DB code: D00007

CATH domain 3.40.50.720 : Rossmann fold Catalytic domain
1.10.1040.10 : N-(1-d-carboxylethyl)-l-norvaline Dehydrogenase; domain 2
E.C. 1.1.1.35
CSA 2hdh
M-CSA 2hdh
MACiE

CATH domain Related DB codes (homologues)
3.40.50.720 : Rossmann fold S00543 S00551 S00552 S00553 S00602 S00604 S00605 S00608 S00610 S00625 S00319 S00328 S00329 S00330 S00331 S00332 D00456 D00457 D00458 S00324 S00320 S00325 S00326 S00327 D00459 S00335 S00336 S00334 T00219 S00339 D00513 D00001 D00002 D00003 D00005 D00008 D00010 D00012 D00017 D00018 D00023 D00027 D00028 D00031 D00032 D00033 D00034 D00035 D00037 D00048 D00071 D00476 D00481 D00482 D00490 D00492 D00494 D00545 D00601 D00603 D00604 D00605 D00615 D00845 D00857 D00858 M00161 M00171 M00210 T00002 T00010 T00011 T00015 T00227 T00247 T00408 T00414 D00827 D00262 D00274 D00275 M00035 T00109
1.10.1040.10 : N-(1-d-carboxylethyl)-l-norvaline Dehydrogenase; domain 2 D00012 D00603 T00002 T00227

Uniprot Enzyme Name
UniprotKB Protein name Synonyms RefSeq Pfam
Q16836 Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial
HCDH
EC 1.1.1.35
Medium and short-chain L-3-hydroxyacyl-coenzyme A dehydrogenase
Short-chain 3-hydroxyacyl-CoA dehydrogenase
NP_001171634.2 (Protein)
NM_001184705.2 (DNA/RNA sequence)
NP_005318.3 (Protein)
NM_005327.4 (DNA/RNA sequence)
PF00725 (3HCDH)
PF02737 (3HCDH_N)
[Graphical View]
P00348 Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial
HCDH
EC 1.1.1.35
Medium and short-chain L-3-hydroxyacyl-coenzyme A dehydrogenase
Short-chain 3-hydroxyacyl-CoA dehydrogenase
NP_999496.1 (Protein)
NM_214331.1 (DNA/RNA sequence)
PF00725 (3HCDH)
PF02737 (3HCDH_N)
[Graphical View]

KEGG enzyme name
3-hydroxyacyl-CoA dehydrogenase
beta-hydroxyacyl dehydrogenase
beta-keto-reductase
3-keto reductase
3-hydroxyacyl coenzyme A dehydrogenase
beta-hydroxyacyl-coenzyme A synthetase
beta-hydroxyacylcoenzyme A dehydrogenase
beta-hydroxybutyrylcoenzyme A dehydrogenase
3-hydroxyacetyl-coenzyme A dehydrogenase
L-3-hydroxyacyl coenzyme A dehydrogenase
L-3-hydroxyacyl CoA dehydrogenase
beta-hydroxyacyl CoA dehydrogenase
3beta-hydroxyacyl coenzyme A dehydrogenase
3-hydroxybutyryl-CoA dehydrogenase
beta-ketoacyl-CoA reductase
beta-hydroxy acid dehydrogenase
3-L-hydroxyacyl-CoA dehydrogenase
3-hydroxyisobutyryl-CoA dehydrogenase
1-specific DPN-linked beta-hydroxybutyric dehydrogenase

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P00348 HCDH_PIG (S)-3-hydroxyacyl-CoA + NAD(+) = 3-oxoacyl-CoA + NADH. Homodimer. Mitochondrion matrix.
Q16836 HCDH_HUMAN (S)-3-hydroxyacyl-CoA + NAD(+) = 3-oxoacyl-CoA + NADH. Homodimer. Mitochondrion matrix.

KEGG Pathways
Map code Pathways E.C.
MAP00062 Fatty acid elongation in mitochondria
MAP00071 Fatty acid metabolism
MAP00280 Valine, leucine and isoleucine degradation
MAP00281 Geraniol degradation
MAP00310 Lysine degradation
MAP00380 Tryptophan metabolism
MAP00592 alpha-Linolenic acid metabolism
MAP00632 Benzoate degradation via CoA ligation
MAP00650 Butanoate metabolism
MAP00930 Caprolactam degradation

Compound table
Substrates Products Intermediates
KEGG-id C00003 C00640 C04405 C00004 C00264 C03344 C00080
E.C.
Compound NAD+ (3S)-3-Hydroxyacyl-CoA (2S,3S)-3-Hydroxy-2-methylbutanoyl-CoA NADH 3-Oxoacyl-CoA 2-Methylacetoacetyl-CoA H+
Type amide group,amine group,nucleotide amine group,carbohydrate,nucleotide ,peptide/protein,sulfide group amine group,carbohydrate,nucleotide ,peptide/protein,sulfide group amide group,amine group,nucleotide amine group,carbohydrate,nucleotide ,peptide/protein,phosphate group/phosphate ion,sulfide group amine group,carbohydrate,nucleotide ,peptide/protein,sulfide group others
ChEBI 15846
15449
16908
15476
15378
PubChem 5893
11966220
440326
439153
193425
439985
1038
1f0yA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:NAD Unbound Unbound Unbound Bound:CAA Unbound
1f0yB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:NAD Unbound Unbound Unbound Bound:CAA Unbound
1f12A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Bound:3HC Unbound Unbound Unbound Unbound
1f12B01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1f14A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1f14B01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1f17A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Bound:NAI Unbound Unbound
1f17B01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Bound:NAI Unbound Unbound
1il0A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:NAD Unbound Unbound Unbound Bound:CAA Unbound
1il0B01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:NAD Unbound Unbound Unbound Bound:CAA Unbound
1lsjA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:NAD Unbound Unbound Unbound Unbound Unbound
1lsjB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:NAD Unbound Unbound Unbound Unbound Unbound
2hdhA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:NAD Unbound Unbound Unbound Unbound Unbound
2hdhB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:NAD Unbound Unbound Unbound Unbound Unbound
3hadA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:NAD Unbound Unbound Unbound Unbound Unbound
3hadB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:NAD Unbound Unbound Unbound Unbound Unbound
3hdhA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:NAD Unbound Unbound Unbound Unbound Unbound
3hdhB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:NAD Unbound Unbound Unbound Unbound Unbound
3hdhC01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:NAD Unbound Unbound Unbound Unbound Unbound
1f0yA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1f0yB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1f12A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1f12B02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1f14A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1f14B02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1f17A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1f17B02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1il0A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1il0B02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1lsjA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1lsjB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
2hdhA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
2hdhB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
3hadA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
3hadB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
3hdhA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
3hdhB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
3hdhC02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
PDB;2hdh, 3had & Swiss-prot;Q16836, P00348 & literature [11], [18]

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1f0yA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 158;GLU 170
1f0yB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 158;GLU 170
1f12A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 158;GLU 170 mutant F80C
1f12B01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 158;GLU 170 mutant F80C
1f14A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 158;GLU 170 mutant F80C
1f14B01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 158;GLU 170 mutant F80C
1f17A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 158;GLU 170 mutant F80C
1f17B01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 158;GLU 170 mutant F80C
1il0A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 158 mutant E170Q
1il0B01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 158 mutant E170Q
1lsjA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 158;GLU 170 mutant E111Q
1lsjB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 158;GLU 170 mutant E111Q
2hdhA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 158;GLU 170 (3 selenomethionine)
2hdhB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 158;GLU 170 (3 selenomethionine)
3hadA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 158;GLU 170
3hadB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 158;GLU 170
3hdhA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 158;GLU 170
3hdhB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 158;GLU 170
3hdhC01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 158;GLU 170
1f0yA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1f0yB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1f12A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1f12B02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1f14A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1f14B02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1f17A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1f17B02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1il0A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1il0B02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1lsjA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1lsjB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
2hdhA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain (4 selenomethionine)
2hdhB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain (4 selenomethionine)
3hadA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
3hadB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
3hdhA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
3hdhB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
3hdhC02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[4]
p.6444-6445
[8]
Fig.3, p.265-268
[11]
Fig.7, p.5795-5797
[17]
[18]
SCHEME 1

References
[1]
Resource
Comments
Medline ID
PubMed ID 7150615
Journal Biochim Biophys Acta
Year 1982
Volume 713
Pages 270-9
Authors El-Fakhri M, Middleton B
Title The existence of an inner-membrane-bound, long acyl-chain-specific 3-hydroxyacyl-CoA dehydrogenase in mammalian mitochondria.
Related PDB
Related UniProtKB
[2]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
Medline ID
PubMed ID 3479790
Journal Proc Natl Acad Sci U S A
Year 1987
Volume 84
Pages 8262-6
Authors Birktoft JJ, Holden HM, Hamlin R, Xuong NH, Banaszak LJ
Title Structure of L-3-hydroxyacyl-coenzyme A dehydrogenase: preliminary chain tracing at 2.8-A resolution.
Related PDB 3had 3hdh
Related UniProtKB P00348
[3]
Resource
Comments
Medline ID
PubMed ID 1848777
Journal Biochemistry
Year 1991
Volume 30
Pages 2782-90
Authors Hartmann D, Philipp R, Schmadel K, Birktoft JJ, Banaszak LJ, Trommer WE
Title Spatial arrangement of coenzyme and substrates bound to L-3-hydroxyacyl-CoA dehydrogenase as studied by spin-labeled analogues of NAD+ and CoA.
Related PDB
Related UniProtKB
[4]
Resource
Comments
Medline ID
PubMed ID 7756275
Journal Biochemistry
Year 1995
Volume 34
Pages 6441-7
Authors Yang SY, He XY, Schulz H
Title 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.
Related PDB
Related UniProtKB
[5]
Resource
Comments
Medline ID
PubMed ID 8687463
Journal Biochem Biophys Res Commun
Year 1996
Volume 223
Pages 718-23
Authors Vredendaal PJ, van den Berg IE, Malingre HE, Stroobants AK, Olde Weghuis DE, Berger R
Title Human short-chain L-3-hydroxyacyl-CoA dehydrogenase: cloning and characterization of the coding sequence.
Related PDB
Related UniProtKB
[6]
Resource
Comments
Medline ID
PubMed ID 8755745
Journal Biochemistry
Year 1996
Volume 35
Pages 9625-30
Authors He XY, Yang SY
Title 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.
Related PDB
Related UniProtKB
[7]
Resource
Comments
Medline ID
PubMed ID 9396725
Journal Biochem J
Year 1997
Volume 328
Pages 815-20
Authors Ishikawa M, Mikami Y, Usukura J, Iwasaki H, Shinagawa H, Morikawa K
Title Reconstitution, morphology and crystallization of a fatty acid beta-oxidation multienzyme complex from Pseudomonas fragi.
Related PDB
Related UniProtKB
[8]
Resource
Comments
Medline ID
PubMed ID 8993342
Journal Biochemistry
Year 1997
Volume 36
Pages 261-8
Authors He XY, Deng H, Yang SY
Title Importance of the gamma-carboxyl group of glutamate-462 of the large alpha-subunit for the catalytic function and the stability of the multienzyme complex of fatty acid oxidation from Escherichia coli.
Related PDB
Related UniProtKB
[9]
Resource
Comments
Medline ID
PubMed ID 9593854
Journal Biochim Biophys Acta
Year 1998
Volume 1392
Pages 119-26
Authors He XY, Yang SY
Title Molecular cloning, expression in Escherichia coli, and characterization of a novel L-3-hydroxyacyl coenzyme A dehydrogenase from pig liver.
Related PDB
Related UniProtKB
[10]
Resource
Comments
Medline ID
PubMed ID 9716664
Journal Mamm Genome
Year 1998
Volume 9
Pages 763-8
Authors Vredendaal PJ, van den Berg IE, Stroobants AK, van der A DL, Malingre HE, Berger R
Title Structural organization of the human short-chain L-3-hydroxyacyl-CoA dehydrogenase gene.
Related PDB
Related UniProtKB
[11]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 13-314.
Medline ID
PubMed ID 10231530
Journal Biochemistry
Year 1999
Volume 38
Pages 5786-98
Authors Barycki JJ, O'Brien LK, Bratt JM, Zhang R, Sanishvili R, Strauss AW, Banaszak LJ
Title Biochemical characterization and crystal structure determination of human heart short chain L-3-hydroxyacyl-CoA dehydrogenase provide insights into catalytic mechanism.
Related PDB 2hdh
Related UniProtKB Q16836
[12]
Resource
Comments
Medline ID
PubMed ID 10064895
Journal Biochim Biophys Acta
Year 1999
Volume 1437
Pages 119-23
Authors He XY, Zhang G, Blecha F, Yang SY
Title Identity of heart and liver L-3-hydroxyacyl coenzyme A dehydrogenase.
Related PDB
Related UniProtKB
[13]
Resource
Comments
Medline ID
PubMed ID 10329704
Journal J Biol Chem
Year 1999
Volume 274
Pages 15014-9
Authors He XY, Merz G, Mehta P, Schulz H, Yang SY
Title Human brain short chain L-3-hydroxyacyl coenzyme A dehydrogenase is a single-domain multifunctional enzyme. Characterization of a novel 17beta-hydroxysteroid dehydrogenase.
Related PDB
Related UniProtKB
[14]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
Medline ID
PubMed ID 10548046
Journal Protein Sci
Year 1999
Volume 8
Pages 2010-8
Authors Barycki JJ, O'Brien LK, Birktoft JJ, Strauss AW, Banaszak LJ
Title Pig heart short chain L-3-hydroxyacyl-CoA dehydrogenase revisited: sequence analysis and crystal structure determination.
Related PDB 3hdh
Related UniProtKB P00348
[15]
Resource
Comments
Medline ID
PubMed ID 10600649
Journal Biochem J
Year 2000
Volume 345
Pages 139-43
Authors He XY, Yang YZ, Schulz H, Yang SY
Title Intrinsic alcohol dehydrogenase and hydroxysteroid dehydrogenase activities of human mitochondrial short-chain L-3-hydroxyacyl-CoA dehydrogenase.
Related PDB
Related UniProtKB
[16]
Resource
Comments
Medline ID
PubMed ID 10760475
Journal Biochim Biophys Acta
Year 2000
Volume 1484
Pages 267-77
Authors He XY, Merz G, Yang YZ, Pullakart R, Mehta P, Schulz H, Yang SY
Title Function of human brain short chain L-3-hydroxyacyl coenzyme A dehydrogenase in androgen metabolism.
Related PDB
Related UniProtKB
[17]
Resource
Comments X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 13-314.
Medline ID
PubMed ID 10840044
Journal J Biol Chem
Year 2000
Volume 275
Pages 27186-96
Authors Barycki JJ, O'Brien LK, Strauss AW, Banaszak LJ
Title Sequestration of the active site by interdomain shifting. Crystallographic and spectroscopic evidence for distinct conformations of L-3-hydroxyacyl-CoA dehydrogenase.
Related PDB 1f0y 1f12 1f14 1f17
Related UniProtKB Q16836
[18]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 11451959
Journal J Biol Chem
Year 2001
Volume 276
Pages 36718-26
Authors Barycki JJ, O'Brien LK, Strauss AW, Banaszak LJ
Title Glutamate 170 of human l-3-hydroxyacyl-CoA dehydrogenase is required for proper orientation of the catalytic histidine and structural integrity of the enzyme.
Related PDB 1il0
Related UniProtKB

Comments
Hi158 acts as a general base, whereas Glu170 acts as a modulator for the base. Ser137 & Asn208 might be also catalytic (see [11]).
###
This enzyme also oxidizes S-3-hydroxyacyl-N-acylthioethanolamine and S-3-hydroxyacylhydrolipoate.
The enzymes (E.C. 1.1.1.211) acts on chain length C(8) or C(10).

Created Updated
2004-06-17 2009-02-26