Escherichia intermedia

G. Para, P. Lucciardi, and J. Barrati, Synthesis of L-tyrosine by immobilized Escherichia intermedia cells, Appl. Microbiol. Biotechnol., 21 273 (1985). 

B-Tyrosinase has been crystallized from the cells of Escherichia intermedia and Erwinia herbicola and characterized to some extent in our laboratory. It has been... 

The conversion of D-glucose (17) into D-fructose (9) by a microbial enzyme (Scheme 5) was first reported in 1957 when Marshall and Kooi found glucose isomerase activity in cell-free extracts of Pseudomonas hydrophila (91. This enzymatic activity was enhanced in the presence of arsenate. Soon thereafter, other arsenate-requiring enzymes were isolated from Aerobacter sp. as well as Escherichia freundii [10]. Enzymes required arsenate when D-glucose or D-fructose was the substrate but not when the corresponding 6-phosphates 11 and 12 were offered. Purification of the arsenate-dependent principle component from Escherichia intermedia allowed the conclusion that the enzyme was a glucose 6-phosphate isomerase (EC 5.3.1.9) that was able to isomerise free D-glucose when it was complexed with arsenate [11]. 

Phenol is formed from L-tyrosine and its derivatives in some bacterial cultures not through a stepwise degradation of the molecule but through primary fission of the side chain. The L-tyrosine inducible enzyme L-tyrosine phenol lyase has been prepared in crystalline form from cell extracts of Escherichia intermedia A-21 and a molecular weight of 170000 was estimated . The enzyme catalyses the stoichiometric conversion of L-tyrosine (5) to phenol (20), pyruvate (21) and ammonia in the presence of added pyridoxal phosphate as a cofactor. Brot, Smit and Weissbach have described... 

---