1MKA

E. COLI BETA-HYDROXYDECANOYL THIOL ESTER DEHYDRASE MODIFIED BY ITS CLASSIC MECHANISM-BASED INACTIVATOR, 3-DECYNOYL-N-ACETYL CYSTEAMINE

Summary for 1MKA

• Entry DOI: 10.2210/pdb1mka/pdb
• Descriptor: BETA-HYDROXYDECANOYL THIOL ESTER DEHYDRASE, 2-DECENOYL N-ACETYL CYSTEAMINE (3 entities in total)
• Functional Keywords: fatty acid biosynthesis
• Biological source: Escherichia coli
• Cellular location: Cytoplasm: P0A6Q3
• Total number of polymer chains: 2
• Total formula weight: 38262.53

Authors

Leesong, M. (deposition date: 1996-01-08, release date: 1996-07-11, Last modification date: 2024-10-09)

Primary citation

Leesong, M.,Henderson, B.S.,Gillig, J.R.,Schwab, J.M.,Smith, J.L.
Structure of a dehydratase-isomerase from the bacterial pathway for biosynthesis of unsaturated fatty acids: two catalytic activities in one active site.
Structure, 4:253-264, 1996

PubMed Abstract: Escherichia coli beta-hydroxydecanoyl thiol ester dehydrase (dehydrase) is essential to the biosynthesis of unsaturated fatty acids, by shunting a 10-carbon intermediate from the saturated fatty acid pathway into the unsaturated fatty acid pathway. Dehydrase catalyzes reactions of dehydration and of double-bond isomerization on 10-carbon thiol esters of acyl carrier protein (ACP). The aim of this work is to elucidate mechanisms for the two enzymatic reactions, which occur in an unusual bifunctional active site, and to understand the specificity of the enzyme for substrates with 10-carbon fatty acyl chains.

PubMed: 8805534
DOI: 10.1016/S0969-2126(96)00030-5

Experimental method

X-RAY DIFFRACTION (2 Å)