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Journal Abstract Search
105 related items for PubMed ID: 5649516
1. Anaerobic degradation of lysine. V. Some properties of the cobamide coenzyme-dependent beta-lysine mutase of Clostridium sticklandii. Stadtman TC, Renz P. Arch Biochem Biophys; 1968 Apr; 125(1):226-39. PubMed ID: 5649516 [No Abstract] [Full Text] [Related]
2. Studies on the fermentation of D-alpha-lysine. Purification and properties of an adenosine triphosphate regulated B 12-coenzyme-dependent D-alpha-lysine mutase complex from Clostridium sticklandii. Morley CG, Stadtman TC. Biochemistry; 1970 Dec 08; 9(25):4890-900. PubMed ID: 5480154 [No Abstract] [Full Text] [Related]
3. Anaerobic degradation of lysine. IV. Cobamide coenzyme-dependent migration of an amino group from carbon 6 of beta-lysine (3,6-diaminohexanoate) to carbon 5 forming a new naturally occurring amino acid, 3,5-diaminohexanoate. Tsai L, Stadtman TC. Arch Biochem Biophys; 1968 Apr 08; 125(1):210-25. PubMed ID: 5649515 [No Abstract] [Full Text] [Related]
4. Identification and cobamide coenzyme-dependent formation of 3,5-diaminohexanoic acid, an intermediate in lysine fermentation. Dekker EE, Barker HA. J Biol Chem; 1968 Jun 25; 243(12):3232-7. PubMed ID: 4297779 [No Abstract] [Full Text] [Related]
6. Studies on the fermentation of p-alpha-lysine. On the hydrogen shift catalyzed by the B 12 coenzyme dependent D-alpha-lysine mutase. Morley CG, Stadtman TC. Biochemistry; 1971 Jun 08; 10(12):2325-9. PubMed ID: 5114991 [No Abstract] [Full Text] [Related]
17. Metabolic role of vitamin B12. Weissbach H, Taylor RT. Vitam Horm; 1968 Jun 15; 26():395-412. PubMed ID: 4887755 [No Abstract] [Full Text] [Related]
18. Purification and mechanism of action of proline racemase. Cardinale GJ, Abeles RH. Biochemistry; 1968 Nov 15; 7(11):3970-8. PubMed ID: 5722267 [No Abstract] [Full Text] [Related]
19. Formation and identification of 3-keto-5-aminohexanoic acid, a probable intermediate in lysine fermentation. Rimerman EA, Barker HA. J Biol Chem; 1968 Dec 10; 243(23):6151-60. PubMed ID: 4301989 [No Abstract] [Full Text] [Related]