoyl-CoA ← (2E,5Z)-dodecenoyl-CoA + H2O (1.1.1.35)

i27: (3S)-hydroxy-(6Z,9Z,12Z,15Z,18Z)-tetracosapentaenoyl-CoA ← (2E,6Z,9Z,12Z,15Z,18Z)-tetracosahexaenoyl-CoA + H2O (4.2.1.17)

i28: (3S)-hydroxy-(6Z,9Z,12Z,15Z,18Z,21Z)-tetracosahexaenoyl-CoA ← (2E,6Z,9Z,12Z,15Z,18Z,21Z)-tetracosaheptaenoyl-CoA + H2O (4.2.1.17)

i29: (S)-3-hydroxyhexadecanoyl-CoA ← trans-hexadec-2-enoyl-CoA + H2O (4.2.1.17)

i30: (S)-3-hydroxy-(9Z)-octadecenoyl-CoA ← (2E,9Z)-octadecenoyl-CoA + H2O (4.2.1.17)

i31: (S)-3-hydroxybutanoyl-CoA ↔ crotonyl-CoA + H2O (4.2.1.150)

i32: (3R)-3-hydroxy-lignoceroyl-CoA → trans-lignocer-2-enoyl-CoA + H2O (4.2.1.134)

i33: (S)-3-hydroxytetradecanoyl-CoA ← 2-trans-tetradecenoyl-CoA + H2O (4.2.1.17)

i34: (S)-3-hydroxy-(7Z)-tetradecenoyl-CoA ← (2E,7Z)-tetradecenoyl-CoA + H2O (1.1.1.35)

i35: (S)-3-hydroxydecanoyl-CoA ← trans-dec-2-enoyl-CoA + H2O (4.2.1.17)

i36: (11Z)-(S)-3-hydroxyhexadec-11-enoyl-CoA ← (2E,11Z)-hexadec-2,11-dienoyl-CoA + H2O (4.2.1.17)

i37: (S)-3-hydroxyhexanoyl-CoA → trans-hex-2-enoyl-CoA + H2O (4.2.1.17)

i38: a long-chain (3S)-3-hydroxyacyl-CoA ← a long-chain trans-2,3-dehydroacyl-CoA + H2O (4.2.1.74)

i39: a short-chain (3S)-3-hydroxyacyl-CoA ← a short-chain trans-2,3-dehydroacyl-CoA + H2O (4.2.1.150)

Instance reactions of [a (3S)-3-hydroxyacyl-CoA + NAD+ → a 3-oxoacyl-CoA + NADH + H+] (1.1.1.35):
i15: (3S)-hydroxy-(6Z,9Z,12Z,15Z,18Z)-tetracosapentaenoyl-CoA + NAD+ → 3-oxo-(6Z,9Z,12Z,15Z,18Z)-tetracosapentaenoyl-CoA + NADH + H+ (1.1.1.-)

i16: (3S)-hydroxy-(6Z,9Z,12Z,15Z,18Z,21Z)-tetracosahexaenoyl-CoA + NAD+ → 3-oxo-(6Z,9Z,12Z,15Z,18Z,21Z)-tetracosahexaenoyl-CoA + NADH + H+ (1.1.1.-)

i17: (S)-3-hydroxyhexadecanoyl-CoA + NAD+ → 3-oxo-palmitoyl-CoA + NADH + H+ (1.1.1.211)

i18: (S)-3-hydroxy-(5Z)-tetradecenoyl-CoA + NAD+ → 3-oxo-(5Z)-tetradecenoyl-CoA + NADH + H+ (1.1.1.211)

i19: (S)-3-hydroxy-(9Z)-octadecenoyl-CoA + NAD+ → 3-oxo-(9Z)-octadecenoyl-CoA + NADH + H+ (1.1.1.35)

i20: (S)-3-hydroxybutanoyl-CoA + NAD+ ↔ acetoacetyl-CoA + NADH + H+ (1.1.1.35)

i21: (S)-3-hydroxytetradecanoyl-CoA + NAD+ → 3-oxo-myristoyl-CoA + NADH + H+ (no EC#)

i22: (S)-3-hydroxydecanoyl-CoA + NAD+ → 3-oxodecanoyl-CoA + NADH + H+ (1.1.1.35)

i23: (11Z)-(S)-3-hydroxyhexadec-11-enoyl-CoA + NAD+ → (11Z)-3-oxo-hexadecenoyl-CoA + NADH + H+ (1.1.1.211)

i24: (S)-3-hydroxyhexanoyl-CoA + NAD+ ← 3-oxohexanoyl-CoA + NADH + H+ (1.1.1.35)

i25: a long-chain (3S)-3-hydroxyacyl-CoA + NAD+ = a long-chain 3-oxoacyl-CoA + NADH + H+ (1.1.1.211)

Instance reactions of [a 2,3,4-saturated fatty acyl CoA + acetyl-CoA ← a 3-oxoacyl-CoA + coenzyme A] (2.3.1.16):
i1: butanoyl-CoA + acetyl-CoA → 3-oxohexanoyl-CoA + coenzyme A (2.3.1.16)

i2: lauroyl-CoA + acetyl-CoA ← 3-oxo-myristoyl-CoA + coenzyme A (2.3.1.16)

i3: hexanoyl-CoA + acetyl-CoA = 3-oxooctanoyl-CoA + coenzyme A (2.3.1.16)

i4: octanoyl-CoA + acetyl-CoA ← 3-oxodecanoyl-CoA + coenzyme A (2.3.1.16)

i5: acetyl-CoA + palmitoleoyl-CoA ← 3-oxo-(11Z)-octadecenoyl-CoA + coenzyme A (2.3.1.16)

i6: acetyl-CoA + (7Z)-tetradecenoyl-CoA ← 3-oxo-(9Z)-hexadecenoyl-CoA + coenzyme A (2.3.1.16)

i7: acetyl-CoA + (5Z)-dodecenoyl-CoA ← 3-oxo-(7Z)-tetradecenoyl-CoA + coenzyme A (2.3.1.16)

i8: (7Z)-hexadecenoyl-CoA + acetyl-CoA ← 3-oxo-(9Z)-octadecenoyl-CoA + coenzyme A (2.3.1.16)

i9: acetyl-CoA + (9Z)-tetradecenoyl-CoA ← (11Z)-3-oxo-hexadecenoyl-CoA + coenzyme A (2.3.1.155)

i10: (5Z)-tetradecenoyl-CoA + acetyl-CoA ← 3-oxo-(7Z)-hexadecenoyl-CoA + coenzyme A (2.3.1.16)

i11: acetyl-CoA + propanoyl-CoA = β-ketovaleryl-CoA + coenzyme A (2.3.1.9)

i12: decanoyl-CoA + acetyl-CoA = 3-oxododecanoyl-CoA + coenzyme A (2.3.1.16)

i13: acetyl-CoA + myristoyl-CoA = 3-oxo-palmitoyl-CoA + coenzyme A (2.3.1.155)

i14: acetyl-CoA + myristoyl-CoA ← 3-oxo-palmitoyl-CoA + coenzyme A (2.3.1.155)


GO Terms:
Biological Process:
Inferred from experimentInferred by computational analysisGO:0006635 - fatty acid beta-oxidation [UniProtGOA12, Pramanik79]
Inferred by computational analysisGO:0006629 - lipid metabolic process [UniProtGOA11a]
Inferred by computational analysisGO:0006631 - fatty acid metabolic process [UniProtGOA11a, GOA06, GOA01a]
Inferred by computational analysisGO:0008152 - metabolic process [UniProtGOA11a, GOA01a]
Inferred by computational analysisGO:0009062 - fatty acid catabolic process [GOA01a]
Inferred by computational analysisGO:0016042 - lipid catabolic process [UniProtGOA11a, GOA06]
Inferred by computational analysisGO:0055114 - oxidation-reduction process [UniProtGOA11a, GOA01a]
Molecular Function:
Inferred from experimentInferred by computational analysisGO:0003857 - 3-hydroxyacyl-CoA dehydrogenase activity [GOA06, GOA01, GOA01a, He96]
Inferred from experimentInferred by computational analysisGO:0004165 - dodecenoyl-CoA delta-isomerase activity [GOA06, GOA01, GOA01a, Pramanik79]
Inferred from experimentInferred by computational analysisGO:0004300 - enoyl-CoA hydratase activity [GOA06, GOA01, GOA01a, Yang93]
Inferred from experimentInferred by computational analysisGO:0008692 - 3-hydroxybutyryl-CoA epimerase activity [GOA06, GOA01, GOA01a, Yang93]
Inferred by computational analysisGO:0003824 - catalytic activity [UniProtGOA11a, GOA01a]
Inferred by computational analysisGO:0016491 - oxidoreductase activity [UniProtGOA11a, GOA01a]
Inferred by computational analysisGO:0016829 - lyase activity [UniProtGOA11a]
Inferred by computational analysisGO:0016853 - isomerase activity [UniProtGOA11a]
Cellular Component:
GO:0005829 - cytosol []
Inferred by computational analysisGO:0036125 - fatty acid beta-oxidation multienzyme complex [GOA01a]

MultiFun Terms: metabolismcarbon utilizationfatty acids

Credits:
Imported from EcoCyc 15-Mar-2016 by Paley S, SRI International


Enzymatic reaction of: 3-hydroxyacyl-CoA dehydrogenase (fatty acid oxidation complex, α component)

Inferred from experiment

(S)-3-hydroxy-(5Z)-tetradecenoyl-CoA + NAD+ → 3-oxo-(5Z)-tetradecenoyl-CoA + NADH + H+

The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the direction in which it was curated.

The reaction is physiologically favored in the direction shown.

Credits:
Imported from EcoCyc 15-Mar-2016 by Paley S, SRI International

Summary:
Experimental work reported by [Ren04a] was conducted using E. coli strain B.


Enzymatic reaction of: 3-hydroxybutyryl-CoA epimerase (fatty acid oxidation complex, α component)

Inferred from experiment

Synonyms: 3-hydroxyacyl-CoA epimerase, 3-hydroxybutanoyl-CoA 3-epimerase

a (3R)-3-hydroxyacyl-CoA ⇄ a (3S)-3-hydroxyacyl-CoA

The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the direction of enzyme catalysis.

This reaction is reversible.

Alternative Substrates [ Comment 1]:

In Pathways: fatty acid β-oxidation I

Credits:
Imported from EcoCyc 15-Mar-2016 by Paley S, SRI International

Summary:
This enzyme is part of a multienzyme complex that has broad substrate specificity. It is also part of a multifunctional polypeptide coded for by the fadB gene. This enzyme is required to feed some unsaturated fatty acids into the β-oxidation pathway. [Pramanik79] The active site for this reaction is also involved in the hydratase reaction (EC 4.2.1.17).

Regulators of Unknown Type: iodoacetamide [Yang83], tris-hydrochloride [Pramanik79]

Enzymatic reaction of: 3-hydroxyacyl-CoA dehydrogenase (fatty acid oxidation complex, α component)

Inferred from experiment

Synonyms: β-hydroxyacyl dehydrogenase, β-keto-reductase, (S)-3-hydroxyacyl-CoA:NAD+ oxidoreductase

EC Number: 1.1.1.35

a (3S)-3-hydroxyacyl-CoA + NAD+ → a 3-oxoacyl-CoA + NADH + H+

The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the direction in which it was curated.

This reaction is reversible.

Alternative Substrates for a (3S)-3-hydroxyacyl-CoA: a S-3-hydroxyacyl-N-acylthioethanolamine, a S-3-hydroxyacylhydrolipoate

In Pathways: photosynthetic 3-hydroxybutanoate biosynthesis (engineered), pyruvate fermentation to hexanol (engineered), pyruvate fermentation to butanol II (engineered), (R)- and (S)-3-hydroxybutanoate biosynthesis (engineered), fatty acid β-oxidation I, methyl ketone biosynthesis (engineered)

Credits:
Imported from EcoCyc 15-Mar-2016 by Paley S, SRI International

Summary:
This enzyme is part of a multienzyme complex that has broad substrate specificity. It is also part of a multifunctional polypeptide coded for by the fadB gene. This enzyme takes part in the oxidation of saturated fatty acids. It exhibits the highest activity with medium-chain substrates. [Binstock81] It also oxidizes S-3-hydroxyacyl-N-acylthioethanolamine and S-3-hydroxyacylhydrolipoate.

Regulators of Unknown Type: iodoacetamide [Yang83], tris-hydrochloride [Pramanik79]

Enzymatic reaction of: enoyl-CoA hydratase (fatty acid oxidation complex, α component)

Inferred from experiment

Synonyms: enoyl hydrase, unsaturated acyl-CoA hydratase, (3S)-3-hydroxyacyl-CoA hydro-lyase

a (3S)-3-hydroxyacyl-CoA ← a trans-2-enoyl-CoA + H2O

The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the Enzyme Commission system.

The reaction is physiologically favored in the opposite direction.

(S)-3-hydroxy-(5Z)-tetradecenoyl-CoA ← (2E,5Z)-tetradecenoyl-CoA + H2O

The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the Enzyme Commission system.

The reaction is favored in the opposite direction.

Alternative Substrates [ Comment 1]:

In Pathways: pyruvate fermentation to hexanol (engineered), pyruvate fermentation to butanol II (engineered), oleate β-oxidation, fatty acid β-oxidation I, methyl ketone biosynthesis (engineered)

Credits:
Imported from EcoCyc 15-Mar-2016 by Paley S, SRI International

Summary:
This enzyme, a crotonase, is part of a multienzyme complex that has broad substrate specificity. It is also part of a multifunctional polypeptide coded for by the fadB gene. This enzyme takes part in the oxidation of saturated fatty acids. The enzyme is active with substrates of varying chain lengths. [Binstock81] The active site also catalyzes epimerization of unsaturated fatty acids (EC 5.1.2.3). [Yang93]

Regulators of Unknown Type: iodoacetamide [Yang83], tris-hydrochloride [Pramanik79]

Enzymatic reaction of: Δ3-cis-Δ2-trans-enoyl-CoA isomerase (fatty acid oxidation complex, α component)

Inferred from experiment

Synonyms: dodecenoyl-CoA δ-isomerase, enoyl-CoA δ-isomerase, acetylene-allene isomerase, dodecenoyl-CoA δ(3)-cis-δ(2)-trans-isomerase

a cis-3-enoyl-CoA ⇄ a trans-2-enoyl-CoA

The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the direction of enzyme catalysis.

This reaction is reversible.

(2E,5Z)-tetradecenoyl-CoA ⇄ 3-trans,5-cis-tetradecadienoyl-CoA

The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the direction of enzyme catalysis.

This reaction is reversible.

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

Credits:
Imported from EcoCyc 15-Mar-2016 by Paley S, SRI International

Summary:
This enzyme is part of a multienzyme complex that has broad substrate specificity. It is also part of a multifunctional polypeptide coded for by the fadB gene. This enzyme is required when carbons 3,4 unsaturated fatty acids are degraded. [Pramanik79] It also catalyses the interconversion of 3-acetylenic fatty acyl thioesters and (+)-2,3-dienoyl fatty acyl thioesters, with fatty acid chain lengths C(6) to C(12).

Regulators of Unknown Type: N-ethylmaleimide [Pawar81], iodoacetamide [Yang83], tris-hydrochloride [Pramanik79]

Subunit of: aerobic fatty acid oxidation complex

Species: Escherichia coli K-12 substr. MG1655

Subunit composition of aerobic fatty acid oxidation complex = [(FadB)2][(FadA)2]
         fatty acid oxidation complex, α component = (FadB)2 (summary available)
                 dodecenoyl-CoA δ-isomerase, enoyl-CoA hydratase, 3-hydroxybutyryl-CoA epimerase, 3-hydroxyacyl-CoA dehydrogenase = FadB
         fatty acid oxidation complex, β component = (FadA)2
                 3-ketoacyl-CoA thiolase = FadA

Credits:
Imported from EcoCyc 15-Mar-2016 by Paley S, SRI International


Sequence Features

Feature Class Location Attached Group Citations Comment
Protein-Segment 1 -> 189  
Author statement[UniProt15]
UniProt: Enoyl-CoA hydratase/isomerase; Sequence Annotation Type: region of interest.
Mutagenesis-Variant 116  
Inferred from experiment[Yang93]
UniProt: Absence of both enoyl-CoA hydratase and 3-hydroxyacyl-CoA epimerase activities. Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase is only slightly affected.
Amino-Acid-Site 119  
Inferred by computational analysis[UniProt15]
UniProt: Important for catalytic activity; Sequence Annotation Type: site.
Amino-Acid-Site 139  
Inferred by computational analysis[UniProt15]
UniProt: Important for catalytic activity; Sequence Annotation Type: site.
Amino-Acid-Sites-That-Bind 296  
Inferred by computational analysis[UniProt15]
UniProt: Substrate.
Protein-Segment 311 -> 729  
Author statement[UniProt15]
UniProt: 3-hydroxyacyl-CoA dehydrogenase; Sequence Annotation Type: region of interest.
Mutagenesis-Variant 322  
Inferred from experiment[He96]
UniProt: 10-fold increase in KM for NADH.
Amino-Acid-Sites-That-Bind 324  
Inferred by curator[UniProt15]
UniProt: NAD; via amide nitrogen.
Amino-Acid-Sites-That-Bind 343  
Inferred by computational analysis[UniProt15]
UniProt: NAD.
Nucleotide-Phosphate-Binding-Region 400 -> 402 NAD+
Inferred by computational analysis[UniProt15]
UniProt: NAD.
Amino-Acid-Sites-That-Bind 407  
Inferred by computational analysis[UniProt15]
UniProt: NAD.
Nucleotide-Phosphate-Binding-Region 427 -> 429 NAD+
Inferred by computational analysis[UniProt15]
UniProt: NAD.
Mutagenesis-Variant 450  
Inferred from experiment[He96]
A or Q: Almost complete loss of 3-hydroxyacyl-CoA dehydrogenase activity.
Active-Site 450  
Inferred from experiment[He96, Yang93]
UniProt: For 3-hydroxyacyl-CoA dehydrogenase activity.
Amino-Acid-Sites-That-Bind 453  
Inferred by computational analysis[UniProt15]
UniProt: NAD.
Amino-Acid-Sites-That-Bind 500  
Inferred by computational analysis[UniProt15]
UniProt: Substrate.
Sequence-Conflict 518  
Inferred by curator[DiRusso90, UniProt15]
UniProt: (in Ref. 1; AAA23750).
Amino-Acid-Sites-That-Bind 660  
Inferred by computational analysis[UniProt15]
UniProt: Substrate.
Sequence-Conflict 664  
Inferred by curator[Nakahigashi90, UniProt15]
UniProt: (in Ref. 3; CAB40809).
Sequence-Conflict 666  
Inferred by curator[Nakahigashi90, UniProt15]
UniProt: (in Ref. 3; CAB40809).


Sequence Pfam Features

Feature Class Location Citations Comment
Pfam PF00378 14 -> 205
Inferred by computational analysis[Finn14]
ECH_1 : Enoyl-CoA hydratase/isomerase [More...]
Pfam PF02737 316 -> 494
Inferred by computational analysis[Finn14]
3HCDH_N : 3-hydroxyacyl-CoA dehydrogenase, NAD binding domain [More...]
Pfam PF00725 496 -> 592
Inferred by computational analysis[Finn14]
3HCDH : 3-hydroxyacyl-CoA dehydrogenase, C-terminal domain [More...]
Pfam PF00725 627 -> 690
Inferred by computational analysis[Finn14]
3HCDH : 3-hydroxyacyl-CoA dehydrogenase, C-terminal domain [More...]


References

Binstock81: Binstock JF, Schulz H (1981). "Fatty acid oxidation complex from Escherichia coli." Methods Enzymol 1981;71 Pt C;403-11. PMID: 7024730

DiRusso90: DiRusso CC (1990). "Primary sequence of the Escherichia coli fadBA operon, encoding the fatty acid-oxidizing multienzyme complex, indicates a high degree of homology to eucaryotic enzymes." J Bacteriol 172(11);6459-68. PMID: 1699931

Finn14: Finn RD, Bateman A, Clements J, Coggill P, Eberhardt RY, Eddy SR, Heger A, Hetherington K, Holm L, Mistry J, Sonnhammer EL, Tate J, Punta M (2014). "Pfam: the protein families database." Nucleic Acids Res 42(Database issue);D222-30. PMID: 24288371

GOA01: GOA, MGI (2001). "Gene Ontology annotation based on Enzyme Commission mapping." Genomics 74;121-128.

GOA01a: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

GOA06: GOA, SIB (2006). "Electronic Gene Ontology annotations created by transferring manual GO annotations between orthologous microbial proteins."

He96: He XY, Yang SY (1996). "Histidine-450 is the catalytic residue of L-3-hydroxyacyl coenzyme A dehydrogenase associated with the large alpha-subunit of the multienzyme complex of fatty acid oxidation from Escherichia coli." Biochemistry 1996;35(29);9625-30. PMID: 8755745

Nakahigashi90: Nakahigashi K, Inokuchi H (1990). "Nucleotide sequence of the fadA and fadB genes from Escherichia coli." Nucleic Acids Res 18(16);4937. PMID: 2204034

Pawar81: Pawar S, Schulz H (1981). "The structure of the multienzyme complex of fatty acid oxidation from Escherichia coli." J Biol Chem 1981;256(8);3894-9. PMID: 7012144

Pramanik79: Pramanik A, Pawar S, Antonian E, Schulz H (1979). "Five different enzymatic activities are associated with the multienzyme complex of fatty acid oxidation from Escherichia coli." J Bacteriol 1979;137(1);469-73. PMID: 368024

Ren04a: Ren Y, Aguirre J, Ntamack AG, Chu C, Schulz H (2004). "An alternative pathway of oleate beta-oxidation in Escherichia coli involving the hydrolysis of a dead end intermediate by a thioesterase." J Biol Chem 279(12);11042-50. PMID: 14707139

UniProt15: UniProt Consortium (2015). "UniProt version 2015-08 released on 2015-07-22." Database.

UniProtGOA11a: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."

UniProtGOA12: UniProt-GOA (2012). "Gene Ontology annotation based on UniPathway vocabulary mapping."

Yang83: Yang SY, Schulz H (1983). "The large subunit of the fatty acid oxidation complex from Escherichia coli is a multifunctional polypeptide. Evidence for the existence of a fatty acid oxidation operon (fad AB) in Escherichia coli." J Biol Chem 1983;258(16);9780-5. PMID: 6350283

Yang91a: Yang XY, Schulz H, Elzinga M, Yang SY (1991). "Nucleotide sequence of the promoter and fadB gene of the fadBA operon and primary structure of the multifunctional fatty acid oxidation protein from Escherichia coli." Biochemistry 1991;30(27);6788-95. PMID: 1712230

Yang93: Yang SY, Elzinga M (1993). "Association of both enoyl coenzyme A hydratase and 3-hydroxyacyl coenzyme A epimerase with an active site in the amino-terminal domain of the multifunctional fatty acid oxidation protein from Escherichia coli." J Biol Chem 1993;268(9);6588-92. PMID: 8454629

Yang95: Yang SY, He XY, Schulz H (1995). "Glutamate 139 of the large alpha-subunit is the catalytic base in the dehydration of both D- and L-3-hydroxyacyl-coenzyme A but not in the isomerization of delta 3, delta 2-enoyl-coenzyme A catalyzed by the multienzyme complex of fatty acid oxidation from Escherichia coli." Biochemistry 1995;34(19);6441-7. PMID: 7756275


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
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