DB code: T00008

CATH domain 1.10.540.10 : Butyryl-Coa Dehydrogenase, subunit A; domain 1
2.40.110.10 : Butyryl-CoA Dehydrogenase, subunit A; domain 2
1.20.140.10 : Butyryl-CoA Dehydrogenase, subunit A; domain 3 Catalytic domain
E.C. 1.3.8.7
CSA 3mdd
M-CSA 3mdd
MACiE

CATH domain Related DB codes (homologues)
1.10.540.10 : Butyryl-Coa Dehydrogenase, subunit A; domain 1 T00007 T00009
1.20.140.10 : Butyryl-CoA Dehydrogenase, subunit A; domain 3 T00007 T00009
2.40.110.10 : Butyryl-CoA Dehydrogenase, subunit A; domain 2 T00007 T00009

Uniprot Enzyme Name
UniprotKB Protein name Synonyms RefSeq Pfam
Q72JJ3
Putative acyl-CoA dehydrogenase
EC 1.3.99.-
YP_004752.1 (Protein)
NC_005835.1 (DNA/RNA sequence)
PF00441 (Acyl-CoA_dh_1)
PF02770 (Acyl-CoA_dh_M)
PF02771 (Acyl-CoA_dh_N)
[Graphical View]
Q5SGZ2
Acyl-CoA dehydrogenase
YP_145204.1 (Protein)
NC_006461.1 (DNA/RNA sequence)
PF00441 (Acyl-CoA_dh_1)
PF02770 (Acyl-CoA_dh_M)
PF02771 (Acyl-CoA_dh_N)
[Graphical View]
P41367 Medium-chain specific acyl-CoA dehydrogenase, mitochondrial
MCAD
EC 1.3.99.3
NP_999204.1 (Protein)
NM_214039.1 (DNA/RNA sequence)
PF00441 (Acyl-CoA_dh_1)
PF02770 (Acyl-CoA_dh_M)
PF02771 (Acyl-CoA_dh_N)
[Graphical View]
P11310 Medium-chain specific acyl-CoA dehydrogenase, mitochondrial
MCAD
EC 1.3.99.3
NP_000007.1 (Protein)
NM_000016.4 (DNA/RNA sequence)
NP_001120800.1 (Protein)
NM_001127328.1 (DNA/RNA sequence)
PF00441 (Acyl-CoA_dh_1)
PF02770 (Acyl-CoA_dh_M)
PF02771 (Acyl-CoA_dh_N)
[Graphical View]

KEGG enzyme name
medium-chain acyl-CoA dehydrogenase
fatty acyl coenzyme A dehydrogenase (ambiguous)
acyl coenzyme A dehydrogenase (ambiguous)
acyl dehydrogenase (ambiguous)
fatty-acyl-CoA dehydrogenase (ambiguous)
acyl CoA dehydrogenase (ambiguous)
general acyl CoA dehydrogenase (ambiguous)
medium-chain acyl-coenzyme A dehydrogenase
acyl-CoA:(acceptor) 2,3-oxidoreductase (ambiguous)
ACADM (gene name)

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
Q72JJ3 Q72JJ3_THET2
Q5SGZ2 Q5SGZ2_THET8
P41367 ACADM_PIG A medium-chain acyl-CoA + electron-transfer flavoprotein = a medium-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein. Homotetramer. Mitochondrion matrix. FAD.
P11310 ACADM_HUMAN A medium-chain acyl-CoA + electron-transfer flavoprotein = a medium-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein. Homotetramer. Interacts with the heterodimeric electron transfer flavoprotein ETF. Mitochondrion matrix. FAD.

KEGG Pathways
Map code Pathways E.C.
MAP00071 Fatty acid metabolism
MAP00280 Valine, leucine and isoleucine degradation
MAP00410 beta-Alanine metabolism
MAP00640 Propanoate metabolism

Compound table
Cofactors Substrates Products Intermediates
KEGG-id C00016 C00040 C04253 C00605 C04570
E.C.
Compound FAD Acyl-CoA Electron-transferring flavoprotein 2,3-Dehydroacyl-CoA Reduced electron-transferring flavoprotein
Type amide group,amine group,aromatic ring (only carbon atom),aromatic ring (with nitrogen atoms),carbohydrate,nucleotide amine group,carbohydrate,nucleotide ,peptide/protein,sulfide group amide group,amine group,aromatic ring (only carbon atom),aromatic ring (with nitrogen atoms),carbohydrate,peptide/protein,phosphate group/phosphate ion amine group,carbohydrate,nucleotide ,peptide/protein,sulfide group amide group,amine group,aromatic ring (only carbon atom),aromatic ring (with nitrogen atoms),carbohydrate,peptide/protein,phosphate group/phosphate ion
ChEBI 16238
16238
PubChem 643975
643975
1ukwA01 Unbound Unbound Unbound Unbound Unbound
1ukwB01 Unbound Unbound Unbound Unbound Unbound
2cx9A01 Unbound Unbound Unbound Unbound Unbound
2cx9B01 Unbound Unbound Unbound Unbound Unbound
2cx9C01 Unbound Unbound Unbound Unbound Unbound
2cx9D01 Unbound Unbound Unbound Unbound Unbound
1udyA01 Unbound Unbound Unbound Unbound Unbound
1udyB01 Unbound Unbound Unbound Unbound Unbound
1udyC01 Unbound Unbound Unbound Unbound Unbound
1udyD01 Unbound Unbound Unbound Unbound Unbound
3mddA01 Unbound Unbound Unbound Unbound Unbound
3mddB01 Unbound Unbound Unbound Unbound Unbound
3mdeA01 Unbound Unbound Unbound Unbound Unbound
3mdeB01 Unbound Unbound Unbound Unbound Unbound
1egcA01 Unbound Unbound Unbound Unbound Unbound
1egcB01 Unbound Unbound Unbound Unbound Unbound
1egcC01 Unbound Unbound Unbound Unbound Unbound
1egcD01 Unbound Unbound Unbound Unbound Unbound
1egdA01 Unbound Unbound Unbound Unbound Unbound
1egdB01 Unbound Unbound Unbound Unbound Unbound
1egdC01 Unbound Unbound Unbound Unbound Unbound
1egdD01 Unbound Unbound Unbound Unbound Unbound
1egeA01 Unbound Unbound Unbound Unbound Unbound
1egeB01 Unbound Unbound Unbound Unbound Unbound
1egeC01 Unbound Unbound Unbound Unbound Unbound
1egeD01 Unbound Unbound Unbound Unbound Unbound
1t9gA01 Unbound Unbound Unbound Unbound Unbound
1t9gB01 Unbound Unbound Unbound Unbound Unbound
1t9gC01 Unbound Unbound Unbound Unbound Unbound
1t9gD01 Unbound Unbound Bound:TYR_192-ALA_193-THR_194-LEU_195 (chain S) Unbound Unbound
2a1tA01 Unbound Unbound Unbound Unbound Unbound
2a1tB01 Unbound Unbound Unbound Unbound Unbound
2a1tC01 Unbound Unbound Unbound Unbound Unbound
2a1tD01 Unbound Unbound Bound:TYR_192-ALA_193-THR_194-LEU_195 (chain S) Unbound Unbound
1ukwA02 Bound:FAD Unbound Unbound Unbound Unbound
1ukwB02 Bound:FAD Unbound Unbound Unbound Unbound
2cx9A02 Unbound Unbound Unbound Unbound Unbound
2cx9B02 Unbound Unbound Unbound Unbound Unbound
2cx9C02 Unbound Unbound Unbound Unbound Unbound
2cx9D02 Unbound Unbound Unbound Unbound Unbound
1udyA02 Bound:FAD Unbound Unbound Unbound Unbound
1udyB02 Bound:FAD Unbound Unbound Unbound Unbound
1udyC02 Bound:FAD Unbound Unbound Unbound Unbound
1udyD02 Bound:FAD Unbound Unbound Unbound Unbound
3mddA02 Bound:FAD Unbound Unbound Unbound Unbound
3mddB02 Bound:FAD Unbound Unbound Unbound Unbound
3mdeA02 Bound:FAD Unbound Unbound Unbound Unbound
3mdeB02 Bound:FAD Unbound Unbound Unbound Unbound
1egcA02 Bound:FAD Unbound Unbound Unbound Unbound
1egcB02 Bound:FAD Unbound Unbound Unbound Unbound
1egcC02 Bound:FAD Unbound Unbound Unbound Unbound
1egcD02 Bound:FAD Unbound Unbound Unbound Unbound
1egdA02 Bound:FAD Unbound Unbound Unbound Unbound
1egdB02 Bound:FAD Unbound Unbound Unbound Unbound
1egdC02 Bound:FAD Unbound Unbound Unbound Unbound
1egdD02 Bound:FAD Unbound Unbound Unbound Unbound
1egeA02 Bound:FAD Unbound Unbound Unbound Unbound
1egeB02 Bound:FAD Unbound Unbound Unbound Unbound
1egeC02 Bound:FAD Unbound Unbound Unbound Unbound
1egeD02 Bound:FAD Unbound Unbound Unbound Unbound
1t9gA02 Bound:FAD Unbound Unbound Unbound Unbound
1t9gB02 Bound:FAD Unbound Unbound Unbound Unbound
1t9gC02 Bound:FAD Unbound Unbound Unbound Unbound
1t9gD02 Bound:FAD Unbound Unbound Unbound Unbound
2a1tA02 Bound:FAD Unbound Unbound Unbound Unbound
2a1tB02 Bound:FAD Unbound Unbound Unbound Unbound
2a1tC02 Bound:FAD Unbound Bound:FAD(chain R) Unbound Unbound
2a1tD02 Bound:FAD Unbound Unbound Unbound Unbound
1ukwA03 Unbound Unbound Unbound Unbound Unbound
1ukwB03 Unbound Unbound Unbound Unbound Unbound
2cx9A03 Unbound Unbound Unbound Unbound Unbound
2cx9B03 Unbound Unbound Unbound Unbound Unbound
2cx9C03 Unbound Unbound Unbound Unbound Unbound
2cx9D03 Unbound Unbound Unbound Unbound Unbound
1udyA03 Unbound Analogue:CS8 Unbound Unbound Unbound
1udyB03 Unbound Analogue:CS8 Unbound Unbound Unbound
1udyC03 Unbound Analogue:CS8 Unbound Unbound Unbound
1udyD03 Unbound Analogue:CS8 Unbound Unbound Unbound
3mddA03 Unbound Unbound Unbound Unbound Unbound
3mddB03 Unbound Unbound Unbound Unbound Unbound
3mdeA03 Unbound Bound:CO8 Unbound Unbound Unbound
3mdeB03 Unbound Bound:CO8 Unbound Unbound Unbound
1egcA03 Unbound Bound:CO8 Unbound Unbound Unbound
1egcB03 Unbound Bound:CO8 Unbound Unbound Unbound
1egcC03 Unbound Bound:CO8 Unbound Unbound Unbound
1egcD03 Unbound Bound:CO8 Unbound Unbound Unbound
1egdA03 Unbound Unbound Unbound Unbound Unbound
1egdB03 Unbound Unbound Unbound Unbound Unbound
1egdC03 Unbound Unbound Unbound Unbound Unbound
1egdD03 Unbound Unbound Unbound Unbound Unbound
1egeA03 Unbound Unbound Unbound Unbound Unbound
1egeB03 Unbound Unbound Unbound Unbound Unbound
1egeC03 Unbound Unbound Unbound Unbound Unbound
1egeD03 Unbound Unbound Unbound Unbound Unbound
1t9gA03 Unbound Unbound Unbound Unbound Unbound
1t9gB03 Unbound Unbound Unbound Unbound Unbound
1t9gC03 Unbound Unbound Unbound Unbound Unbound
1t9gD03 Unbound Unbound Unbound Unbound Unbound
2a1tA03 Unbound Unbound Unbound Unbound Unbound
2a1tB03 Unbound Unbound Unbound Unbound Unbound
2a1tC03 Unbound Unbound Unbound Unbound Unbound
2a1tD03 Unbound Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
PDB;1egc, 1egd, 1ege, 3mde & Swiss-prot;P11310, P41367 & literature [6], [15], [21], [24], [32], [35], [39], [54]

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1ukwA01
1ukwB01
2cx9A01
2cx9B01
2cx9C01
2cx9D01
1udyA01
1udyB01
1udyC01
1udyD01
3mddA01
3mddB01
3mdeA01
3mdeB01
1egcA01
1egcB01
1egcC01
1egcD01
1egdA01
1egdB01
1egdC01
1egdD01
1egeA01
1egeB01
1egeC01
1egeD01
1t9gA01
1t9gB01
1t9gC01
1t9gD01
2a1tA01
2a1tB01
2a1tC01
2a1tD01
1ukwA02
1ukwB02
2cx9A02
2cx9B02
2cx9C02
2cx9D02
1udyA02
1udyB02
1udyC02
1udyD02
3mddA02
3mddB02
3mdeA02
3mdeB02
1egcA02
1egcB02
1egcC02
1egcD02
1egdA02
1egdB02
1egdC02
1egdD02
1egeA02
1egeB02
1egeC02
1egeD02
1t9gA02
1t9gB02
1t9gC02
1t9gD02
2a1tA02
2a1tB02
2a1tC02
2a1tD02
1ukwA03 GLU 393 GLU 393
1ukwB03 GLU 393 GLU 393
2cx9A03 GLU 369 GLU 369
2cx9B03 GLU 369 GLU 369
2cx9C03 GLU 369 GLU 369
2cx9D03 GLU 369 GLU 369
1udyA03 GLU 376 GLU 376
1udyB03 GLU 376 GLU 376
1udyC03 GLU 376 GLU 376
1udyD03 GLU 376 GLU 376
3mddA03 GLU 376 GLU 376
3mddB03 GLU 376 GLU 376
3mdeA03 GLU 376 GLU 376
3mdeB03 GLU 376 GLU 376
1egcA03 mutant T255E, E376G
1egcB03 mutant T255E, E376G
1egcC03 mutant T255E, E376G
1egcD03 mutant T255E, E376G
1egdA03 mutant T255E, E376G
1egdB03 mutant T255E, E376G
1egdC03 mutant T255E, E376G
1egdD03 mutant T255E, E376G
1egeA03 GLU 376 GLU 376 mutant T255E
1egeB03 GLU 376 GLU 376 mutant T255E
1egeC03 GLU 376 GLU 376 mutant T255E
1egeD03 GLU 376 GLU 376 mutant T255E
1t9gA03 GLU 376 GLU 376
1t9gB03 GLU 376 GLU 376
1t9gC03 GLU 376 GLU 376
1t9gD03 GLU 376 GLU 376
2a1tA03 GLU 376 GLU 376
2a1tB03 GLU 376 GLU 376
2a1tC03 GLU 376 GLU 376
2a1tD03 GLU 376 GLU 376

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[1]
Scheme 2
[4]
p.417
[15]
p.7525-7527
[19]
Scheme 1
[21]
Scheme 3, p.719, p.722-723
[22]
Fig.10, Fig.11, p.805-807
[24]
p.12417-12420
[30]
Scheme 1
[31]
Fig.4, p.14609-14612
[32]
p.1701-1704
[35]
Scheme 1, Scheme 2, Scheme 5, p.8443-8444
[36]
p.8454
[37]
Scheme 1, p.1856-1860
[38]
Fig.1, Fig.3
[39]
Fig.1, p.226
[40]
Scheme 4, p.264-266
[41]
Scheme 1, Fig.7
[42]
Scheme 2, p.13989-13991
[45]
Scheme 1
[50]
Scheme 1, p.4638
[50]
Fig.8, p.4645-4647
[53]
Scheme 1, Scheme 2, p.11852-11855
[54]
p.301-303
[55]
p.488-491
[56]
[58]
Fig.5

References
[1]
Resource
Comments
Medline ID
PubMed ID 3968064
Journal J Biol Chem
Year 1985
Volume 260
Pages 1326-37
Authors Ikeda Y, Hine DG, Okamura-Ikeda K, Tanaka K
Title Mechanism of action of short-chain, medium-chain, and long-chain acyl-CoA dehydrogenases. Direct evidence for carbanion formation as an intermediate step using enzyme-catalyzed C-2 proton/deuteron exchange in the absence of C-3 exchange.
Related PDB
Related UniProtKB
[2]
Resource
Comments
Medline ID
PubMed ID 3769916
Journal Eur J Biochem
Year 1986
Volume 160
Pages 109-15
Authors Pohl B, Raichle T, Ghisla S
Title Studies on the reaction mechanism of general acyl-CoA dehydrogenase. Determination of selective isotope effects in the dehydrogenation of butyryl-CoA.
Related PDB
Related UniProtKB
[3]
Resource
Comments
Medline ID
PubMed ID 3115254
Journal Biochem J
Year 1987
Volume 243
Pages 519-24
Authors Steenkamp DJ
Title Preferential cross-linking of the small subunit of the electron-transfer flavoprotein to general acyl-CoA dehydrogenase.
Related PDB
Related UniProtKB
[4]
Resource
Comments
Medline ID
PubMed ID 3053288
Journal Biochem Soc Trans
Year 1988
Volume 16
Pages 416-8
Authors Frerman FE
Title Acyl-CoA dehydrogenases, electron transfer flavoprotein and electron transfer flavoprotein dehydrogenase.
Related PDB
Related UniProtKB
[5]
Resource
Comments
Medline ID
PubMed ID 3413116
Journal Proc Natl Acad Sci U S A
Year 1988
Volume 85
Pages 6677-81
Authors Kim JJ, Wu J
Title Structure of the medium-chain acyl-CoA dehydrogenase from pig liver mitochondria at 3-A resolution.
Related PDB
Related UniProtKB
[6]
Resource
Comments
Medline ID
PubMed ID 1970566
Journal J Biol Chem
Year 1990
Volume 265
Pages 7116-9
Authors Bross P, Engst S, Strauss AW, Kelly DP, Rasched I, Ghisla S
Title Characterization of wild-type and an active site mutant of human medium chain acyl-CoA dehydrogenase after expression in Escherichia coli.
Related PDB
Related UniProtKB
[7]
Resource
Comments VARIANT MCAD GLU-329.
Medline ID 91067682
PubMed ID 2251268
Journal Proc Natl Acad Sci U S A
Year 1990
Volume 87
Pages 9236-40
Authors Kelly DP, Whelan AJ, Ogden ML, Alpers R, Zhang ZF, Bellus G, Gregersen N, Dorland L, Strauss AW
Title Molecular characterization of inherited medium-chain acyl-CoA dehydrogenase deficiency.
Related PDB
Related UniProtKB P11310
[8]
Resource
Comments
Medline ID
PubMed ID 2326312
Journal Prog Clin Biol Res
Year 1990
Volume 321
Pages 569-76
Authors Kim JJ, Wu J
Title Structural studies of medium-chain acyl-CoA dehydrogenase from pig liver mitochondria.
Related PDB
Related UniProtKB
[9]
Resource
Comments T00007-5
Medline ID
PubMed ID 1931995
Journal Biochemistry
Year 1991
Volume 30
Pages 10755-60
Authors Tserng KY, Jin SJ, Hoppel CL
Title Spiropentaneacetic acid as a specific inhibitor of medium-chain acyl-CoA dehydrogenase.
Related PDB
Related UniProtKB
[10]
Resource
Comments VARIANT MCAD GLU-329.
Medline ID 91224627
PubMed ID 1902818
Journal Hum Genet
Year 1991
Volume 86
Pages 545-51
Authors Gregersen N, Andresen BS, Bross P, Winter V, Rudiger N, Engst S, Christensen E, Kelly D, Strauss AW, Kolvraa S, et al
Title Molecular characterization of medium-chain acyl-CoA dehydrogenase (MCAD) deficiency: identification of a lys329 to glu mutation in the MCAD gene, and expression of inactive mutant enzyme protein in E. coli.
Related PDB
Related UniProtKB P11310
[11]
Resource
Comments T00007-6
Medline ID
PubMed ID 8102510
Journal Am J Hum Genet
Year 1993
Volume 53
Pages 730-9
Authors Andresen BS, Bross P, Jensen TG, Winter V, Knudsen I, Kolvraa S, Jensen UB, Bolund L, Duran M, Kim JJ, et al
Title A rare disease-associated mutation in the medium-chain acyl-CoA dehydrogenase (MCAD) gene changes a conserved arginine, previously shown to be functionally essential in short-chain acyl-CoA dehydrogenase (SCAD).
Related PDB
Related UniProtKB
[12]
Resource
Comments
Medline ID
PubMed ID 8218225
Journal Biochemistry
Year 1993
Volume 32
Pages 11575-85
Authors Johnson JK, Kumar NR, Srivastava DK
Title Microscopic pathway for the medium-chain fatty acyl CoA dehydrogenase catalyzed oxidative half-reaction: changes in the electronic structures of flavin and CoA derivatives during catalysis.
Related PDB
Related UniProtKB
[13]
Resource
Comments
Medline ID
PubMed ID 8267794
Journal Biochemistry
Year 1993
Volume 32
Pages 8004-13
Authors Johnson JK, Srivastava DK
Title Detection and identification of a chromophoric intermediate during the medium-chain fatty acyl-CoA dehydrogenase-catalyzed reaction via rapid-scanning UV/visible spectroscopy.
Related PDB
Related UniProtKB
[14]
Resource
Comments
Medline ID
PubMed ID 8454567
Journal J Biochem (Tokyo)
Year 1993
Volume 113
Pages 106-13
Authors Miura R, Nishina Y, Sato K, Fujii S, Kuroda K, Shiga K
Title 13C- and 15N-NMR studies on medium-chain acyl-CoA dehydrogenase reconstituted with 13C- and 15N-enriched flavin adenine dinucleotide.
Related PDB
Related UniProtKB
[15]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
Medline ID 93361479
PubMed ID 8356049
Journal Proc Natl Acad Sci U S A
Year 1993
Volume 90
Pages 7523-7
Authors Kim JJ, Wang M, Paschke R
Title Crystal structures of medium-chain acyl-CoA dehydrogenase from pig liver mitochondria with and without substrate.
Related PDB 3mdd 3mde
Related UniProtKB P41367
[16]
Resource
Comments
Medline ID
PubMed ID 8161532
Journal Biochemistry
Year 1994
Volume 33
Pages 4738-44
Authors Johnson JK, Kumar NR, Srivastava DK
Title Molecular basis of the medium-chain fatty acyl-CoA dehydrogenase-catalyzed "oxidase" reaction: pH-dependent distribution of intermediary enzyme species during catalysis.
Related PDB
Related UniProtKB
[17]
Resource
Comments
Medline ID
PubMed ID 7905878
Journal J Biol Chem
Year 1994
Volume 269
Pages 4401-8
Authors Saijo T, Welch WJ, Tanaka K
Title Intramitochondrial folding and assembly of medium-chain acyl-CoA dehydrogenase (MCAD). Demonstration of impaired transfer of K304E-variant MCAD from its complex with hsp60 to the native tetramer.
Related PDB
Related UniProtKB
[18]
Resource
Comments
Medline ID
PubMed ID 7703241
Journal Biochemistry
Year 1995
Volume 34
Pages 4276-86
Authors Fitzsimmons ME, Thorpe C, Anders MW
Title Medium-chain acyl-CoA dehydrogenase- and enoyl-CoA hydratase-dependent bioactivation of 5,6-dichloro-4-thia-5-hexenoyl-CoA.
Related PDB
Related UniProtKB
[19]
Resource
Comments
Medline ID
PubMed ID 8845370
Journal Biochemistry
Year 1995
Volume 34
Pages 16424-32
Authors Schaller RA, Thorpe C
Title Oxidative inactivation of a charge transfer complex in the medium-chain acyl-CoA dehydrogenase.
Related PDB
Related UniProtKB
[20]
Resource
Comments
Medline ID
PubMed ID 7718565
Journal Biochemistry
Year 1995
Volume 34
Pages 4625-32
Authors Srivastava DK, Kumar NR, Peterson KL
Title "Dehydrogenase" and "oxidase" reactions of medium-chain fatty acyl-CoA dehydrogenase utilizing chromogenic substrates: role of the 3',5'-adenosine diphosphate moiety of the coenzyme A thioester in catalysis.
Related PDB
Related UniProtKB
[21]
Resource
Comments
Medline ID
PubMed ID 7601336
Journal FASEB J
Year 1995
Volume 9
Pages 718-25
Authors Thorpe C, Kim JJ
Title Structure and mechanism of action of the acyl-CoA dehydrogenases.
Related PDB
Related UniProtKB
[22]
Resource
Comments
Medline ID
PubMed ID 7592542
Journal J Biochem (Tokyo)
Year 1995
Volume 117
Pages 800-8
Authors Nishina Y, Sato K, Hazekawa I, Shiga K
Title Structural modulation of 2-enoyl-CoA bound to reduced acyl-CoA dehydrogenases: a resonance Raman study of a catalytic intermediate.
Related PDB
Related UniProtKB
[23]
Resource
Comments
Medline ID
PubMed ID 7730333
Journal J Biol Chem
Year 1995
Volume 270
Pages 10284-90
Authors Bross P, Jespersen C, Jensen TG, Andresen BS, Kristensen MJ, Winter V, Nandy A, Krautle F, Ghisla S, Bolundi L, et al
Title Effects of two mutations detected in medium chain acyl-CoA dehydrogenase (MCAD)-deficient patients on folding, oligomer assembly, and stability of MCAD enzyme.
Related PDB
Related UniProtKB
[24]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
Medline ID 96420477
PubMed ID 8823176
Journal Biochemistry
Year 1996
Volume 35
Pages 12412-20
Authors Lee HJ, Wang M, Paschke R, Nandy A, Ghisla S, Kim JJ
Title Crystal structures of the wild type and the Glu376Gly/Thr255Glu mutant of human medium-chain acyl-CoA dehydrogenase: influence of the location of the catalytic base on substrate specificity.
Related PDB 1egc 1egd 1ege
Related UniProtKB P11310
[25]
Resource
Comments
Medline ID
PubMed ID 8823175
Journal Biochemistry
Year 1996
Volume 35
Pages 12402-11
Authors Nandy A, Kieweg V, Krautle FG, Vock P, Kuchler B, Bross P, Kim JJ, Rasched I, Ghisla S
Title Medium-long-chain chimeric human Acyl-CoA dehydrogenase: medium-chain enzyme with the active center base arrangement of long-chain Acyl-CoA dehydrogenase.
Related PDB
Related UniProtKB
[26]
Resource
Comments
Medline ID
PubMed ID 9271097
Journal Biochem J
Year 1997
Volume 325
Pages 751-60
Authors Peterson KL, Srivastava DK
Title Functional role of a distal (3'-phosphate) group of CoA in the recombinant human liver medium-chain acyl-CoA dehydrogenase-catalysed reaction.
Related PDB
Related UniProtKB
[27]
Resource
Comments
Medline ID
PubMed ID 9426198
Journal Biol Chem
Year 1997
Volume 378
Pages 1381-5
Authors Macheroux P, Sanner C, Buttner H, Kieweg V, Ruterjans H, Ghisla S
Title Medium-chain acyl CoA dehydrogenase: evidence for phosphorylation.
Related PDB
Related UniProtKB
[28]
Resource
Comments
Medline ID
PubMed ID 9434899
Journal Curr Opin Struct Biol
Year 1997
Volume 7
Pages 804-10
Authors Mattevi A, Vanoni MA, Curti B
Title Structure of D-amino acid oxidase: new insights from an old enzyme.
Related PDB
Related UniProtKB
[29]
Resource
Comments
Medline ID
PubMed ID 9208949
Journal Eur J Biochem
Year 1997
Volume 246
Pages 548-56
Authors Kieweg V, Krautle FG, Nandy A, Engst S, Vock P, Abdel-Ghany AG, Bross P, Gregersen N, Rasched I, Strauss A, Ghisla S
Title Biochemical characterization of purified, human recombinant Lys304-->Glu medium-chain acyl-CoA dehydrogenase containing the common disease-causing mutation and comparison with the normal enzyme.
Related PDB
Related UniProtKB
[30]
Resource
Comments
Medline ID
PubMed ID 9477967
Journal Biochemistry
Year 1998
Volume 37
Pages 1383-93
Authors Baker-Malcolm JF, Haeffner-Gormley L, Wang L, Anders MW, Thorpe C
Title Elimination reactions in the medium-chain acyl-CoA dehydrogenase: bioactivation of cytotoxic 4-thiaalkanoic acids.
Related PDB
Related UniProtKB
[31]
Resource
Comments
Medline ID
PubMed ID 9772189
Journal Biochemistry
Year 1998
Volume 37
Pages 14605-12
Authors Mancini-Samuelson GJ, Kieweg V, Sabaj KM, Ghisla S, Stankovich MT
Title Redox properties of human medium-chain acyl-CoA dehydrogenase, modulation by charged active-site amino acid residues.
Related PDB
Related UniProtKB
[32]
Resource
Comments
Medline ID
PubMed ID 9484241
Journal Biochemistry
Year 1998
Volume 37
Pages 1697-705
Authors Peterson KL, Galitz DS, Srivastava DK
Title Influence of excision of a methylene group from Glu-376 (Glu376-->Asp mutation) in the medium chain acyl-CoA dehydrogenase-catalyzed reaction.
Related PDB
Related UniProtKB
[33]
Resource
Comments
Medline ID
PubMed ID 9730839
Journal Biochemistry
Year 1998
Volume 37
Pages 12659-71
Authors Peterson KL, Peterson KM, Srivastava DK
Title Thermodynamics of ligand binding and catalysis in human liver medium-chain acyl-CoA dehydrogenase: comparative studies involving normal and 3'-dephosphorylated C8-CoAs and wild-type and Asn191 --> Ala (N191A) mutant enzymes.
Related PDB
Related UniProtKB
[34]
Resource
Comments
Medline ID
PubMed ID 9521671
Journal Biochemistry
Year 1998
Volume 37
Pages 3499-508
Authors Qin L, Srivastava DK
Title Energetics of two-step binding of a chromophoric reaction product, trans-3-indoleacryloyl-CoA, to medium-chain acyl-coenzyme-A dehydrogenase.
Related PDB
Related UniProtKB
[35]
Resource
Comments
Medline ID
PubMed ID 9622495
Journal Biochemistry
Year 1998
Volume 37
Pages 8437-45
Authors Rudik I, Ghisla S, Thorpe C
Title Protonic equilibria in the reductive half-reaction of the medium-chain acyl-CoA dehydrogenase.
Related PDB
Related UniProtKB
[36]
Resource
Comments
Medline ID
PubMed ID 9622496
Journal Biochemistry
Year 1998
Volume 37
Pages 8446-56
Authors Srivastava DK, Peterson KL
Title Discriminatory influence of Glu-376-->Asp mutation in medium-chain acyl-CoA dehydrogenase on the binding of selected CoA-ligands: spectroscopic, thermodynamic, kinetic, and model building studies.
Related PDB
Related UniProtKB
[37]
Resource
Comments
Medline ID
PubMed ID 9485310
Journal Biochemistry
Year 1998
Volume 37
Pages 1848-60
Authors Vock P, Engst S, Eder M, Ghisla S
Title Substrate activation by acyl-CoA dehydrogenases: transition-state stabilization and pKs of involved functional groups.
Related PDB
Related UniProtKB
[38]
Resource
Comments
Medline ID
PubMed ID 10496972
Journal Arch Biochem Biophys
Year 1999
Volume 370
Pages 16-21
Authors Stankovich MT, Sabaj KM, Tonge PJ
Title Structure/function of medium chain acyl-CoA dehydrogenase: the importance of substrate polarization.
Related PDB
Related UniProtKB
[39]
Resource
Comments
Medline ID
PubMed ID 9882619
Journal Biochem J
Year 1999
Volume 337
Pages 225-30
Authors Kuchler B, Abdel-Ghany AG, Bross P, Nandy A, Rasched I, Ghisla S
Title Biochemical characterization of a variant human medium-chain acyl-CoA dehydrogenase with a disease-associated mutation localized in the active site.
Related PDB
Related UniProtKB
[40]
Resource
Comments
Medline ID
PubMed ID 9890906
Journal Biochemistry
Year 1999
Volume 38
Pages 257-67
Authors Engst S, Vock P, Wang M, Kim JJ, Ghisla S
Title Mechanism of activation of acyl-CoA substrates by medium chain acyl-CoA dehydrogenase: interaction of the thioester carbonyl with the flavin adenine dinucleotide ribityl side chain.
Related PDB
Related UniProtKB
[41]
Resource
Comments
Medline ID
PubMed ID 9990125
Journal J Biochem (Tokyo)
Year 1999
Volume 125
Pages 285-96
Authors Tamaoki H, Nishina Y, Shiga K, Miura R
Title Mechanism for the recognition and activation of substrate in medium-chain acyl-CoA dehydrogenase.
Related PDB
Related UniProtKB
[42]
Resource
Comments
Medline ID
PubMed ID 11076541
Journal Biochemistry
Year 2000
Volume 39
Pages 13982-92
Authors Pellett JD, Sabaj KM, Stephens AW, Bell AF, Wu J, Tonge PJ, Stankovich MT
Title Medium-chain acyl-coenzyme A dehydrogenase bound to a product analogue, hexadienoyl-coenzyme A: effects on reduction potential, pK(a), and polarization.
Related PDB
Related UniProtKB
[43]
Resource
Comments
Medline ID
PubMed ID 11027146
Journal Biochemistry
Year 2000
Volume 39
Pages 12659-70
Authors Peterson KM, Gopalan KV, Srivastava DK
Title Influence of alpha-CH-->NH substitution in C8-CoA on the kinetics of association and dissociation of ligands with medium chain acyl-CoA dehydrogenase.
Related PDB
Related UniProtKB
[44]
Resource
Comments
Medline ID
PubMed ID 11027148
Journal Biochemistry
Year 2000
Volume 39
Pages 12678-87
Authors Peterson KM, Srivastava DK
Title Energetic consequences of accommodating a bulkier ligand at the active site of medium chain acyl-CoA dehydrogenase by creating a complementary enzyme site cavity.
Related PDB
Related UniProtKB
[45]
Resource
Comments
Medline ID
PubMed ID 10625483
Journal Biochemistry
Year 2000
Volume 39
Pages 92-101
Authors Rudik I, Bell A, Tonge PJ, Thorpe C
Title 4-Hydroxycinnamoyl-CoA: an ionizable probe of the active site of the medium chain acyl-CoA dehydrogenase.
Related PDB
Related UniProtKB
[46]
Resource
Comments
Medline ID
PubMed ID 10694883
Journal Trends Biochem Sci
Year 2000
Volume 25
Pages 126-32
Authors Fraaije MW, Mattevi A
Title Flavoenzymes: diverse catalysts with recurrent features.
Related PDB
Related UniProtKB
[47]
Resource
Comments
Medline ID
PubMed ID 11488611
Journal Arch Biochem Biophys
Year 2001
Volume 392
Pages 341-8
Authors Rudik I, Thorpe C
Title Thioester enolate stabilization in the acyl-CoA dehydrogenases: the effect of 5-deaza-flavin substitution.
Related PDB
Related UniProtKB
[48]
Resource
Comments
Medline ID
PubMed ID 11591145
Journal Biochemistry
Year 2001
Volume 40
Pages 12266-75
Authors Wang W, Fu Z, Zhou JZ, Kim JJ, Thorpe C
Title Interaction of 3,4-dienoyl-CoA thioesters with medium chain acyl-CoA dehydrogenase: stereochemistry of inactivation of a flavoenzyme.
Related PDB
Related UniProtKB
[49]
Resource
Comments VARIANT MCAD LEU-245.
Medline ID 21302532
PubMed ID 11409868
Journal Hum Genet
Year 2001
Volume 108
Pages 404-8
Authors Zschocke J, Schulze A, Lindner M, Fiesel S, Olgemoller K, Hoffmann GF, Penzien J, Ruiter JP, Wanders RJ, Mayatepek E
Title Molecular and functional characterisation of mild MCAD deficiency.
Related PDB
Related UniProtKB P11310
[50]
Resource
Comments
Medline ID
PubMed ID 11926826
Journal Biochemistry
Year 2002
Volume 41
Pages 4638-48
Authors Gopalan KV, Srivastava DK
Title Beyond the proton abstracting role of Glu-376 in medium-chain acyl-CoA dehydrogenase: influence of Glu-376-->Gln substitution on ligand binding and catalysis.
Related PDB
Related UniProtKB
[51]
Resource
Comments
Medline ID
PubMed ID 11872165
Journal J Biochem (Tokyo)
Year 2002
Volume 131
Pages 365-74
Authors Nakajima Y, Miyahara I, Hirotsu K, Nishina Y, Shiga K, Setoyama C, Tamaoki H, Miura R
Title Three-dimensional structure of the flavoenzyme acyl-CoA oxidase-II from rat liver, the peroxisomal counterpart of mitochondrial acyl-CoA dehydrogenase.
Related PDB
Related UniProtKB
[52]
Resource
Comments
Medline ID
PubMed ID 12504892
Journal Arch Biochem Biophys
Year 2003
Volume 409
Pages 251-61
Authors Lamm TR, Kohls TD, Saenger AK, Stankovich MT
Title Comparison of ligand polarization and enzyme activation in medium- and short-chain acyl-coenzyme A dehydrogenase-novel analog complexes.
Related PDB
Related UniProtKB
[53]
Resource
Comments
Medline ID
PubMed ID 14529297
Journal Biochemistry
Year 2003
Volume 42
Pages 11846-56
Authors Wu J, Bell AF, Luo L, Stephens AW, Stankovich MT, Tonge PJ
Title Probing hydrogen-bonding interactions in the active site of medium-chain acyl-CoA dehydrogenase using Raman spectroscopy.
Related PDB
Related UniProtKB
[54]
Resource
Comments X|ray crystallography
Medline ID
PubMed ID 12966080
Journal J Biochem (Tokyo)
Year 2003
Volume 134
Pages 297-304
Authors Satoh A, Nakajima Y, Miyahara I, Hirotsu K, Tanaka T, Nishina Y, Shiga K, Tamaoki H, Setoyama C, Miura R
Title Structure of the transition state analog of medium-chain acyl-CoA dehydrogenase. Crystallographic and molecular orbital studies on the charge-transfer complex of medium-chain acyl-CoA dehydrogenase with 3-thiaoctanoyl-CoA.
Related PDB 1udy
Related UniProtKB
[55]
Resource
Comments
Medline ID
PubMed ID 14728675
Journal Eur J Biochem
Year 2004
Volume 271
Pages 483-93
Authors Kim JJ, Miura R
Title Acyl-CoA dehydrogenases and acyl-CoA oxidases. Structural basis for mechanistic similarities and differences.
Related PDB
Related UniProtKB
[56]
Resource
Comments X|ray crystallography
Medline ID
PubMed ID 15159392
Journal J Biol Chem
Year 2004
Volume 279
Pages 32904-12
Authors Toogood HS, van Thiel A, Basran J, Sutcliffe MJ, Scrutton NS, Leys D
Title Extensive domain motion and electron transfer in the human electron transferring flavoprotein.medium chain Acyl-CoA dehydrogenase complex.
Related PDB 1t9g
Related UniProtKB
[57]
Resource
Comments
Medline ID
PubMed ID 15358373
Journal Protein Expr Purif
Year 2004
Volume 37
Pages 472-8
Authors Zeng J, Li D
Title Expression and purification of His-tagged rat mitochondrial medium-chain acyl-CoA dehydrogenase wild-type and Arg256 mutant proteins.
Related PDB
Related UniProtKB
[58]
Resource
Comments
Medline ID
PubMed ID 15975918
Journal J Biol Chem
Year 2005
Volume 280
Pages 30361-6
Authors Toogood HS, van Thiel A, Scrutton NS, Leys D
Title Stabilization of non-productive conformations underpins rapid electron transfer to electron-transferring flavoprotein.
Related PDB 2a1t
Related UniProtKB

Comments
This enzyme is a member of medium-chain acyl-CoA dehydrogenases.
Accoriding to the literature, this enzyme catalyzes the following reactions:
(A) Hydride transfer from acyl-CoA substrate to FAD, giving 2,3-dehydroacyl-CoA and FADH2(Two-electron-reduced form of FAD) (Reductive half-reaction):
(B) Hydride transfer from FADH2 to FAD of an acceptor protein, Electron-Transferring Flavoprotein (ETF):
The ETF protein is heterodimer (alpha/beta subunits) containing one FAD and one AMP per dimer (see [58], Swissprot;P13804, P38117). This protein seems to accept electrons from various oxidoreductases.

Created Updated
2005-05-12 2012-10-02