1.13.11.3	DELTA319-322	turnover-number is 4.14fold lower than that of the wild-type enzyme, the Km-value for 3,4-dihydroxybenzoate is 2.1fold lower than that of the wild-type enzyme	657551	
1.13.11.3	additional information	immobilization of the enzyme in alginate gel shifts its optimum pH towards high-alkaline pH while immobilization of the enzyme on glyoxyl agarose does not influence pH-profile of the enzyme. Protocatechuate 3,4-dioygenase immobilized in calcium alginate shows increased activity towards 2,5-dihydroxybenzoate, caffeic acid, 2,3-dihydroxybenzoate, and 3,5-dihydroxybenzoate. Slightly lower activity of the enzyme is observed after its immobilization on glyoxyl agarose. Entrapment of the enzyme in alginate gel protects it against chelators and aliphatic alcohols while its immobilization on glyoxyl agarose enhanced enzyme resistance to inactivation by metal ions. Immobilization of dioxygenase in calcium alginate or on glyoxyl agarose results in decrease in the optimum temperature by 5°C and10°C, respectively. Activity of the enzyme immobilized on calcium alginate increases particularly towards 2,5-dihydroxybenzoate, caffeic acid, 2,3-dihydroxybenzoate, and 3,5-dihydroxybenzoate	-, 742046	
1.13.11.3	additional information	immobilization of the enzyme, the immobilized extract exhibited higher enzyme activity than the cell-free extract in the presence of trace elements and cations	726481	
1.13.11.3	additional information	mutants are constructed so that their pcaG genes contained variations in repeat sequence capable of producing a selectable phenotype following a specific deletion. Deletion frequencies of the various mutations is determined and compared with repair frequencies of three different single-base mutations.	671470	
1.13.11.3	R133H	gain of function mutation confers catechol 1,2-dioxygenase activity	-, 439509	
1.13.11.3	R133H	turnover-number is fold 500lower than that of the wild-type enzyme, the Km-value for 3,4-dihydroxybenzoate is 1.8fold higher than that of the wild-type enzyme	657551	
1.13.11.3	R142K	like wild-type no acticity of mutated protocatechuate 3,4-dioxygenase I with 4-sulfocatechol	439513	
1.13.11.3	R142K/W153V	protocatechuate 3,4-dioxygenase I gain of function mutation, mutant enzyme oxidizes 4-sulfocatechol	439513	
1.13.11.3	R153V	protocatechuate 3,4-dioxygenase I gain of function mutation, mutant enzyme oxidizes 4-sulfocatechol	439513	
1.13.11.3	R457S	turnover-number is 1333fold lower than that of the wild-type enzyme, the Km-value for 3,4-dihydroxybenzoate is 2.2fold lower than that of the wild-type enzyme	657551