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93 related items for PubMed ID: 11926997
1. Catalytic mechanism of beta-amylase from Bacillus cereus var. mycoides: chemical rescue of hydrolytic activity for a catalytic site mutant (Glu367-->Ala) by azide. Miyake H, Otsuka C, Nishimura S, Nitta Y. J Biochem; 2002 Apr; 131(4):587-91. PubMed ID: 11926997 [Abstract] [Full Text] [Related]
3. Crystal structure of beta-amylase from Bacillus cereus var. mycoides at 2.2 A resolution. Oyama T, Kusunoki M, Kishimoto Y, Takasaki Y, Nitta Y. J Biochem; 1999 Jun; 125(6):1120-30. PubMed ID: 10348915 [Abstract] [Full Text] [Related]
4. Structure of raw starch-digesting Bacillus cereus beta-amylase complexed with maltose. Mikami B, Adachi M, Kage T, Sarikaya E, Nanmori T, Shinke R, Utsumi S. Biochemistry; 1999 Jun 01; 38(22):7050-61. PubMed ID: 10353816 [Abstract] [Full Text] [Related]
6. Engineering of the pH optimum of Bacillus cereus beta-amylase: conversion of the pH optimum from a bacterial type to a higher-plant type. Hirata A, Adachi M, Utsumi S, Mikami B. Biochemistry; 2004 Oct 05; 43(39):12523-31. PubMed ID: 15449941 [Abstract] [Full Text] [Related]
7. Crystal structures of beta-amylase from Bacillus cereus var mycoides in complexes with substrate analogs and affinity-labeling reagents. Oyama T, Miyake H, Kusunoki M, Nitta Y. J Biochem; 2003 Apr 05; 133(4):467-74. PubMed ID: 12761294 [Abstract] [Full Text] [Related]
13. Cloning, sequencing, and expression of a beta-amylase gene from Bacillus cereus var. mycoides and characterization of its products. Yamaguchi T, Matsumoto Y, Shirakawa M, Kibe M, Hibino T, Kozaki S, Takasaki Y, Nitta Y. Biosci Biotechnol Biochem; 1996 Aug 05; 60(8):1255-9. PubMed ID: 8987540 [Abstract] [Full Text] [Related]
14. Expression and site-directed mutagenesis of the phosphatidylcholine-preferring phospholipase C of Bacillus cereus: probing the role of the active site Glu146. Martin SF, Spaller MR, Hergenrother PJ. Biochemistry; 1996 Oct 01; 35(39):12970-7. PubMed ID: 8841144 [Abstract] [Full Text] [Related]
16. General base catalysis by the phosphatidylcholine-preferring phospholipase C from Bacillus cereus: the role of Glu4 and Asp55. Martin SF, Hergenrother PJ. Biochemistry; 1998 Apr 21; 37(16):5755-60. PubMed ID: 9548962 [Abstract] [Full Text] [Related]
18. Structural analysis of threonine 342 mutants of soybean beta-amylase: role of a conformational change of the inner loop in the catalytic mechanism. Kang YN, Tanabe A, Adachi M, Utsumi S, Mikami B. Biochemistry; 2005 Apr 05; 44(13):5106-16. PubMed ID: 15794648 [Abstract] [Full Text] [Related]
19. Engineering of the nonspecific phospholipase C from Bacillus cereus: replacement of glutamic acid-4 by alanine results in loss of interfacial catalysis and enhanced phosphomonoesterase activity. Tan CA, Roberts MF. Biochemistry; 1998 Mar 24; 37(12):4275-9. PubMed ID: 9521750 [Abstract] [Full Text] [Related]