Enzyme

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     2. Transferases
        2.3 Acyltransferases
            2.3.1 Transferring groups other than aminoacyl groups
ID:2.3.1.16
Description:Acetyl-CoA C-acyltransferase.
Alternative Name: Beta-ketothiolase.
3-ketoacyl-CoA thiolase.
Prosite: PDOC00092;
PDB:
PDBScop
Cath: 3.40.190.10; 3.40.47.10;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 2.3.1.16
BRENDA Enzyme Link: BRENDA 2.3.1.16
KEGG Enzyme Link: KEGG2.3.1.16
BioCyc Enzyme Link: BioCyc 2.3.1.16
ExPASy Enzyme Link: ExPASy2.3.1.16
EC2PDB Enzyme Link: EC2PDB 2.3.1.16
ExplorEnz Enzyme Link: ExplorEnz 2.3.1.16
PRIAM enzyme-specific profiles Link: PRIAM 2.3.1.16
IntEnz Enzyme Link: IntEnz 2.3.1.16
MEDLINE Enzyme Link: MEDLINE 2.3.1.16
MSA:

2.3.1.16;

Phylogenetic Tree:

2.3.1.16;

Uniprot:
M-CSA:
RHEA:21564 acetyl-CoA + an acyl-CoA = a 3-oxoacyl-CoA + CoA
RULE(radius=1) [*:1]-[C;H0;+0:2](=[*:3])-[S;H0;+0:4]-[*:5].[*:6]-[CH3;+0:7]>>[*:1]-[C;H0;+0:2](=[*:3])-[CH2;+0:7]-[*:6].[*:5]-[SH;+0:4]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
FadA5 a thiolase from Mycobacterium tuberculosis: a steroid-binding pocket reveals the potential for drug development against tuberculosis.Schaefer CM, Lu R, Nesbitt NM, Schiebel J, Sampson NS, Kisker C2015 Jan 625482540
A thiolase of Mycobacterium tuberculosis is required for virulence and production of androstenedione and androstadienedione from cholesterol.Nesbitt NM, Yang X, Fontán P, Kolesnikova I, Smith I, Sampson NS, Dubnau E2010 Jan19822655
Antifungal activity of Saccharomyces cerevisiae peroxisomal 3-ketoacyl-CoA thiolase.Lee JR, Kim SY, Chae HB, Jung JH, Lee SY2009 May 3119470242
Studies on the fatty acid oxidizing system of animal tissues. VII. The beta-ketoacyl coenzyme A cleavage enzyme.GOLDMAN DS1954 May13174544
Enzymatic breakdown and synthesis of acetoacetate.STERN JR, COON MJ, DEL CAMPILLO A1953 Jan 313025466