scholarly journals ORF17 from the Clavulanic Acid Biosynthesis Gene Cluster Catalyzes the ATP-dependent Formation ofN-Glycyl-clavaminic Acid

2005 ◽  
Vol 281 (1) ◽  
pp. 279-287 ◽  
Author(s):  
Haren Arulanantham ◽  
Nadia J. Kershaw ◽  
Kirsty S. Hewitson ◽  
Claire E. Hughes ◽  
Jan E. Thirkettle ◽  
...  
Keyword(s):  
Clavulanic Acid ◽  
Gene Cluster ◽  
Acid Biosynthesis ◽  
Biosynthesis Gene Cluster ◽  
Biosynthesis Gene

scholarly journals X-ray crystal structure of ornithine acetyltransferase from the clavulanic acid biosynthesis gene cluster

2005 ◽  
Vol 385 (2) ◽  
pp. 565-573 ◽  
Author(s):  
Jonathan M. ELKINS ◽  
Nadia J. KERSHAW ◽  
Christopher J. SCHOFIELD
Keyword(s):  
Crystal Structure ◽  
Clavulanic Acid ◽  
Gene Cluster ◽  
Acid Biosynthesis ◽  
Biosynthesis Gene Cluster ◽  
Reading Frame ◽  
X Ray ◽  
Orf6 Gene ◽  
Biosynthesis Gene ◽  
Acetyl Transfer

The orf6 gene from the clavulanic acid biosynthesis gene cluster encodes an OAT (ornithine acetyltransferase). Similar to other OATs the enzyme has been shown to catalyse the reversible transfer of an acetyl group from N-acetylornithine to glutamate. OATs are Ntn (N-terminal nucleophile) enzymes, but are distinct from the better-characterized Ntn hydrolase enzymes as they catalyse acetyl transfer rather than a hydrolysis reaction. In the present study, we describe the X-ray crystal structure of the OAT, corresponding to the orf6 gene product, to 2.8 Å (1 Å=0.1 nm) resolution. The larger domain of the structure consists of an αββα sandwich as in the structures of Ntn hydrolase enzymes. However, differences in the connectivity reveal that OATs belong to a structural family different from that of other structurally characterized Ntn enzymes, with one exception: unexpectedly, the αββα sandwich of ORF6 (where ORF stands for open reading frame) displays the same fold as an DmpA (L-aminopeptidase D-ala-esterase/amidase from Ochrobactrum anthropi), and so the OATs and DmpA form a new structural subfamily of Ntn enzymes. The structure reveals an α2β2-heterotetrameric oligomerization state in which the intermolecular interface partly defines the active site. Models of the enzyme–substrate complexes suggest a probable oxyanion stabilization mechanism as well as providing insight into how the enzyme binds its two differently charged substrates.

Deletion analysis of the itaconic acid biosynthesis gene cluster components in Aspergillus pseudoterreus ATCC32359

2020 ◽  
Vol 104 (9) ◽  
pp. 3981-3992
Author(s):  
Shuang Deng ◽  
Ziyu Dai ◽  
Marie Swita ◽  
Kyle R. Pomraning ◽  
Beth Hofstad ◽  
...  
Keyword(s):  
Gene Cluster ◽  
Itaconic Acid ◽  
Deletion Analysis ◽  
Acid Biosynthesis ◽  
Biosynthesis Gene Cluster ◽  
Biosynthesis Gene

Cyclopiazonic acid biosynthesis gene cluster gene cpaM is required for speradine A biosynthesis

2015 ◽  
Vol 79 (12) ◽  
pp. 2081-2085 ◽  
Author(s):  
Masafumi Tokuoka ◽  
Tomoki Kikuchi ◽  
Yasutomo Shinohara ◽  
Akifumi Koyama ◽  
Shin-ichiro Iio ◽  
...  
Keyword(s):  
Gene Cluster ◽  
Cyclopiazonic Acid ◽  
Acid Biosynthesis ◽  
Biosynthesis Gene Cluster ◽  
Biosynthesis Gene ◽  
Cluster Gene
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