Names and origin

Protein names

Gene names
Organism
Taxonomic
identifier
Taxonomic
lineage

Recommended name:
Succinyl-CoA:3-ketoacid coenzyme A transferase 1, mitochondrial
EC=2.8.3.5
Alternative name(s):
3-oxoacid CoA-transferase 1
Somatic-type succinyl-CoA:3-oxoacid CoA-transferase
Short name=SCOT-s
Name:
OXCT1
Synonyms:
OXCT, SCOT
Homo sapiens (Human) [Reference proteome]
9606 [NCBI]
Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria
Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo

Protein attributes
Sequence length
Sequence status
Sequence processing
Protein existence

520 AA.
Complete.
The displayed sequence is further processed into a mature form.
Evidence at protein level

General annotation (Comments)

Function

Key enzyme for ketone body catabolism. Transfers the CoA moiety from succinate to acetoacetate.
Formation of the enzyme-CoA intermediate proceeds via an unstable anhydride species formed
between the carboxylate groups of the enzyme and substrate.

Catalytic
activity

Succinyl-CoA + a 3-oxo acid = succinate + a 3-oxoacyl-CoA.

Pathway

Ketone metabolism; succinyl-CoA degradation; acetoacetyl-CoA from succinyl-CoA: step 1/1.

Subunit
structure

Homodimer.

Subcellular
location

Mitochondrion matrix.

Tissue
specificity

Abundant in heart, followed in order by kidney, brain, and muscle, whereas in liver it is
undetectable; also detectable in leukocytes and fibroblasts.

Involvement in
disease
Defects in OXCT1 are a cause of succinyl-CoA-3-ketoacid-CoA transferase deficiency (SCOTD)

[MIM:245050]. A disorder of ketone body metabolism, characterized by episodic ketoacidosis.

Patients are usually asymptomatic between episodes. Ref.2 Ref.8 Ref.9
Sequence
similarities

Belongs to the 3-oxoacid CoA-transferase family.

Names and origin

Protein names

Gene names
Organism
Taxonomic
identifier
Taxonomic
lineage

Recommended name:
D-beta-hydroxybutyrate dehydrogenase, mitochondrial
Short name=BDH
EC=1.1.1.30
Alternative name(s):
3-hydroxybutyrate dehydrogenase
Name:
Synonyms:
Homo sapiens (Human) [Reference proteome]

BDH1
BDH

9606 [NCBI]
Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria
Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo

Protein attributes
Sequence length
Sequence status
Sequence processing
Protein existence

343 AA.
Complete.
The displayed sequence is further processed into a mature form.
Evidence at protein level

General annotation (Comments)

Catalytic activity

(R)-3-hydroxybutanoate + NAD+ = acetoacetate + NADH.

Enzyme regulation

Requires phosphatidylcholine as an allosteric activator for enzymatic activity.

Subunit structure

Homotetramer.

Subcellular location Mitochondrion matrix.

Sequence
similarities

Belongs to the short-chain dehydrogenases/reductases (SDR) family.

Sequence caution

The sequence AAA58352.1 differs from that shown. Reason: Frameshift at positions 124 and
134.

Names and origin

Recommended name:
3-hydroxybutyrate dehydrogenase type 2
EC=1.1.1.EC=1.1.1.30
Protein names
Alternative name(s):
Dehydrogenase/reductase SDR family member 6
Oxidoreductase UCPA
R-beta-hydroxybutyrate dehydrogenase
Name:
BDH2
Gene names
Synonyms:
DHRS6
ORF Names:
UNQ6308/PRO20933
Organism
Homo sapiens (Human) [Reference proteome]
Taxonomic
9606 [NCBI]
identifier
Taxonomic
Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria
lineage
Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo
Protein attributes
Sequence length
Sequence status
Protein existence

245 AA.
Complete.
Evidence at protein level

General annotation (Comments)

Function

Dehydrogenase that mediates the formation of 2,5-dihydroxybenzoic acid (2,5-DHBA), a

siderophore that shares structural similarities with bacterial enterobactin and associates with
LCN2, thereby playing a key role in iron homeostasis and transport. Also acts as a 3hydroxybutyrate dehydrogenase By similarity. Ref.10

Catalytic activity

(R)-3-hydroxybutanoate + NAD+ = acetoacetate + NADH.

Pathway

Siderophore biosynthesis.

Subunit structure
Homotetramer. Ref.10

Subcellular location

Cytoplasm Ref.10.

Sequence similarities Belongs to the short-chain dehydrogenases/reductases (SDR) family.

Kinetic parameters:
KM=60 M for NAD Ref.10
Biophysicochemical
properties

KM=10 mM for R-hydroxybutyrate

Vmax=82 nmol/min/mg enzyme (at 30 degrees Celsius)
pH dependence:
Optimum pH is 7.5-9.0.

Names and origin

Protein names

Gene names
Organism
Taxonomic
identifier
Taxonomic
lineage

Recommended name:
Acetyl-CoA acetyltransferase, mitochondrial
EC=2.3.1.9
Alternative name(s):
Acetoacetyl-CoA thiolase
T2
Name:
ACAT1
Synonyms:
ACAT, MAT
Homo sapiens (Human) [Reference proteome]
9606 [NCBI]
Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria
Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo

Protein attributes
Sequence length
Sequence status
Sequence processing
Protein existence

427 AA.
Complete.
The displayed sequence is further processed into a mature form.
Evidence at protein level

General annotation (Comments)

Function

Plays a major role in ketone body metabolism.

Catalytic activity

2 acetyl-CoA = CoA + acetoacetyl-CoA. Ref.9

Enzyme regulation

Activated by potassium ions, but not sodium ions. Ref.9

Subunit structure

Homotetramer. Ref.9

Subcellular location

Mitochondrion.

Involvement in
disease

Defects in ACAT1 are a cause of 3-ketothiolase deficiency (3KTD) [MIM:203750]; also

known as alpha-methylacetoaceticaciduria. 3KTD is an inborn error of isoleucine
catabolism characterized by intermittent ketoacidotic attacks associated with
unconsciousness. Some patients die during an attack or are mentally retarded. Urinary
excretion of 2-methyl-3-hydroxybutyric acid, 2-methylacetoacetic acid, triglylglycine,
butanone is increased. It seems likely that the severity of this disease correlates better with
the environmental or acquired factors than with the ACAT1 genotype. Ref.11 Ref.12 Ref.13
Ref.14

Sequence similarities Belongs to the thiolase family.

Kinetic parameters:
KM=4 M for acteoacetyl coenzyme A Ref.9
Biophysicochemical
properties

KM=20 M for coenzyme A

KM=8 M for 2-methylacteoacetyl coenzyme A
KM=508 M for acetyl coenzyme A