Photoinduced molecular transformations. 104. Pathways of the photorearrangements of five-membered cyclic steroidal .alpha.-nitro ketones to N-hydroxy cyclic imides, cyclic hydroxamic acid, and cyclic imide

1989 ◽  
Vol 54 (25) ◽  
pp. 5945-5953 ◽  
Author(s):  
Hiroshi Suginome ◽  
Yoshitaka Kurokawa
Keyword(s):  
Hydroxamic Acid ◽  
Cyclic Imide ◽  
Cyclic Imides ◽  
Cyclic Hydroxamic Acid

Analogs of the cyclic hydroxamic acid 2,4-dihydroxy-7-methoxy-2H-1,4-benzoxazin-3-one (DIMBOA): decomposition to benzoxazolinones and reaction with .beta.-mercaptoethanol

1991 ◽  
Vol 56 (5) ◽  
pp. 1788-1800 ◽  
Author(s):  
Jeffrey Atkinson ◽  
Peter Morand ◽  
John T. Arnason ◽  
Hermann M. Niemeyer ◽  
Hector R. Bravo
Keyword(s):  
Hydroxamic Acid ◽  
Cyclic Hydroxamic Acid

Reaction of a cyclic hydroxamic acid from gramineae with thiols

1982 ◽  
Vol 21 (9) ◽  
pp. 2287-2289 ◽  
Author(s):  
Hermann M. Niemeyer ◽  
Luis J. Corcuera ◽  
Francisco J. Pérez
Keyword(s):  
Hydroxamic Acid ◽  
Cyclic Hydroxamic Acid

scholarly journals A Novel Amidase (Half-Amidase) for Half-Amide Hydrolysis Involved in the Bacterial Metabolism of Cyclic Imides

2000 ◽  
Vol 66 (5) ◽  
pp. 1947-1952 ◽  
Author(s):  
Chee-Leong Soong ◽  
Jun Ogawa ◽  
Sakayu Shimizu
Keyword(s):  
Catalytic Efficiency ◽  
High Specificity ◽  
Bacterial Metabolism ◽  
Second Step ◽  
Cyclic Imide ◽  
Sulfhydryl Reagents ◽  
Succinamic Acid ◽  
Amide Hydrolysis ◽  
Cyclic Imides ◽  
Hydrolysis Of

ABSTRACT A novel amidase involved in bacterial cyclic imide metabolism was purified from Blastobacter sp. strain A17p-4. The enzyme physiologically functions in the second step of cyclic imide degradation, i.e., the hydrolysis of monoamidated dicarboxylates (half-amides) to dicarboxylates and ammonia. Enzyme production was enhanced by cyclic imides such as succinimide and glutarimide but not by amide compounds which are conventional substrates and inducers of known amidases. The purified amidase showed high catalytic efficiency toward half-amides such as succinamic acid (Km = 6.2 mM; k cat = 5.76 s−1) and glutaramic acid (Km = 2.8 mM;k cat = 2.23 s−1). However, the substrates of known amidases such as short-chain (C2 to C4) aliphatic amides, long-chain (above C16) aliphatic amides, amino acid amides, aliphatic diamides, α-keto acid amides, N-carbamoyl amino acids, and aliphatic ureides were not substrates for the enzyme. Based on its high specificity toward half-amides, the enzyme was named half-amidase. This half-amidase exists as a monomer with an M r of 48,000 and was strongly inhibited by heavy metal ions and sulfhydryl reagents.

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