Two structural types of mercury reductases and possible ways of their evolution.
Structural differences have been revealed among mercury reductases of immunologically unrelated types from Gram-positive bacteria: enzymes of one immunological type have a molecular mass of 62-69 kDa and seem to contain an N-terminal extension of 5-15 kDa, which is easily cleaved by trypsin and chymotrypsin; enzymes of the other immunological type have a molecular mass of 52-57 kDa and are resistant to proteolysis. The existence of at least two different lines in the evolution of mercury reductases is surmised.
Bogdanova
E S
ES
Institute of Molecular Genetics, USSR Academy of Sciences, Moscow.
Mindlin
S Z
SZ
D001173:Arthrobacter / Q000201:enzymology; D001407:Bacillus / Q000201:enzymology; D005075:Biological Evolution; D002918:Chymotrypsin; D004591:Electrophoresis, Polyacrylamide Gel; D015151:Immunoblotting; D008970:Molecular Weight; D009161:Mycobacterium / Q000201:enzymology; D010088:Oxidoreductases / Q000235:genetics / Q000378:metabolism; D013211:Staphylococcus aureus / Q000201:enzymology; D014357:Trypsin / Q000378:metabolism
D010088:Oxidoreductases; C021551:mercuric reductase; D002918:Chymotrypsin; D014357:Trypsin