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Comparative Biochemistry and Evolution of Aspartate Transcarbamoylase from Diverse Bacteria

Description: Aspartate transcarbamoylase (ATCase) catalyzes the first committed step in pyrimidine biosynthesis. Bacterial ATCases are divided into three classes, A, B and C. Class A ATCases are largest at 450-500, are. dodecamers and represented by Pseudomonas ATCase. The overlapping pyrBC' genes encode the Pseudomonases ATCase, which is active only as a 480 kDa dodecamer and requires an inactive pyrC'-encoded DHOase for ATCase activity. ATCase has been studied in two non-pathogenic members of Mycobacterium, M. smegmatis and M. phlei. Their ATCases are dodecamers of molecular weight 480 kDa, composed of six PyrB and six PyrC polypeptides. Unlike the Pseudomonas ATCase, the PyrC polypeptide in these mycobacteria encodes an active DHOase. Moreover, the ATCase: DHOase complex in M. smegmatis is active both as the native 480 kDa and as a 390 kDa complex. The latter lacks two PyrC polypeptides yet retains ATCase activity. The ATCase from M. phlei is similar, except that it is active as the native 480 kDa form but also as 450,410 and 380 kDa forms. These complexes lack one, two, and three PyrC polypeptides, respectively. By contrast,.ATCases from pathogenic mycobacteria are active only at 480 kDa. Mycobacterial ATCases contain active DHOases and accordingly. are placed in class A1 . The class A1 ATCases contain active DHOases while class A2 ATCases contain inactive DHOases. ATCase has also been purified from Burkholderia cepacia and from an E. coli strain in which the cloned pyrB of B. cepacia was expressed. The B. cepacia ATCase has a molecular mass of 550 kDa, with two different polypeptides, PyrB (52 kDa) and PyrC of (39 kDa). The enzyme is active both as the native enzyme at 550 kDa and as smaller molecular forms including 240 kDa and 165 kDa. The ATCase synthesized by the cloned pyrB gene has a molecular weight of 165 kDa composed ...
Date: May 1999
Creator: Hooshdaran, Massoumeh Ziba
Partner: UNT Libraries

Scientific Considerations of Olestra as a Fat Substitute

Description: Olestra is, a sucrose polyester, a noncaloric fat substitute, made from sucrose and several fatty acid esters. It has been approved by the FDA as a food additive used in preparing low-fat deep-frying foods such as savory snacks. Available literature on olestra was evaluated that had both positive and negative connotations. Clinical trials in numerous species of animals including humans were conducted to determine if olestra would affect the utilization and absorption of macro- and micronutrients; the effects of olestra on growth, reproduction, or its toxicity were also examined. The roles of olestra as a fat substitute, how it could effect on humans and the environment, and the potential impacts from its use in large amounts were assessed. Olestra can be removed from the environment by aerobic bacteria and fungi which may be isolated from activated sludge and soils.
Date: December 1999
Creator: Rattagool, Kullakan
Partner: UNT Libraries