The Enzyme Database

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EC 2.3.1.281     
Accepted name: 5-hydroxydodecatetraenal polyketide synthase
Reaction: 6 malonyl-CoA + 5 NADPH + NADH + 6 H+ = (2E,5S,6E,8E,10E)-5-hydroxydodeca-2,6,8,10-tetraenal + 6 CoA + 5 NADP+ + NAD+ + 6 CO2 + 4 H2O
Glossary: coelimycin P1 = N-[(3R)-8-[(2E)-but-2-enoyl]-6-[(2E)-5,6-dihydropyridin-2(1H)-ylidene]-2-oxo-3,4-dihydro-2H,6H-1,5-oxathiocin-3-yl]acetamide
Other name(s): cpkABC (gene names)
Systematic name: malonyl-CoA:malonyl-CoA malonyltransferase ((2E,5S,6E,8E,10E)-5-hydroxydodeca-2,6,8,10-tetraenal-forming)
Comments: This polyketide synthase enzyme, characterized from the bacterium Streptomyces coelicolor A3(2), catalyses the first reaction in the biosynthesis of coelimycin P1. The enzyme is made of three proteins which together comprise six modules that contain a total of 28 domains. An NADH-dependent terminal reductase domain at the C-terminus of the enzyme catalyses the reductive release of the product.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Pawlik, K., Kotowska, M., Chater, K.F., Kuczek, K. and Takano, E. A cryptic type I polyketide synthase (cpk) gene cluster in Streptomyces coelicolor A3(2). Arch. Microbiol. 187 (2007) 87–99. [PMID: 17009021]
2.  Awodi, U.R., Ronan, J.L., Masschelein, J., Santos, E.LC. and Challis, G.L. Thioester reduction and aldehyde transamination are universal steps in actinobacterial polyketide alkaloid biosynthesis. Chem. Sci. 8 (2017) 411–415. [PMID: 28451186]
[EC 2.3.1.281 created 2019]
 
 
EC 2.6.1.115     
Accepted name: 5-hydroxydodecatetraenal 1-aminotransferase
Reaction: (2E,5S,6E,8E,10E)-1-aminododeca-2,6,8,10-tetraen-5-ol + pyruvate = (2E,5S,6E,8E,10E)-5-hydroxydodeca-2,6,8,10-tetraenal + L-alanine
Glossary: coelimycin P1 = N-[(3R)-8-[(2E)-but-2-enoyl]-2-oxo-6-[(2E)-1,2,5,6-tetrahydropyridin-2-ylidene]-2,3,4,6-tetrahydro-1,5-oxathiocin-3-yl]acetamide
Other name(s): cpkG (gene name)
Systematic name: (2E,5S,6E,8E,10E)-1-aminododeca-2,6,8,10-tetraen-5-ol:pyruvate aminotransferase
Comments: The enzyme, characterized from the bacterium Streptomyces coelicolor A3(2), participates in the biosynthesis of coelimycin P1, where it catalyses the amination of (2E,5S,6E,8E,10E)-5-hydroxydodeca-2,6,8,10-tetraenal. L-glutamate can also serve as the amino group donor with lower efficiency.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Pawlik, K., Kotowska, M., Chater, K.F., Kuczek, K. and Takano, E. A cryptic type I polyketide synthase (cpk) gene cluster in Streptomyces coelicolor A3(2). Arch. Microbiol. 187 (2007) 87–99. [PMID: 17009021]
2.  Awodi, U.R., Ronan, J.L., Masschelein, J., Santos, E.LC. and Challis, G.L. Thioester reduction and aldehyde transamination are universal steps in actinobacterial polyketide alkaloid biosynthesis. Chem. Sci. 8 (2017) 411–415. [PMID: 28451186]
[EC 2.6.1.115 created 2019]
 
 


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