Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(3-hydroxy-phenylalkanoic acid)n + H2O
(3-hydroxy-phenylalkanoic acid)n-x + 3-hydroxy-phenylalkanoic acid
-
novel natural aromatic plastic with an even number of carbon atoms
-
?
(R)-3-[[(3'R)-3'-hydroxybutanoyl]oxy]butanoic acid + H2O
(R)-3-hydroxybutanoic acid
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
4-nitrophenyl butanoate + H2O
4-nitrophenol + butanoate
-
wild type lipase activity is rather low
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
4-nitrophenyl hexanoate + H2O
4-nitrophenol + hexanoate
4-nitrophenyl octanoate + H2O
4-nitrophenol + octanoate
4-nitrophenyl pentanoate + H2O
4-nitrophenol + pentanoate
4-nitrophenyl propionate + H2O
4-nitrophenol + propionate
4-nitrophenyl valerate + H2O
4-nitrophenol + valerate
cyclic [(R)-3-hydroxybutanoate]3 + H2O
?
-
-
-
-
?
cyclic [(R)-3-hydroxybutanoate]5 + H2O
?
methyl (3R)-3-[[(3'R)-3'-hydroxybutanoyl]oxy]butanoate + H2O
(R)-3-hydroxybutanoic acid + methyl-(R)-3-hydroxybutanoate + (R)-3-[[(3'R)-3'-hydroxybutanoyl]oxy]butanoic acid
methyl (3R)-3-[[(3'R)-3'-methoxybutanoyl]oxy]butanoate + H2O
(R)-3-methoxybutanoic acid + methyl-(R)-3-hydroxybutanoate + methyl-[[(R)-3-methoxybutanoyl]oxy]butanoate
-
-
-
?
methyl (3R)-3-[[(3'R)-3'-[[(3''R)-3''-hydroxybutanoyl]oxy]butanoyl]oxy]butanoate + H2O
(R)-3-hydroxybutanoic acid + methyl-(R)-3-hydroxybutanoate + (R)-3-[[(3'R)-3'-hydroxybutanoyl]oxy]butanoic acid + methyl (3R)-3-[[(3'R)-3'-hydroxybutanoyl]oxy]butanoate + (R)-3-[[(3'R)-3'-[[(3''R)-3''-hydroxybutanoyl]oxy]butanoyl]oxy]butanoic acid
-
-
-
?
methyl (3R)-3-[[(3'R)-3'-[[(3''R)-3''-[[(3'''R)-3'''-hydroxybutanoyl]oxy]butanoyl]oxy]butanoyl]oxy]butanoate + H2O
(R)-3-hydroxybutanoic acid + methyl-(R)-3-hydroxybutanoate + (R)-3-[[(3'R)-3'-hydroxybutanoyl]oxy]butanoic acid + methyl (3R)-3-[[(3'R)-3'-hydroxybutanoyl]oxy]butanoate + (R)-3-[[(3'R)-3'-[[(3''R)-3''-hydroxybutanoyl]oxy]butanoyl]oxy]butanoic acid + methyl (3R)-3-[[(3'R)-3'-[[(3''R)-3''-[[(3'''R)-3'''-hydroxybutanoyl]oxy]butanoyl]oxy]butanoyl]oxy]butanoate
-
-
-
?
p-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
?
p-nitrophenyl acetate + H2O
p-nitrophenol + acetate
p-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
-
-
?
p-nitrophenyl butyrate + H2O
p-nitrophenol + butyrate
p-nitrophenyl laurate + H2O
p-nitrophenol + laurate
-
-
-
-
?
p-nitrophenyl myristate + H2O
4-nitrophenol + myristate
-
-
-
?
p-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
-
-
-
?
p-nitrophenyl valerate + H2O
4-nitrophenol + pentanoate
-
-
-
?
p-nitrophenyl-decanoate + H2O
p-nitrophenol + decanoate
-
wild type lipase activity is rather low
-
-
?
p-nitrophenyl-palmitate + H2O
p-nitrophenol + palmitate
-
wild type lipase activity is rather low
-
-
?
p-nitrophenyldecanoate + H2O
p-nitrophenol + decanoate
-
-
-
-
?
PEG containing poly(3-hydroxybutyrate-co-3-hydroxyvalerate) + H2O
?
poly (3-hydroxybutanoate) n + n H2O
poly (3-hydroxybutanoate) n-1 + (R)-3-hydroxybutanoate
-
-
-
-
?
poly (3-hydroxybutyrate) + H2O
?
poly((R)-3-hydroxybutyrate) + H2O
?
poly(2-hydroxybutanoate) + H2O
2-hydroxybutanoate + ?
-
-
-
-
?
poly(3-hydroxybutanoate) + H2O
?
poly(3-hydroxybutanoate-co-3-hydroxyvalerate) + H2O
?
poly(3-hydroxybutyrate) + H2O
3-hydroxybutyrate + 3-hydroxybutyryl-3-hydroxybutyrate
poly(3-hydroxybutyrate) + H2O
?
poly(3-hydroxybutyrate-co-3-hydroxyvalerate) + H2O
?
poly(3-hydroxybutyrate-co-3-hydroxyvalerate)n + H2O
poly(3-hydroxybutyrate-co-3-hydroxyvalerate)n-x + poly(3-hydroxybutyrate-co-3-hydroxyvalerate)
poly(3-hydroxybutyrate-co-4-hydroxybutyrate) + H2O
?
poly(3-hydroxybutyrate-co-[12%]3-hydroxyvalerate)n + H2O
poly(3-hydroxybutyrate-co-[12%]3-hydroxyvalerate)n-x + poly(3-hydroxybutyrate-co-[12%]3-hydroxyvalerate)n
poly(3-hydroxybutyrate-co-[14%]3-hydroxyvalerate)n + H2O
poly(3-hydroxybutyrate-co-[14%]3-hydroxyvalerate)n-x + poly(3-hydroxybutyrate-co-[14%]3-hydroxyvalerate)
-
-
-
?
poly(3-hydroxybutyrate-co-[22%]3-hydroxyvalerate)n + H2O
poly(3-hydroxybutyrate-co-[22%]3-hydroxyvalerate)n-x + poly(3-hydroxybutyrate-co-[22%]3-hydroxyvalerate)
-
best carbon source for enzyme synthesis in strain W6
-
?
poly(3-hydroxybutyrate-co-[43%]3-hydroxyvalerate)n + H2O
poly(3-hydroxybutyrate-co-[43%]3-hydroxyvalerate)n-x + poly(3-hydroxybutyrate-co-[43%]3-hydroxyvalerate)
poly(3-hydroxybutyrate-co-[9%]3-hydroxyvalerate)n + H2O
poly(3-hydroxybutyrate-co-[9%]3-hydroxyvalerate)n-x + poly(3-hydroxybutyrate-co-[9%]3-hydroxyvalerate)n
poly(3-hydroxybutyric acid) + H2O
?
poly(3-hydroxypropionate) + H2O
?
poly(3-hydroxypropionate)n + H2O
poly(3-hydroxypropionate)n-x + poly(3-propionate)
poly(3-hydroxyvalerate)n + H2O
poly(3-hydroxyvalerate)n-x + poly(3-hydroxyvalerate)
poly(4-hydroxybutyrate)n + H2O
poly(4-hydroxybutyrate)n-x + poly(4-hydroxybutyrate)
poly(4-hydroxybutyrate)n + H2O
poly(4-hydroxybutyrate)n-x + poly(4-hydroxybutyrate)x
-
-
-
?
poly(beta-propiolactone) + H2O
?
-
-
-
-
?
poly(butylene succinate) + H2O
?
poly(butylene succinate-co-adipate)n + H2O
?
-
-
-
?
poly(caprolactone)n + H2O
?
-
-
-
?
poly(ethylene adipate)n + H2O
poly(ethylene adipate)n-x + poly(ethylene adipate)
poly(ethylene succinate) + H2O
?
poly(ethylene succinate)n + H2O
poly(ethylene succinate)n-x + poly(ethylene succinate)
poly(L-lactic acid) + H2O
?
poly(lactic acid) + H2O
?
poly(lactic acid)n + H2O
?
-
-
-
?
poly(propiolactone)n + H2O
poly(propiolactone)n-x + poly(propiolactone)n
poly(R)-3-hydroxybutyrate + H2O
?
poly-3-hydroxybutyrate + H2O
?
-
-
-
-
?
poly-[(R)-3-hydroxybutyrate] + H2O
?
degradation of poly-[(R)-3-hydroxybutyrate] (PHB) films
-
-
?
polyhydroxyalkanoate + H2O
?
-
-
-
-
?
polyhydroxybutyrate + H2O
3-hydroxybutyrate + ?
-
-
-
-
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
[(R)-3-hydroxybutanoate]3 + H2O
?
[(R)-3-hydroxybutanoate]4 + H2O
?
[(R)-3-hydroxybutanoate]5 + H2O
?
[(R)-3-hydroxybutanoate]6 + H2O
?
-
-
-
-
?
[(R)-3-hydroxybutanoate]n + H2O
[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]
[(R)-3-hydroxybutanoate]n + H2O
[(R)-3-hydroxybutanoate]n-x + [(R)-3-hydroxybutanoate]x
additional information
?
-
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
-
-
-
?
4-nitrophenyl hexanoate + H2O
4-nitrophenol + hexanoate
-
wild type lipase activity is rather low
-
-
?
4-nitrophenyl hexanoate + H2O
4-nitrophenol + hexanoate
-
-
-
?
4-nitrophenyl hexanoate + H2O
4-nitrophenol + hexanoate
-
-
-
?
4-nitrophenyl hexanoate + H2O
4-nitrophenol + hexanoate
-
-
-
-
?
4-nitrophenyl octanoate + H2O
4-nitrophenol + octanoate
-
-
-
?
4-nitrophenyl octanoate + H2O
4-nitrophenol + octanoate
-
wild type lipase activity is rather low
-
-
?
4-nitrophenyl pentanoate + H2O
4-nitrophenol + pentanoate
-
-
-
?
4-nitrophenyl pentanoate + H2O
4-nitrophenol + pentanoate
-
-
-
?
4-nitrophenyl propionate + H2O
4-nitrophenol + propionate
-
-
-
?
4-nitrophenyl propionate + H2O
4-nitrophenol + propionate
-
-
-
?
4-nitrophenyl propionate + H2O
4-nitrophenol + propionate
-
-
-
-
?
4-nitrophenyl valerate + H2O
4-nitrophenol + valerate
-
-
-
?
4-nitrophenyl valerate + H2O
4-nitrophenol + valerate
-
-
-
?
4-nitrophenyl valerate + H2O
4-nitrophenol + valerate
-
-
-
-
?
4-nitrophenyl valerate + H2O
4-nitrophenol + valerate
-
-
-
-
?
cyclic [(R)-3-hydroxybutanoate]5 + H2O
?
-
-
-
-
?
cyclic [(R)-3-hydroxybutanoate]5 + H2O
?
-
-
-
-
?
methyl (3R)-3-[[(3'R)-3'-hydroxybutanoyl]oxy]butanoate + H2O
(R)-3-hydroxybutanoic acid + methyl-(R)-3-hydroxybutanoate + (R)-3-[[(3'R)-3'-hydroxybutanoyl]oxy]butanoic acid
-
-
-
?
methyl (3R)-3-[[(3'R)-3'-hydroxybutanoyl]oxy]butanoate + H2O
(R)-3-hydroxybutanoic acid + methyl-(R)-3-hydroxybutanoate + (R)-3-[[(3'R)-3'-hydroxybutanoyl]oxy]butanoic acid
-
-
-
?
methyl (3R)-3-[[(3'R)-3'-hydroxybutanoyl]oxy]butanoate + H2O
(R)-3-hydroxybutanoic acid + methyl-(R)-3-hydroxybutanoate + (R)-3-[[(3'R)-3'-hydroxybutanoyl]oxy]butanoic acid
-
-
-
?
p-nitrophenyl acetate + H2O
p-nitrophenol + acetate
-
-
-
-
?
p-nitrophenyl acetate + H2O
p-nitrophenol + acetate
-
-
-
-
?
p-nitrophenyl acetate + H2O
p-nitrophenol + acetate
-
-
-
-
?
p-nitrophenyl acetate + H2O
p-nitrophenol + acetate
-
-
-
?
p-nitrophenyl acetate + H2O
p-nitrophenol + acetate
-
-
-
?
p-nitrophenyl butyrate + H2O
p-nitrophenol + butyrate
-
-
-
-
?
p-nitrophenyl butyrate + H2O
p-nitrophenol + butyrate
-
-
-
-
?
p-nitrophenyl butyrate + H2O
p-nitrophenol + butyrate
-
-
-
-
?
p-nitrophenyl butyrate + H2O
p-nitrophenol + butyrate
-
-
-
?
p-nitrophenyl butyrate + H2O
p-nitrophenol + butyrate
-
-
-
?
PEG containing poly(3-hydroxybutyrate-co-3-hydroxyvalerate) + H2O
?
-
the relative substrate specificity of the i-PHA depolymerase of MAL-201 is poly(3-hydroxybutyric acid) > poly(3-hydroxybutyrate-co-3-hydroxyvalerate) > PHBVPEG copolymer
-
-
?
PEG containing poly(3-hydroxybutyrate-co-3-hydroxyvalerate) + H2O
?
-
the relative substrate specificity of the i-PHA depolymerase of MAL-201 is poly(3-hydroxybutyric acid) > poly(3-hydroxybutyrate-co-3-hydroxyvalerate) > PHBVPEG copolymer
-
-
?
poly (3-hydroxybutyrate) + H2O
?
-
-
-
-
?
poly (3-hydroxybutyrate) + H2O
?
-
-
-
-
?
poly (3-hydroxybutyrate) + H2O
?
-
-
-
-
?
poly (3-hydroxybutyrate) + H2O
?
-
-
-
-
?
poly((R)-3-hydroxybutyrate) + H2O
?
-
-
-
-
?
poly((R)-3-hydroxybutyrate) + H2O
?
-
-
-
?
poly(3-hydroxybutanoate) + H2O
?
-
-
-
-
?
poly(3-hydroxybutanoate) + H2O
?
-
-
-
-
?
poly(3-hydroxybutanoate) + H2O
?
-
-
-
-
?
poly(3-hydroxybutanoate) + H2O
?
-
recombinant enzyme has a stronger binding affinity for poly(3-hydroxybutanoate) than native enzyme
-
-
?
poly(3-hydroxybutanoate) + H2O
?
-
-
-
-
?
poly(3-hydroxybutanoate) + H2O
?
-
-
-
-
?
poly(3-hydroxybutanoate-co-3-hydroxyvalerate) + H2O
?
-
-
-
-
?
poly(3-hydroxybutanoate-co-3-hydroxyvalerate) + H2O
?
-
18 mol% hydroxyvalerate content
-
-
?
poly(3-hydroxybutyrate) + H2O
3-hydroxybutyrate + 3-hydroxybutyryl-3-hydroxybutyrate
average molecular mass of 437 kDa
-
-
?
poly(3-hydroxybutyrate) + H2O
3-hydroxybutyrate + 3-hydroxybutyryl-3-hydroxybutyrate
average molecular mass of 437 kDa
-
-
?
poly(3-hydroxybutyrate) + H2O
?
-
-
-
-
?
poly(3-hydroxybutyrate) + H2O
?
-
-
-
-
?
poly(3-hydroxybutyrate) + H2O
?
-
-
-
?
poly(3-hydroxybutyrate) + H2O
?
-
-
-
?
poly(3-hydroxybutyrate) + H2O
?
-
-
-
?
poly(3-hydroxybutyrate) + H2O
?
-
-
-
?
poly(3-hydroxybutyrate) + H2O
?
-
-
-
?
poly(3-hydroxybutyrate) + H2O
?
-
-
-
-
?
poly(3-hydroxybutyrate) + H2O
?
intracellular native poly(3-hydroxybutyrate) granules in vitro are rapidly degraded without the need for protease treatment. Almost all the final hydrolytic products produced from the in vitro degradation of nPHB granules by PhaZ1 are 3-hydroxybutyric acid monomers. PhaZ1 is also able to hydrolyze denatured semicrystalline poly(3-hydroxybutyrate), with the generation of 3-hydroxybutyric acid monomers
-
-
?
poly(3-hydroxybutyrate) + H2O
?
-
-
-
-
?
poly(3-hydroxybutyrate) + H2O
?
-
-
-
-
?
poly(3-hydroxybutyrate) + H2O
?
-
-
-
?
poly(3-hydroxybutyrate) + H2O
?
-
-
-
?
poly(3-hydroxybutyrate) + H2O
?
-
-
-
-
?
poly(3-hydroxybutyrate) + H2O
?
-
-
-
-
?
poly(3-hydroxybutyrate) + H2O
?
-
-
-
-
?
poly(3-hydroxybutyrate) + H2O
?
-
-
-
-
?
poly(3-hydroxybutyrate) + H2O
?
-
-
-
-
?
poly(3-hydroxybutyrate) + H2O
?
-
-
-
-
?
poly(3-hydroxybutyrate) + H2O
?
-
-
-
-
?
poly(3-hydroxybutyrate) + H2O
?
-
-
-
-
?
poly(3-hydroxybutyrate) + H2O
?
-
-
-
-
?
poly(3-hydroxybutyrate) + H2O
?
-
-
-
-
?
poly(3-hydroxybutyrate) + H2O
?
-
-
-
-
?
poly(3-hydroxybutyrate) + H2O
?
-
-
-
-
?
poly(3-hydroxybutyrate) + H2O
?
-
-
-
-
?
poly(3-hydroxybutyrate) + H2O
?
-
-
-
-
?
poly(3-hydroxybutyrate-co-3-hydroxyvalerate) + H2O
?
-
-
-
-
?
poly(3-hydroxybutyrate-co-3-hydroxyvalerate) + H2O
?
-
-
-
-
?
poly(3-hydroxybutyrate-co-3-hydroxyvalerate) + H2O
?
-
-
-
-
?
poly(3-hydroxybutyrate-co-3-hydroxyvalerate) + H2O
?
-
-
-
-
?
poly(3-hydroxybutyrate-co-3-hydroxyvalerate) + H2O
?
-
-
-
-
?
poly(3-hydroxybutyrate-co-3-hydroxyvalerate) + H2O
?
-
-
-
-
?
poly(3-hydroxybutyrate-co-3-hydroxyvalerate) + H2O
?
-
-
-
-
?
poly(3-hydroxybutyrate-co-3-hydroxyvalerate) + H2O
?
-
-
-
-
?
poly(3-hydroxybutyrate-co-3-hydroxyvalerate) + H2O
?
substrate co-polymer with 5 or 12% (wt) 3-hydroxyvalerate
-
-
?
poly(3-hydroxybutyrate-co-3-hydroxyvalerate) + H2O
?
substrate co-polymer with 5 or 12% (wt) 3-hydroxyvalerate
-
-
?
poly(3-hydroxybutyrate-co-3-hydroxyvalerate) + H2O
?
-
-
-
-
?
poly(3-hydroxybutyrate-co-3-hydroxyvalerate) + H2O
?
-
-
-
-
?
poly(3-hydroxybutyrate-co-3-hydroxyvalerate) + H2O
?
-
-
-
-
?
poly(3-hydroxybutyrate-co-3-hydroxyvalerate) + H2O
?
-
-
-
-
?
poly(3-hydroxybutyrate-co-3-hydroxyvalerate) + H2O
?
-
with 5 or 12 mol% 3-hydroxyvalerate content
-
-
?
poly(3-hydroxybutyrate-co-3-hydroxyvalerate) + H2O
?
-
with 5 or 12 mol% 3-hydroxyvalerate content
-
-
?
poly(3-hydroxybutyrate-co-3-hydroxyvalerate) + H2O
?
-
-
-
-
?
poly(3-hydroxybutyrate-co-3-hydroxyvalerate) + H2O
?
-
-
-
-
?
poly(3-hydroxybutyrate-co-3-hydroxyvalerate) + H2O
?
-
-
-
-
?
poly(3-hydroxybutyrate-co-3-hydroxyvalerate) + H2O
?
-
-
-
-
?
poly(3-hydroxybutyrate-co-3-hydroxyvalerate) + H2O
?
-
-
-
-
?
poly(3-hydroxybutyrate-co-3-hydroxyvalerate) + H2O
?
-
-
-
-
?
poly(3-hydroxybutyrate-co-3-hydroxyvalerate) + H2O
?
-
-
-
-
?
poly(3-hydroxybutyrate-co-3-hydroxyvalerate) + H2O
?
-
poly(3-hydroxybutyrate-co-3-hydroxyvalerate) pof MW 43000 Da and 42000 Da
-
-
?
poly(3-hydroxybutyrate-co-3-hydroxyvalerate) + H2O
?
-
-
-
-
?
poly(3-hydroxybutyrate-co-3-hydroxyvalerate)n + H2O
poly(3-hydroxybutyrate-co-3-hydroxyvalerate)n-x + poly(3-hydroxybutyrate-co-3-hydroxyvalerate)
-
BIOPOL
-
?
poly(3-hydroxybutyrate-co-3-hydroxyvalerate)n + H2O
poly(3-hydroxybutyrate-co-3-hydroxyvalerate)n-x + poly(3-hydroxybutyrate-co-3-hydroxyvalerate)
-
3-hydroxyvalerate composition can vary from 7-65 mol%
-
?
poly(3-hydroxybutyrate-co-3-hydroxyvalerate)n + H2O
poly(3-hydroxybutyrate-co-3-hydroxyvalerate)n-x + poly(3-hydroxybutyrate-co-3-hydroxyvalerate)
-
BIOPOL
-
?
poly(3-hydroxybutyrate-co-3-hydroxyvalerate)n + H2O
poly(3-hydroxybutyrate-co-3-hydroxyvalerate)n-x + poly(3-hydroxybutyrate-co-3-hydroxyvalerate)
-
BIOPOL
-
?
poly(3-hydroxybutyrate-co-4-hydroxybutyrate) + H2O
?
-
-
-
?
poly(3-hydroxybutyrate-co-4-hydroxybutyrate) + H2O
?
-
-
-
?
poly(3-hydroxybutyrate-co-4-hydroxybutyrate) + H2O
?
-
-
-
-
?
poly(3-hydroxybutyrate-co-4-hydroxybutyrate) + H2O
?
-
-
-
-
?
poly(3-hydroxybutyrate-co-[12%]3-hydroxyvalerate)n + H2O
poly(3-hydroxybutyrate-co-[12%]3-hydroxyvalerate)n-x + poly(3-hydroxybutyrate-co-[12%]3-hydroxyvalerate)n
-
-
-
?
poly(3-hydroxybutyrate-co-[12%]3-hydroxyvalerate)n + H2O
poly(3-hydroxybutyrate-co-[12%]3-hydroxyvalerate)n-x + poly(3-hydroxybutyrate-co-[12%]3-hydroxyvalerate)n
-
-
-
?
poly(3-hydroxybutyrate-co-[43%]3-hydroxyvalerate)n + H2O
poly(3-hydroxybutyrate-co-[43%]3-hydroxyvalerate)n-x + poly(3-hydroxybutyrate-co-[43%]3-hydroxyvalerate)
-
-
-
?
poly(3-hydroxybutyrate-co-[43%]3-hydroxyvalerate)n + H2O
poly(3-hydroxybutyrate-co-[43%]3-hydroxyvalerate)n-x + poly(3-hydroxybutyrate-co-[43%]3-hydroxyvalerate)
-
-
-
?
poly(3-hydroxybutyrate-co-[9%]3-hydroxyvalerate)n + H2O
poly(3-hydroxybutyrate-co-[9%]3-hydroxyvalerate)n-x + poly(3-hydroxybutyrate-co-[9%]3-hydroxyvalerate)n
-
-
-
?
poly(3-hydroxybutyrate-co-[9%]3-hydroxyvalerate)n + H2O
poly(3-hydroxybutyrate-co-[9%]3-hydroxyvalerate)n-x + poly(3-hydroxybutyrate-co-[9%]3-hydroxyvalerate)n
-
-
-
?
poly(3-hydroxybutyric acid) + H2O
?
-
-
-
-
?
poly(3-hydroxybutyric acid) + H2O
?
-
-
-
-
?
poly(3-hydroxybutyric acid) + H2O
?
-
-
-
-
?
poly(3-hydroxybutyric acid) + H2O
?
-
-
-
-
?
poly(3-hydroxybutyric acid) + H2O
?
-
-
-
-
?
poly(3-hydroxybutyric acid) + H2O
?
-
-
-
-
?
poly(3-hydroxybutyric acid) + H2O
?
-
-
-
-
?
poly(3-hydroxybutyric acid) + H2O
?
-
-
-
-
?
poly(3-hydroxybutyric acid) + H2O
?
-
-
-
-
?
poly(3-hydroxybutyric acid) + H2O
?
-
-
-
-
?
poly(3-hydroxypropionate) + H2O
?
-
-
-
-
?
poly(3-hydroxypropionate) + H2O
?
-
-
-
-
?
poly(3-hydroxypropionate) + H2O
?
-
-
-
-
?
poly(3-hydroxypropionate) + H2O
?
-
-
-
-
?
poly(3-hydroxypropionate) + H2O
?
-
-
-
-
?
poly(3-hydroxypropionate) + H2O
?
-
-
-
-
?
poly(3-hydroxypropionate) + H2O
?
-
-
-
-
?
poly(3-hydroxypropionate) + H2O
?
-
-
-
-
?
poly(3-hydroxypropionate)n + H2O
poly(3-hydroxypropionate)n-x + poly(3-propionate)
-
-
-
?
poly(3-hydroxypropionate)n + H2O
poly(3-hydroxypropionate)n-x + poly(3-propionate)
-
-
-
?
poly(3-hydroxypropionate)n + H2O
poly(3-hydroxypropionate)n-x + poly(3-propionate)
-
-
-
?
poly(3-hydroxyvalerate)n + H2O
poly(3-hydroxyvalerate)n-x + poly(3-hydroxyvalerate)
-
-
-
?
poly(3-hydroxyvalerate)n + H2O
poly(3-hydroxyvalerate)n-x + poly(3-hydroxyvalerate)
-
-
-
?
poly(3-hydroxyvalerate)n + H2O
poly(3-hydroxyvalerate)n-x + poly(3-hydroxyvalerate)
-
highest activity for poly(3-hydroxyvaleric acid) depolymerase, low activity for poly(3-hydroxybutyrate) depolymerases A and B
-
?
poly(3-hydroxyvalerate)n + H2O
poly(3-hydroxyvalerate)n-x + poly(3-hydroxyvalerate)
-
highest activity for PhaZ6 protein
-
?
poly(4-hydroxybutyrate)n + H2O
poly(4-hydroxybutyrate)n-x + poly(4-hydroxybutyrate)
-
-
-
?
poly(4-hydroxybutyrate)n + H2O
poly(4-hydroxybutyrate)n-x + poly(4-hydroxybutyrate)
-
-
-
?
poly(4-hydroxybutyrate)n + H2O
poly(4-hydroxybutyrate)n-x + poly(4-hydroxybutyrate)
-
-
-
?
poly(butylene succinate) + H2O
?
-
-
-
-
?
poly(butylene succinate) + H2O
?
-
-
-
-
?
poly(ethylene adipate)n + H2O
poly(ethylene adipate)n-x + poly(ethylene adipate)
-
-
-
?
poly(ethylene adipate)n + H2O
poly(ethylene adipate)n-x + poly(ethylene adipate)
-
-
-
?
poly(ethylene adipate)n + H2O
poly(ethylene adipate)n-x + poly(ethylene adipate)
-
-
-
?
poly(ethylene succinate) + H2O
?
-
-
-
-
?
poly(ethylene succinate) + H2O
?
-
-
-
-
?
poly(ethylene succinate) + H2O
?
-
-
-
-
?
poly(ethylene succinate)n + H2O
poly(ethylene succinate)n-x + poly(ethylene succinate)
-
-
-
?
poly(ethylene succinate)n + H2O
poly(ethylene succinate)n-x + poly(ethylene succinate)
-
-
-
?
poly(ethylene succinate)n + H2O
poly(ethylene succinate)n-x + poly(ethylene succinate)
-
-
-
?
poly(L-lactic acid) + H2O
?
-
-
-
?
poly(L-lactic acid) + H2O
?
-
-
-
?
poly(lactic acid) + H2O
?
-
-
-
-
?
poly(lactic acid) + H2O
?
-
-
-
-
?
poly(propiolactone)n + H2O
poly(propiolactone)n-x + poly(propiolactone)n
-
-
-
?
poly(propiolactone)n + H2O
poly(propiolactone)n-x + poly(propiolactone)n
-
-
-
?
poly(R)-3-hydroxybutyrate + H2O
?
-
-
-
?
poly(R)-3-hydroxybutyrate + H2O
?
-
-
-
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
-
-
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
-
-
-
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
linear 3-hydroxybutyrate dimer, trimer, tetramer, pentamer, cyclic 3-hydroxybutyrate trimer, pentamer, hexamer
-
-
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
-
-
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
-
-
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
-
-
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
-
-
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
-
main products: dimer and trimer
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
consists of two domains of poly(3-hydroxybutyrate)-specific and poly(3-hydroxyvalerate)-specific binding
-
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
-
main products: dimer and trimer
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
consists of two domains of poly(3-hydroxybutyrate)-specific and poly(3-hydroxyvalerate)-specific binding
-
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
-
-
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
-
-
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
-
-
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
-
-
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
PhaZ can function as a PHB depolymerase in vivo
-
-
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
purified His-tagged PhaZ can efficiently degrade trypsin-activated native poly-3-hydroxybutyrate granules as well as artificial amorphous poly-3-hydroxybutyrate granules and release 3-hydroxybutyrate monomer as a hydrolytic product, but it can not hydrolyze denatured semicrystalline poly-3-hydroxybutyrate
-
-
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
-
-
-
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
degradation of amorphous poly(3-hydroxybutyrate), 3-hydroxybutyrate tetramer and pentamer, but not crystalline poly(3-hydroxybutyrate)
-
-
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
-
-
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
-
-
-
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
no hydrolysis of crystalline poly(3-hydroxybutyrate)
mainly oligomeric and some monomeric release of D(-)-3-hydroxybutyrate
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
specific for amorphous poly(3-hydroxybutyrate)
mainly 3-hydroxybutyrate oligomers
-
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
specific for amorphous poly(3-hydroxybutyrate) granules
-
-
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
linear 3-hydroxybutyrate dimer, trimer, tetramer, pentamer, cyclic 3-hydroxybutyrate trimer, pentamer, hexamer
-
-
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
specific for amorphous poly(3-hydroxybutyrate) granules, weak activity on 3-hydroxybutyrate dimers and trimers, no activity on tetramers or pentamers
-
-
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
-
-
-
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
linear 3-hydroxybutyrate dimer, trimer, tetramer, pentamer, cyclic 3-hydroxybutyrate trimer, pentamer, hexamer
-
-
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
no hydrolysis of crystalline poly(3-hydroxybutyrate)
mainly oligomeric and some monomeric release of D(-)-3-hydroxybutyrate
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
specific for amorphous poly(3-hydroxybutyrate) granules
-
-
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
specific for amorphous poly(3-hydroxybutyrate) granules, weak activity on 3-hydroxybutyrate dimers and trimers, no activity on tetramers or pentamers
-
-
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
-
-
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
-
main products: dimer and monomer
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
-
-
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
-
-
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
-
main products: dimer and monomer
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
-
-
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
-
-
-
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
highest activities for poly(3-hydroxybutyrate) depolymerases A and B, low activity for poly(3-hydroxyvaleric acid) depolymerase
-
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
highest activities for PhaZ1-5 proteins
-
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
specific for amorphous PHB
-
-
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
specific for amorphous poly(3-hydroxbutyrate)
-
-
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
specific for amorphous poly(3-hydroxybutyrate)
-
-
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
specific for amorphous poly(3-hydroxbutyrate), inhibits hydrolysis of crystalline poly(3-hydroxbutyrate) by PHB depolymerases PhaZ2 and PhaZ5
-
-
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
-
-
-
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
-
-
-
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
-
-
-
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
activity of mutant strain DS9713a-01 obtained by ultraviolet light mutagenesis is 97% higher than that of the wild-type strain. The DS9713a-01 mutant can completely degrade PHB films in 5 days. The wild-type strain achieves only 61% at the same time. The primary product is the monomer, 3-hydroxybutyric acid
-
-
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
-
-
-
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
activity of mutant strain DS9713a-01 obtained by ultraviolet light mutagenesis is 97% higher than that of the wild-type strain. The DS9713a-01 mutant can completely degrade PHB films in 5 days. The wild-type strain achieves only 61% at the same time. The primary product is the monomer, 3-hydroxybutyric acid
-
-
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
the addition of PHB to the medium leads to a sixfold increase in PhaZBm mRNA, while the presence of glucose represses phaZBm expression
-
-
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
the addition of PHB to the medium leads to a sixfold increase in PhaZBm mRNA, while the presence of glucose represses phaZBm expression
-
-
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
-
-
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
-
-
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
-
-
-
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
linear 3-hydroxbutyrate dimer, trimer, tetramer, pentamer, cyclic 3-hydroxbutyrate trimer, pentamer, hexamer
-
-
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
-
-
-
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
linear 3-hydroxbutyrate dimer, trimer, tetramer, pentamer, cyclic 3-hydroxbutyrate trimer, pentamer, hexamer
-
-
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
-
-
-
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
highly specific for oligomers or polymers of 3-hydroxybutyrate in the (R) configuration
-
-
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
-
-
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
-
-
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
-
-
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
-
3-hydroxybutyrate as only product detected, 3-hydroxybutyrate as sole product detected
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
-
3-hydroxybutyrate as only product detected, 3-hydroxybutyrate as sole product detected
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
degradation mainly to D-3-hydroxybutyric acid monomer
-
-
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
-
-
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
-
-
-
?
[(R)-3-hydroxybutanoate]3 + H2O
?
-
-
-
-
?
[(R)-3-hydroxybutanoate]3 + H2O
?
-
-
-
-
?
[(R)-3-hydroxybutanoate]4 + H2O
?
-
-
-
-
?
[(R)-3-hydroxybutanoate]4 + H2O
?
-
-
-
-
?
[(R)-3-hydroxybutanoate]5 + H2O
?
-
-
-
-
?
[(R)-3-hydroxybutanoate]5 + H2O
?
-
-
-
-
?
[(R)-3-hydroxybutanoate]n + H2O
[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]
-
-
-
?
[(R)-3-hydroxybutanoate]n + H2O
[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]
-
-
-
?
[(R)-3-hydroxybutanoate]n + H2O
[(R)-3-hydroxybutanoate]n-x + [(R)-3-hydroxybutanoate]x
-
poly(3-hydroxybutyrate) depolymerase PhaZa1 is involved in mobilization of accumulated poly(3-hydroxybutyrate) in Ralstonia eutropha H16
-
-
?
[(R)-3-hydroxybutanoate]n + H2O
[(R)-3-hydroxybutanoate]n-x + [(R)-3-hydroxybutanoate]x
x is 1-5
-
-
?
[(R)-3-hydroxybutanoate]n + H2O
[(R)-3-hydroxybutanoate]n-x + [(R)-3-hydroxybutanoate]x
x is 1-5
-
-
?
[(R)-3-hydroxybutanoate]n + H2O
[(R)-3-hydroxybutanoate]n-x + [(R)-3-hydroxybutanoate]x
-
poly(3-hydroxybutyrate) depolymerase PhaZa1 is involved in mobilization of accumulated poly(3-hydroxybutyrate) in Ralstonia eutropha H16
-
-
?
additional information
?
-
-
no substrates: polycaprolactone, or polylactide
-
-
?
additional information
?
-
-
no substrates: polycaprolactone, or polylactide
-
-
?
additional information
?
-
-
inactive against p-nitrophenylpalmitate, tributyrin, and triolein
-
-
?
additional information
?
-
-
no substrates: p-nitrophenyl fatty acids or polycaprolactone
-
-
?
additional information
?
-
-
the enzyme is also active on poly(epsilon-caprolactone), cf. EC 3.1.1.76, but not on poly(butylene succinate) and poly(lactic acid)
-
-
?
additional information
?
-
-
the enzyme is also active on poly(epsilon-caprolactone), cf. EC 3.1.1.76, but not on poly(butylene succinate) and poly(lactic acid)
-
-
?
additional information
?
-
-
adsorption of single molecules of the PHB depolymerase onto poly[(R)-3-hydroxybutyric acid] single crystals and the degradation of the single crystals in a phosphate buffer solution at 37°C by real-time atomic force microscopy is observed
-
-
?
additional information
?
-
interaction between the substrate-binding domain (SBD) of P(3HB) depolymerase and various polymer substrates with different chemical structures, surface plasmon resonance (SPR) measurements
-
-
?
additional information
?
-
-
adsorption of single molecules of the PHB depolymerase onto poly[(R)-3-hydroxybutyric acid] single crystals and the degradation of the single crystals in a phosphate buffer solution at 37°C by real-time atomic force microscopy is observed
-
-
?
additional information
?
-
interaction between the substrate-binding domain (SBD) of P(3HB) depolymerase and various polymer substrates with different chemical structures, surface plasmon resonance (SPR) measurements
-
-
?
additional information
?
-
-
interaction between the substrate-binding domain (SBD) of P(3HB) depolymerase and various polymer substrates with different chemical structures, surface plasmon resonance (SPR) measurements
-
-
?
additional information
?
-
-
the enzyme is active with medium-chain-length polyhydroxyalkanoate with 6 to 14 carbon atoms, e.g. poly(epsilon-caprolactone), EC 3.1.1.76, as well as with short-chain-length polyhydroxyalkanoates with 3 to 5 carbon atoms, but not with poly(ethylene succinate) and poly(L-lactide), substrate specificity in vivo, overview
-
-
?
additional information
?
-
-
the enzyme is active with medium-chain-length polyhydroxyalkanoate with 6 to 14 carbon atoms, e.g. poly(epsilon-caprolactone), EC 3.1.1.76, as well as with short-chain-length polyhydroxyalkanoates with 3 to 5 carbon atoms, but not with poly(ethylene succinate) and poly(L-lactide), substrate specificity in vivo, overview
-
-
?
additional information
?
-
the enzyme is able to degrade polyhydroxybutyrate, but also shows ability to degrade films made of poly(3-hydroxybutyrate-co-3-hydroxyvalerate) copolymers and a blend of poly(3-hydroxybutyrate) and starch (7:3 proportion wt/wt)
-
-
?
additional information
?
-
-
the enzyme is able to degrade polyhydroxybutyrate, but also shows ability to degrade films made of poly(3-hydroxybutyrate-co-3-hydroxyvalerate) copolymers and a blend of poly(3-hydroxybutyrate) and starch (7:3 proportion wt/wt)
-
-
?
additional information
?
-
the enzyme is able to degrade polyhydroxybutyrate, but also shows ability to degrade films made of poly(3-hydroxybutyrate-co-3-hydroxyvalerate) copolymers and a blend of poly(3-hydroxybutyrate) and starch (7:3 proportion wt/wt)
-
-
?
additional information
?
-
-
the enzyme is active with medium-chain-length polyhydroxyalkanoate with 6 to 14 carbon atoms, EC 3.1.1.76, as well as with short-chain-length polyhydroxyalkanoates with 3 to 5 carbon atoms, but not with poly(ethylene succinate), poly(L-lactide), and poly(epsilon-caprolactone), substrate specificity in vivo, overview
-
-
?
additional information
?
-
-
the enzyme is active with medium-chain-length polyhydroxyalkanoate with 6 to 14 carbon atoms, EC 3.1.1.76, as well as with short-chain-length polyhydroxyalkanoates with 3 to 5 carbon atoms, but not with poly(ethylene succinate), poly(L-lactide), and poly(epsilon-caprolactone), substrate specificity in vivo, overview
-
-
?
additional information
?
-
-
the enzyme is active with medium-chain-length polyhydroxyalkanoate with 6 to 14 carbon atoms, e.g. poly(epsilon-caprolactone), EC 3.1.1.76, as well as with short-chain-length polyhydroxyalkanoates with 3 to 5 carbon atoms, but not with poly(ethylene succinate) and poly(L-lactide), substrate specificity in vivo, overview
-
-
?
additional information
?
-
-
the enzyme is active with medium-chain-length polyhydroxyalkanoate with 6 to 14 carbon atoms, e.g. poly(epsilon-caprolactone), EC 3.1.1.76, as well as with short-chain-length polyhydroxyalkanoates with 3 to 5 carbon atoms, but not with poly(ethylene succinate) and poly(L-lactide), substrate specificity in vivo, overview
-
-
?
additional information
?
-
-
the enzyme is active with medium-chain-length polyhydroxyalkanoate with 6 to 14 carbon atoms, e.g. poly(epsilon-caprolactone), EC 3.1.1.76, as well as with short-chain-length polyhydroxyalkanoates with 3 to 5 carbon atoms, but not with poly(ethylene succinate) and poly(L-lactide), substrate specificity in vivo, overview
-
-
?
additional information
?
-
-
the enzyme is active with medium-chain-length polyhydroxyalkanoate with 6 to 14 carbon atoms, e.g. poly(epsilon-caprolactone), EC 3.1.1.76, as well as with short-chain-length polyhydroxyalkanoates with 3 to 5 carbon atoms, but not with poly(ethylene succinate) and poly(L-lactide), substrate specificity in vivo, overview
-
-
?
additional information
?
-
-
the enzyme is active with medium-chain-length polyhydroxyalkanoate with 6 to 14 carbon atoms, e.g. poly(epsilon-caprolactone), EC 3.1.1.76, as well as with short-chain-length polyhydroxyalkanoates with 3 to 5 carbon atoms, but not with poly(ethylene succinate) and poly(L-lactide), substrate specificity in vivo, overview
-
-
?
additional information
?
-
-
the enzyme is active with medium-chain-length polyhydroxyalkanoate with 6 to 14 carbon atoms, e.g. poly(epsilon-caprolactone), EC 3.1.1.76, as well as with short-chain-length polyhydroxyalkanoates with 3 to 5 carbon atoms, but not with poly(ethylene succinate) and poly(L-lactide), substrate specificity in vivo, overview
-
-
?
additional information
?
-
-
the enzyme from actinobacteria is active with medium-chain-length polyhydroxyalkanoate with 6 to 14 carbon atoms, e.g. poly(epsilon-caprolactone), EC 3.1.1.76, as well as with short-chain-length polyhydroxyalkanoates with 3 to 5 carbon atoms like poly(3-hydroxybutyrate) and poly(3-hydroxypropionate), but not with poly(ethylene succinate) and poly(L-lactide), substrate specificity in vivo, overview
-
-
?
additional information
?
-
-
the enzyme from actinobacteria is active with medium-chain-length polyhydroxyalkanoate with 6 to 14 carbon atoms, e.g. poly(epsilon-caprolactone), EC 3.1.1.76, as well as with short-chain-length polyhydroxyalkanoates with 3 to 5 carbon atoms like poly(3-hydroxybutyrate) and poly(3-hydroxypropionate), but not with poly(ethylene succinate) and poly(L-lactide), substrate specificity in vivo, overview
-
-
?
additional information
?
-
-
the enzymes is adsorbed onto the surface of poly[(R)-3-hydroxybutyric acid] single crystals
-
-
?
additional information
?
-
-
purified enzyme is able to hydrolyze 4-nitrophenyl butyrate but not other artificial p-nitrophenyl fatty acid esters, such as p-nitrophenyl octanoate, p-nitrophenyl laurate, indicating preference of this enzyme for C4 substrates
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(3-hydroxy-phenylalkanoic acid)n + H2O
(3-hydroxy-phenylalkanoic acid)n-x + 3-hydroxy-phenylalkanoic acid
-
novel natural aromatic plastic with an even number of carbon atoms
-
?
poly((R)-3-hydroxybutyrate) + H2O
?
-
-
-
?
poly(3-hydroxybutyrate) + H2O
?
poly(3-hydroxybutyrate-co-3-hydroxyvalerate) + H2O
?
poly(3-hydroxypropionate) + H2O
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
[(R)-3-hydroxybutanoate]n + H2O
[(R)-3-hydroxybutanoate]n-x + [(R)-3-hydroxybutanoate]x
additional information
?
-
poly(3-hydroxybutyrate) + H2O
?
-
-
-
-
?
poly(3-hydroxybutyrate) + H2O
?
-
-
-
-
?
poly(3-hydroxybutyrate) + H2O
?
-
-
-
?
poly(3-hydroxybutyrate) + H2O
?
-
-
-
?
poly(3-hydroxybutyrate) + H2O
?
-
-
-
?
poly(3-hydroxybutyrate) + H2O
?
-
-
-
-
?
poly(3-hydroxybutyrate) + H2O
?
-
-
-
-
?
poly(3-hydroxybutyrate) + H2O
?
-
-
-
-
?
poly(3-hydroxybutyrate) + H2O
?
-
-
-
-
?
poly(3-hydroxybutyrate) + H2O
?
-
-
-
-
?
poly(3-hydroxybutyrate) + H2O
?
-
-
-
-
?
poly(3-hydroxybutyrate) + H2O
?
-
-
-
-
?
poly(3-hydroxybutyrate) + H2O
?
-
-
-
-
?
poly(3-hydroxybutyrate) + H2O
?
-
-
-
-
?
poly(3-hydroxybutyrate) + H2O
?
-
-
-
-
?
poly(3-hydroxybutyrate) + H2O
?
-
-
-
-
?
poly(3-hydroxybutyrate) + H2O
?
-
-
-
-
?
poly(3-hydroxybutyrate) + H2O
?
-
-
-
-
?
poly(3-hydroxybutyrate) + H2O
?
-
-
-
-
?
poly(3-hydroxybutyrate-co-3-hydroxyvalerate) + H2O
?
-
-
-
-
?
poly(3-hydroxybutyrate-co-3-hydroxyvalerate) + H2O
?
-
-
-
-
?
poly(3-hydroxybutyrate-co-3-hydroxyvalerate) + H2O
?
-
-
-
-
?
poly(3-hydroxybutyrate-co-3-hydroxyvalerate) + H2O
?
-
-
-
-
?
poly(3-hydroxybutyrate-co-3-hydroxyvalerate) + H2O
?
-
-
-
-
?
poly(3-hydroxybutyrate-co-3-hydroxyvalerate) + H2O
?
-
-
-
-
?
poly(3-hydroxybutyrate-co-3-hydroxyvalerate) + H2O
?
-
-
-
-
?
poly(3-hydroxybutyrate-co-3-hydroxyvalerate) + H2O
?
-
-
-
-
?
poly(3-hydroxybutyrate-co-3-hydroxyvalerate) + H2O
?
-
-
-
-
?
poly(3-hydroxybutyrate-co-3-hydroxyvalerate) + H2O
?
-
-
-
-
?
poly(3-hydroxybutyrate-co-3-hydroxyvalerate) + H2O
?
-
-
-
-
?
poly(3-hydroxybutyrate-co-3-hydroxyvalerate) + H2O
?
-
-
-
-
?
poly(3-hydroxybutyrate-co-3-hydroxyvalerate) + H2O
?
-
-
-
-
?
poly(3-hydroxybutyrate-co-3-hydroxyvalerate) + H2O
?
-
-
-
-
?
poly(3-hydroxypropionate) + H2O
?
-
-
-
-
?
poly(3-hydroxypropionate) + H2O
?
-
-
-
-
?
poly(3-hydroxypropionate) + H2O
?
-
-
-
-
?
poly(3-hydroxypropionate) + H2O
?
-
-
-
-
?
poly(3-hydroxypropionate) + H2O
?
-
-
-
-
?
poly(3-hydroxypropionate) + H2O
?
-
-
-
-
?
poly(3-hydroxypropionate) + H2O
?
-
-
-
-
?
poly(3-hydroxypropionate) + H2O
?
-
-
-
-
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
-
-
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
-
-
-
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
-
-
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
-
-
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
-
-
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
-
-
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
-
main products: dimer and trimer
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
consists of two domains of poly(3-hydroxybutyrate)-specific and poly(3-hydroxyvalerate)-specific binding
-
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
-
main products: dimer and trimer
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
consists of two domains of poly(3-hydroxybutyrate)-specific and poly(3-hydroxyvalerate)-specific binding
-
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
-
-
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
-
-
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
-
-
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
-
-
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
PhaZ can function as a PHB depolymerase in vivo
-
-
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
-
-
-
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
-
-
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
-
-
-
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
no hydrolysis of crystalline poly(3-hydroxybutyrate)
mainly oligomeric and some monomeric release of D(-)-3-hydroxybutyrate
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
specific for amorphous poly(3-hydroxybutyrate)
-
-
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
specific for amorphous poly(3-hydroxybutyrate) granules
-
-
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
-
-
-
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
no hydrolysis of crystalline poly(3-hydroxybutyrate)
mainly oligomeric and some monomeric release of D(-)-3-hydroxybutyrate
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
specific for amorphous poly(3-hydroxybutyrate) granules
-
-
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
-
-
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
-
main products: dimer and monomer
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
-
-
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
-
-
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
-
main products: dimer and monomer
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
-
-
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
-
-
-
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
highest activities for poly(3-hydroxybutyrate) depolymerases A and B, low activity for poly(3-hydroxyvaleric acid) depolymerase
-
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
highest activities for PhaZ1-5 proteins
-
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
specific for amorphous PHB
-
-
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
specific for amorphous poly(3-hydroxbutyrate)
-
-
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
specific for amorphous poly(3-hydroxybutyrate)
-
-
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
-
-
-
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
-
-
-
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
the addition of PHB to the medium leads to a sixfold increase in PhaZBm mRNA, while the presence of glucose represses phaZBm expression
-
-
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
the addition of PHB to the medium leads to a sixfold increase in PhaZBm mRNA, while the presence of glucose represses phaZBm expression
-
-
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
-
-
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
-
-
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
-
-
-
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
-
-
-
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
-
-
-
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
-
-
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
-
-
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
-
-
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
-
3-hydroxybutyrate as sole product detected
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
-
3-hydroxybutyrate as sole product detected
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
-
-
?
poly[(R)-3-hydroxybutanoate]n + H2O
poly[(R)-3-hydroxybutanoate]n-x + poly[(R)-3-hydroxybutanoate]x
-
-
-
-
?
[(R)-3-hydroxybutanoate]n + H2O
[(R)-3-hydroxybutanoate]n-x + [(R)-3-hydroxybutanoate]x
-
poly(3-hydroxybutyrate) depolymerase PhaZa1 is involved in mobilization of accumulated poly(3-hydroxybutyrate) in Ralstonia eutropha H16
-
-
?
[(R)-3-hydroxybutanoate]n + H2O
[(R)-3-hydroxybutanoate]n-x + [(R)-3-hydroxybutanoate]x
-
poly(3-hydroxybutyrate) depolymerase PhaZa1 is involved in mobilization of accumulated poly(3-hydroxybutyrate) in Ralstonia eutropha H16
-
-
?
additional information
?
-
-
the enzyme is active with medium-chain-length polyhydroxyalkanoate with 6 to 14 carbon atoms, e.g. poly(epsilon-caprolactone), EC 3.1.1.76, as well as with short-chain-length polyhydroxyalkanoates with 3 to 5 carbon atoms, but not with poly(ethylene succinate) and poly(L-lactide), substrate specificity in vivo, overview
-
-
?
additional information
?
-
-
the enzyme is active with medium-chain-length polyhydroxyalkanoate with 6 to 14 carbon atoms, e.g. poly(epsilon-caprolactone), EC 3.1.1.76, as well as with short-chain-length polyhydroxyalkanoates with 3 to 5 carbon atoms, but not with poly(ethylene succinate) and poly(L-lactide), substrate specificity in vivo, overview
-
-
?
additional information
?
-
-
the enzyme is active with medium-chain-length polyhydroxyalkanoate with 6 to 14 carbon atoms, EC 3.1.1.76, as well as with short-chain-length polyhydroxyalkanoates with 3 to 5 carbon atoms, but not with poly(ethylene succinate), poly(L-lactide), and poly(epsilon-caprolactone), substrate specificity in vivo, overview
-
-
?
additional information
?
-
-
the enzyme is active with medium-chain-length polyhydroxyalkanoate with 6 to 14 carbon atoms, EC 3.1.1.76, as well as with short-chain-length polyhydroxyalkanoates with 3 to 5 carbon atoms, but not with poly(ethylene succinate), poly(L-lactide), and poly(epsilon-caprolactone), substrate specificity in vivo, overview
-
-
?
additional information
?
-
-
the enzyme is active with medium-chain-length polyhydroxyalkanoate with 6 to 14 carbon atoms, e.g. poly(epsilon-caprolactone), EC 3.1.1.76, as well as with short-chain-length polyhydroxyalkanoates with 3 to 5 carbon atoms, but not with poly(ethylene succinate) and poly(L-lactide), substrate specificity in vivo, overview
-
-
?
additional information
?
-
-
the enzyme is active with medium-chain-length polyhydroxyalkanoate with 6 to 14 carbon atoms, e.g. poly(epsilon-caprolactone), EC 3.1.1.76, as well as with short-chain-length polyhydroxyalkanoates with 3 to 5 carbon atoms, but not with poly(ethylene succinate) and poly(L-lactide), substrate specificity in vivo, overview
-
-
?
additional information
?
-
-
the enzyme is active with medium-chain-length polyhydroxyalkanoate with 6 to 14 carbon atoms, e.g. poly(epsilon-caprolactone), EC 3.1.1.76, as well as with short-chain-length polyhydroxyalkanoates with 3 to 5 carbon atoms, but not with poly(ethylene succinate) and poly(L-lactide), substrate specificity in vivo, overview
-
-
?
additional information
?
-
-
the enzyme is active with medium-chain-length polyhydroxyalkanoate with 6 to 14 carbon atoms, e.g. poly(epsilon-caprolactone), EC 3.1.1.76, as well as with short-chain-length polyhydroxyalkanoates with 3 to 5 carbon atoms, but not with poly(ethylene succinate) and poly(L-lactide), substrate specificity in vivo, overview
-
-
?
additional information
?
-
-
the enzyme is active with medium-chain-length polyhydroxyalkanoate with 6 to 14 carbon atoms, e.g. poly(epsilon-caprolactone), EC 3.1.1.76, as well as with short-chain-length polyhydroxyalkanoates with 3 to 5 carbon atoms, but not with poly(ethylene succinate) and poly(L-lactide), substrate specificity in vivo, overview
-
-
?
additional information
?
-
-
the enzyme is active with medium-chain-length polyhydroxyalkanoate with 6 to 14 carbon atoms, e.g. poly(epsilon-caprolactone), EC 3.1.1.76, as well as with short-chain-length polyhydroxyalkanoates with 3 to 5 carbon atoms, but not with poly(ethylene succinate) and poly(L-lactide), substrate specificity in vivo, overview
-
-
?
additional information
?
-
-
the enzyme from actinobacteria is active with medium-chain-length polyhydroxyalkanoate with 6 to 14 carbon atoms, e.g. poly(epsilon-caprolactone), EC 3.1.1.76, as well as with short-chain-length polyhydroxyalkanoates with 3 to 5 carbon atoms like poly(3-hydroxybutyrate) and poly(3-hydroxypropionate), but not with poly(ethylene succinate) and poly(L-lactide), substrate specificity in vivo, overview
-
-
?
additional information
?
-
-
the enzyme from actinobacteria is active with medium-chain-length polyhydroxyalkanoate with 6 to 14 carbon atoms, e.g. poly(epsilon-caprolactone), EC 3.1.1.76, as well as with short-chain-length polyhydroxyalkanoates with 3 to 5 carbon atoms like poly(3-hydroxybutyrate) and poly(3-hydroxypropionate), but not with poly(ethylene succinate) and poly(L-lactide), substrate specificity in vivo, overview
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
1,2-epoxy-3-(p-nitrophenoxy)propane
-
complete inactivation at 100 mM, slow inactivation process
1-ethyl-3-(3-dimethylaminopropyl)carbodiimide/glycinamide
33% inhibition at 5 mM
2-Hydroxy-5-nitrobenzyl bromide
-
complete inactivation
3-hydroxybutyrate
-
cyclic trimers, reversible inhibition
acetone
82% inhibition at 10% (vol/vol)
acetonitrile
70% inhibition at 10% (vol/vol)
Aprotinin
-
10 mM, 26% inhibition
Ba(CH3COO)2
-
complete inhibition at 10 mM
Ba2+
-
5 mM, 32% loss of activity
CaCl2
-
at 10 mM 39% inhibition
citrate
-
depressed activity
diazo-DL-norleucine methyl ester
diethyldicarbonate
40% inhibition at 5 mM, 90% at 20 mM
diethylene glycol
71% inhibition at 10% (vol/vol)
diisopropyl fluorophosphate
diisopropylfluorophosphate
dithioerythritol
-
complete inhibition of P(3HV) depolymerase at 4 mM, reversible by dithionitrobenzene
DMF
84% inhibition at 10% (vol/vol)
DMSO
85% inhibition at 10% (vol/vol)
ethylene glycol
28% inhibition at 10% (vol/vol)
Fe3+
-
5 mM, 38% loss of activity
KCl
100 mM, 75% inhibition
mercaptoethanol
-
0.5%, 47% loss of activity
Mercuric chloride
-
complete inhibition at 10 mM
methanol
91% inhibition at 10% (vol/vol)
MgCl2
-
slight inhibition 1 mM, 57% inhibition at 10 mM
N-ethylmaleimide
-
1 mM, complete inhibition
NaN3
-
1 mM: 86%, 10 mM: 84% activity, compared to no addition
Ni2+
-
10 mM, 28% inhibition
p-(chloromercuri)benzoic acid
-
no inhibition below 1 mM
p-chloromercuribenzoic acid
-
complete inhibition at 0.1 mM
Pb2+
-
marked inhibition at 0.1 mM
phenylmethanesulfonyl fluoride
Phenylmethylsulfonylfluoride
10% inhibition at 1 mM and 70% inhibition at 10 mM
Plysurf A210G
-
100 mg/l, 48% inhibition
-
tetrahydrofuran
51% inhibition at 10% (vol/vol)
triethylene glycol
73% inhibition at 10% (vol/vol)
tyrosine
-
depressed activity
2-mercaptoethanol
-
-
2-mercaptoethanol
-
strong inhibition at 4 mM
2-mercaptoethanol
-
1% (v/v): 20% activity, compared to no addition
2-propanol
-
partial inhibition of P(3HV) depolymerase
2-propanol
71% inhibition at 10% (vol/vol)
Ag+
-
marked inhibition at 0.1 mM
Ag+
-
10 mM, 38% inhibition
Ca2+
activates up to 10 mM, inhibits above; activates up to 10 mM, inhibits above
Ca2+
-
5 mM, 44% loss of activity
Cu2+
-
1 mM, 41% inhibition
Cu2+
-
5 mM, complete loss of activity
Cu2+
-
1 mM, 30% residual activity
diazo-DL-norleucine methyl ester
-
very sensitive to
diazo-DL-norleucine methyl ester
-
97% inhibition at 25 mM
diazo-DL-norleucine methyl ester
-
complete inhibition at 25 mM, pseudo-first-order kinetic
diisopropyl fluorophosphate
-
-
diisopropyl fluorophosphate
-
90% inhibition at 10 mM
diisopropyl fluorophosphate
-
very sensitive to
diisopropyl fluorophosphate
-
complete inhibition at 500 nM
diisopropylfluorophosphate
-
at 10 microM 53% inhibition, at 100 microM total loss of activity
diisopropylfluorophosphate
-
almost complete inhibition at 1 mM
dithiothreitol
-
-
dithiothreitol
-
considerable inactivation
dithiothreitol
-
inactivation of the purified enzyme
dithiothreitol
-
at 0.1 mM 86% inhibition, complete inhibition at 1 mM
dithiothreitol
-
83% inhibition at 10 mM
dithiothreitol
-
rapid inactivation
dithiothreitol
-
1 mM, complete inhibition
dithiothreitol
-
complete inhibition at 5 mM
dithiothreitol
70% inhibition at 1 mM and 90% inhibition at 10 mM
dithiothreitol
-
strong inhibition at 4 mM
dithiothreitol
-
5 mM, complete inhibition
dithiothreitol
-
complete inhibition at 5 mM, reversible by H2O2
EDTA
activates alone, but inhibits in presence of divalent cations; activates alone, but inhibits in presence of divalent cations
EDTA
-
partial inhibition of P(3HV) depolymerase at concentrations higher than 5 mM
EDTA
-
0.5%, 83% loss of activity
EDTA
-
79% activity at 1 mM, 20% activity at 20 mM
EDTA
-
1 mM, 50% residual activity
EDTA
-
10 mM, 27% inhibition
EDTA
-
0.1 mM: 51%, 1 mM: 24%, 10 mM: 17% activity, compared to no addition
ethanol
-
partial inhibition of P(3HV) depolymerase
ethanol
82% inhibition at 10% (vol/vol)
Fe2+
-
88% inhibition at 5 mM
Fe2+
-
1 mM, 84% inhibition
Fe2+
-
56% inhibition at 1 mM, almost complete inhibition at 4 mM
Fe2+
-
5 mM, 50% loss of activity
Fe2+
-
1 mM less than 10% residual activity
Fe2+
-
1 mM, 90% residual activity
Fe2+
-
10 mM, 17% inhibition
Hg2+
-
marked inhibition at 0.1 mM
Hg2+
-
complete inhibition at 5 mM
Hg2+
-
1 mM, 82% inhibition
Hg2+
-
5 mM, 97% loss of activity
Hg2+
-
90% inhibition at 6 mM, completely reversible by 2-mercaptoethanol
K+
-
5 mM, 32% loss of activity
Mg2+
activates up to 10 mM, inhibits above; activates up to 10 mM, inhibits above
Mn2+
-
-
Mn2+
-
10 mM, 17% inhibition
N-bromosuccinimide
-
inactivation of the purified enzyme
N-bromosuccinimide
-
complete inactivation
Na+
-
5 mM, 10% loss of activity
NaCl
-
required for native enzyme, optimum activity at 0.5 M. Inhibitory for recombinant enzyme
NaCl
complete inactivation at 2.5 M
NaCl
-
complete inhibition at 3 M
NaCl
-
1 mM: 100%, 2 mM: 90%, 5 mM: 60%, 10 mM: 45% activity, compared to no addition
phenylmethanesulfonyl fluoride
-
considerable inactivation
phenylmethanesulfonyl fluoride
-
42% inhibition at 10 mM
PMSF
-
complete inactivation at 1 mM
PMSF
-
marked inhibition at 0.1 mM
PMSF
-
49% inhibition at 10 mM
PMSF
-
partial inhibition at 0.5 mM
PMSF
-
5 mM, complete inhibition
PMSF
complete inactivation at 1 mM
PMSF
-
10 mM, 72% inhibition
PMSF
-
1 mM: 24%, 10 mM: 10% activity, compared to no addition
SDS
-
at 0.01% (w/v) 28% inhibition, at 0.1% complete inhibition
SDS
almost complete inhibition at 0.01% v/v; almost complete inhibition at 0.01% v/v
SDS
-
10 mM, 86% inhibition
SDS
almost complete inhibition at 0.1%
SDS
-
almost complete inhibition at 0.1%
SDS
-
0.1%, complete inhibition
Triton X-100
-
-
Triton X-100
-
complete inhibition at at 0.1% (w/v)
Triton X-100
-
at 0.1% 57% inhibition, at 1% 64% inhibition
Triton X-100
almost complete inhibition at 0.01% v/v; almost complete inhibition at 0.01% v/v
Triton X-100
almost complete inhibition at 0.1%
Triton X-100
-
almost complete inhibition at 0.1%
Triton X-100
-
competitive inhibition, Ki: 0.014%
Triton X-100
-
0.1% (v/v): 115%, 1% (v/v): 70%, 10% (v/v): 56% activity, compared to no addition
Tween 20
-
considerable inactivation
Tween 20
-
nearly complete inhibition at 0.1%, v/v
Tween 20
amlnost complete inhibition at 0.1%
Tween 20
-
almost complete inhibition at 0.1%
Tween 20
-
0.1%, complete inhibition
Tween 20
-
0.1% (v/v): 100%, 1% (v/v): 64%, 10% (v/v): 25% activity, compared to no addition
Tween 80
-
-
Tween 80
-
almost complete inhibition at 0.1%
Tween 80
-
competitive inhibition, Ki: 0.56%
Tween 80
-
0.1% (v/v): 80%, 1% (v/v): 65%, 10% (v/v): 42% activity, compared to no addition
Zn2+
-
5 mM, 88% loss of activity
additional information
-
no inhibition by phenylmethylsulfonyl fluoride
-
additional information
activation of PhaZd2 depolymerase activity by salts, but salts affect the activity of PhaZd2 with nPHB granules as substrate but have no significant influence on the hydrolysis of p-nitrophenyl esters such as p-nitrophenyl butyrate. Poor effect by DTT; activation of PhaZd2 depolymerase activity by salts, but salts affect the activity of PhaZd2 with nPHB granules as substrate but have no significant influence on the hydrolysis of p-nitrophenyl esters such as p-nitrophenylbutyrate. Poor effect by DTT
-
additional information
activation of PhaZd2 depolymerase activity by salts, but salts affect the activity of PhaZd2 with nPHB granules as substrate but have no significant influence on the hydrolysis of p-nitrophenyl esters such as p-nitrophenyl butyrate. Poor effect by DTT; activation of PhaZd2 depolymerase activity by salts, but salts affect the activity of PhaZd2 with nPHB granules as substrate but have no significant influence on the hydrolysis of p-nitrophenyl esters such as p-nitrophenylbutyrate. Poor effect by DTT
-
additional information
-
activation of PhaZd2 depolymerase activity by salts, but salts affect the activity of PhaZd2 with nPHB granules as substrate but have no significant influence on the hydrolysis of p-nitrophenyl esters such as p-nitrophenyl butyrate. Poor effect by DTT; activation of PhaZd2 depolymerase activity by salts, but salts affect the activity of PhaZd2 with nPHB granules as substrate but have no significant influence on the hydrolysis of p-nitrophenyl esters such as p-nitrophenylbutyrate. Poor effect by DTT
-
additional information
-
no or poor inhibition by EDTA, Triton X-10, Tween-20, and urea; no or poor inhibition by Triton X-10, Tween-20, and urea
-
additional information
poor inhibition by glycerol. Increase of ionic strength gradually inhibits the poly(3-hydroxybutyrate) depolymerase activity leading to its complete inactivation at 2.5 M NaCl
-
additional information
-
poor inhibition by glycerol. Increase of ionic strength gradually inhibits the poly(3-hydroxybutyrate) depolymerase activity leading to its complete inactivation at 2.5 M NaCl
-
additional information
-
no inhibition of activity by azide
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.24 - 2.43
4-nitrophenyl acetate
0.16 - 1.25
4-nitrophenyl butyrate
0.05 - 0.45
4-nitrophenyl hexanoate
0.05 - 0.89
4-nitrophenyl pentanoate
0.27 - 2.7
4-nitrophenyl propionate
0.84
cyclic [(R)-3-hydroxybutanoate]3
-
cyclic 3-hydroxybutyrate oligomer
0.34 - 4.6
cyclic [(R)-3-hydroxybutanoate]5
0.79
p-nitrophenyl butyrate
-
0.67
poly(3-hydroxybutyrate-co-3-hydroxyvalerate)
-
pH 8.0, 30°C
4.1 - 9.7
[(R)-3-hydroxybutanoate]3
0.67 - 3.1
[(R)-3-hydroxybutanoate]4
0.56 - 1.3
[(R)-3-hydroxybutanoate]5
0.36
[(R)-3-hydroxybutanoate]6
-
cyclic 3-hydroxybutyrate oligomer
additional information
additional information
-
0.24
4-nitrophenyl acetate
recombinant mutant A66V/N285D/G310G, pH 7.0, 30°C
0.26
4-nitrophenyl acetate
recombinant mutant A66V, pH 7.0, 30°C
0.28
4-nitrophenyl acetate
recombinant mutant G108G/Q125L/R230R/K260M/T284S/G310G, pH 7.0, 30°C
0.41
4-nitrophenyl acetate
recombinant mutant A66V/N251S/T290A, pH 7.0, 30°C
0.56
4-nitrophenyl acetate
recombinant mutant S92S/G180D/I292F, pH 7.0, 30°C
0.56
4-nitrophenyl acetate
recombinant mutant T145S/S246T/T252T/S257T, pH 7.0, 30°C
0.66
4-nitrophenyl acetate
recombinant mutant T37A/N285D, pH 7.0, 30°C
0.67
4-nitrophenyl acetate
recombinant mutant T37A/N285Y, pH 7.0, 30°C
0.73
4-nitrophenyl acetate
recombinant wild-type enzyme, pH 7.0, 30°C
0.82
4-nitrophenyl acetate
recombinant mutant A66V/T145S/N285D, pH 7.0, 30°C
1.29
4-nitrophenyl acetate
recombinant mutant N285D, pH 7.0, 30°C
1.35
4-nitrophenyl acetate
recombinant mutant N285Y, pH 7.0, 30°C
1.96
4-nitrophenyl acetate
recombinant mutant S92S/T145S/N285Y, pH 7.0, 30°C
2.43
4-nitrophenyl acetate
recombinant mutant T252T/S257T/N285D, pH 7.0, 30°C
0.16
4-nitrophenyl butyrate
recombinant mutant S92S/G180D/I292F, pH 7.0, 30°C
0.16
4-nitrophenyl butyrate
recombinant mutant T145S/S246T/T252T/S257T, pH 7.0, 30°C
0.19
4-nitrophenyl butyrate
recombinant mutant G108G/Q125L/R230R/K260M/T284S/G310G, pH 7.0, 30°C
0.23
4-nitrophenyl butyrate
recombinant mutant A66V, pH 7.0, 30°C
0.23
4-nitrophenyl butyrate
recombinant mutant A66V/N251S/T290A, pH 7.0, 30°C
0.37
4-nitrophenyl butyrate
recombinant mutant A66V/N285D/G310G, pH 7.0, 30°C
0.46
4-nitrophenyl butyrate
recombinant mutant A66V/T145S/N285D, pH 7.0, 30°C
0.51
4-nitrophenyl butyrate
recombinant mutant T252T/S257T/N285D, pH 7.0, 30°C
0.56
4-nitrophenyl butyrate
recombinant wild-type enzyme, pH 7.0, 30°C
0.63
4-nitrophenyl butyrate
recombinant mutant N285D, pH 7.0, 30°C
0.63
4-nitrophenyl butyrate
recombinant mutant T37A/N285Y, pH 7.0, 30°C
0.67
4-nitrophenyl butyrate
recombinant mutant T37A/N285D, pH 7.0, 30°C
0.78
4-nitrophenyl butyrate
recombinant mutant N285Y, pH 7.0, 30°C
1.25
4-nitrophenyl butyrate
recombinant mutant S92S/T145S/N285Y, pH 7.0, 30°C
0.05
4-nitrophenyl hexanoate
recombinant mutant A66V/N251S/T290A, pH 7.0, 30°C
0.05
4-nitrophenyl hexanoate
recombinant mutant G108G/Q125L/R230R/K260M/T284S/G310G, pH 7.0, 30°C
0.06
4-nitrophenyl hexanoate
recombinant mutant A66V/T145S/N285D, pH 7.0, 30°C
0.06
4-nitrophenyl hexanoate
recombinant mutant S92S/G180D/I292F, pH 7.0, 30°C
0.06
4-nitrophenyl hexanoate
recombinant mutant T145S/S246T/T252T/S257T, pH 7.0, 30°C
0.07
4-nitrophenyl hexanoate
recombinant mutant A66V/N285D/G310G, pH 7.0, 30°C
0.09
4-nitrophenyl hexanoate
recombinant mutant A66V, pH 7.0, 30°C
0.1
4-nitrophenyl hexanoate
recombinant wild-type enzyme, pH 7.0, 30°C
0.29
4-nitrophenyl hexanoate
recombinant mutant T37A/N285Y, pH 7.0, 30°C
0.3
4-nitrophenyl hexanoate
recombinant mutant S92S/T145S/N285Y, pH 7.0, 30°C
0.32
4-nitrophenyl hexanoate
recombinant mutant N285Y, pH 7.0, 30°C
0.41
4-nitrophenyl hexanoate
recombinant mutant T252T/S257T/N285D, pH 7.0, 30°C
0.43
4-nitrophenyl hexanoate
recombinant mutant T37A/N285D, pH 7.0, 30°C
0.45
4-nitrophenyl hexanoate
recombinant mutant N285D, pH 7.0, 30°C
0.05
4-nitrophenyl pentanoate
recombinant mutant A66V/N251S/T290A, pH 7.0, 30°C
0.09
4-nitrophenyl pentanoate
recombinant mutant A66V, pH 7.0, 30°C
0.09
4-nitrophenyl pentanoate
recombinant mutant S92S/G180D/I292F, pH 7.0, 30°C
0.09
4-nitrophenyl pentanoate
recombinant mutant T145S/S246T/T252T/S257T, pH 7.0, 30°C
0.09
4-nitrophenyl pentanoate
recombinant wild-type enzyme, pH 7.0, 30°C
0.1
4-nitrophenyl pentanoate
recombinant mutant A66V/N285D/G310G, pH 7.0, 30°C
0.16
4-nitrophenyl pentanoate
recombinant mutant A66V/T145S/N285D, pH 7.0, 30°C
0.24
4-nitrophenyl pentanoate
recombinant mutant G108G/Q125L/R230R/K260M/T284S/G310G, pH 7.0, 30°C
0.46
4-nitrophenyl pentanoate
recombinant mutant T37A/N285Y, pH 7.0, 30°C
0.58
4-nitrophenyl pentanoate
recombinant mutant S92S/T145S/N285Y, pH 7.0, 30°C
0.59
4-nitrophenyl pentanoate
recombinant mutant N285Y, pH 7.0, 30°C
0.66
4-nitrophenyl pentanoate
recombinant mutant T37A/N285D, pH 7.0, 30°C
0.71
4-nitrophenyl pentanoate
recombinant mutant T252T/S257T/N285D, pH 7.0, 30°C
0.89
4-nitrophenyl pentanoate
recombinant mutant N285D, pH 7.0, 30°C
0.27
4-nitrophenyl propionate
recombinant wild-type enzyme, pH 7.0, 30°C
0.31
4-nitrophenyl propionate
recombinant mutant A66V/N251S/T290A, pH 7.0, 30°C
0.38
4-nitrophenyl propionate
recombinant mutant S92S/G180D/I292F, pH 7.0, 30°C
0.38
4-nitrophenyl propionate
recombinant mutant T145S/S246T/T252T/S257T, pH 7.0, 30°C
0.46
4-nitrophenyl propionate
recombinant mutant A66V, pH 7.0, 30°C
0.53
4-nitrophenyl propionate
recombinant mutant G108G/Q125L/R230R/K260M/T284S/G310G, pH 7.0, 30°C
0.54
4-nitrophenyl propionate
recombinant mutant T37A/N285Y, pH 7.0, 30°C
0.68
4-nitrophenyl propionate
recombinant mutant N285D, pH 7.0, 30°C
1.01
4-nitrophenyl propionate
recombinant mutant T252T/S257T/N285D, pH 7.0, 30°C
1.07
4-nitrophenyl propionate
recombinant mutant A66V/N285D/G310G, pH 7.0, 30°C
1.17
4-nitrophenyl propionate
recombinant mutant A66V/T145S/N285D, pH 7.0, 30°C
1.28
4-nitrophenyl propionate
recombinant mutant N285Y, pH 7.0, 30°C
1.29
4-nitrophenyl propionate
recombinant mutant T37A/N285D, pH 7.0, 30°C
2.7
4-nitrophenyl propionate
recombinant mutant S92S/T145S/N285Y, pH 7.0, 30°C
0.34
cyclic [(R)-3-hydroxybutanoate]5
-
cyclic 3-hydroxybutyrate oligomer
4.6
cyclic [(R)-3-hydroxybutanoate]5
-
cyclic 3-hydroxybutyrate oligomer
4.1
[(R)-3-hydroxybutanoate]3
-
linear 3-hydroxybutyrate oligomer
9.7
[(R)-3-hydroxybutanoate]3
-
linear 3-hydroxybutyrate oligomer
0.67
[(R)-3-hydroxybutanoate]4
-
linear 3-hydroxybutyrate oligomer
3.1
[(R)-3-hydroxybutanoate]4
-
linear 3-hydroxybutyrate oligomer
0.56
[(R)-3-hydroxybutanoate]5
-
linear 3-hydroxybutyrateoligomer
1.3
[(R)-3-hydroxybutanoate]5
-
linear 3-hydroxybutyrate oligomer
additional information
additional information
kinetics of wild-type and mutant enzymes, overview
-
additional information
additional information
-
apparent Km value of the purified enzyme for polyhydroxybutyrate is 53 microg/ml
-
additional information
additional information
-
for poly (3-hydroxybutyrate), 0.69 g/l
-
additional information
additional information
kinetics of random mutants, overview
-
additional information
poly(2-hydroxybutanoate)
-
Km value 1.04 microg/ml, pH 5.0, 50°C
-
additional information
poly(3-hydroxybutanoate)n
-
0.17 mg/ml
additional information
poly(3-hydroxybutanoate)n
-
0.27mg/ml, in 200 mM NaCl
additional information
poly(3-hydroxybutanoate)n
-
0.018 mg/ml, isoform E1, 0.07 mg/ml, isoform E2
additional information
poly(3-hydroxybutanoate)n
-
0.018 mg/ml
additional information
poly(3-hydroxybutanoate)n
-
0.06 mg/ml, P(3HB) depolymerase B, 0.1 mg/ml, P(3HB) depolymerase A
additional information
poly(3-hydroxybutanoate)n
-
values in mg/ml
additional information
poly(3-hydroxybutanoate)n
-
values in mg/ml
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
S102A
-
mutant without poly[(R)-3-hydroxybutanoate]n hydrolyzing activity
C178A
-
no degradation of amorphous poly(3-hydroxybutyrate) granules or 3-hydroxybutyrate oligomers
S190A
site-directed mutagenesis, inactive mutant
S193A
site-directed mutagenesis, inactive mutant
S190A
-
site-directed mutagenesis, inactive mutant
-
S193A
-
site-directed mutagenesis, inactive mutant
-
A134G
-
PHB depolymerase activity similar to wild type
A134G, H135L
-
PHB depolymerase activity similar to wild type, 2fold lipase activity compared to wild type
D242A
-
no PHB depolymerase activity
D242N
-
no PHB depolymerase activity
D256A
-
PHB depolymerase activity similar to wild type
D256N
-
PHB depolymerase activity similar to wild type
F198E
site-directed mutagenesis, the mutant shows similar activity compared to the wild-type enzyme
F251E
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
F9E
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
F9E/S136A
site-directed mutagenesis, inactive mutant
H306A
-
no PHB depolymerase activity
H47A
-
no PHB depolymerase activity
INPNC-PhaZ1
fusion protein
INPNC-PhaZ1-INPNC-PrePhaZ1 fusion construct
does not affect growth of host cells
INPNC-PrePhaZ1
fusion protein
PhaZ1-PrePhaZ1 fusion construct
construct containing PhaZ1 and its own N-terminal signal peptide (PrePhaZ1) enables the secretion of active PhaZ1 into the extracellular medium
PrePhaZ1
N-terminal signal peptide
S136A/?W202-V208
site-directed mutagenesis, inactive mutant
S136A/W207E
site-directed mutagenesis, inactive mutant
S136A/W252E
site-directed mutagenesis, inactive mutant
S136A/Y176E
site-directed mutagenesis, inactive mutant
S136A/Y189E
site-directed mutagenesis, inactive mutant
S136A/Y190E
site-directed mutagenesis, inactive mutant
S136T
-
20% PHB depolymerase activity
W202-V208
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
W207E
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
W252E
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Y103A
site-directed mutagenesis, the mutant shows similar activity compared to the wild-type enzyme
Y103E
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
Y105A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Y105E/S136A
site-directed mutagenesis, inactive mutant
Y105E/S136A/Y189E
site-directed mutagenesis, inactive mutant, no substrate binding
Y105E/S136A/Y190E
site-directed mutagenesis, inactive mutant, no substrate binding
Y105F
site-directed mutagenesis, the mutant shows similar activity compared to the wild-type enzyme
Y124E
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Y169E
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
Y172A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Y173S
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Y176E
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Y189A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Y190A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Y203S
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
Y204S
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Y66E
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Y66E/S136A
site-directed mutagenesis, inactive mutant
KTMQ01
-
phaZ knockout mutant, Pseudomonas putida KTMQ01
A66V
random mutagenesis, the mutant enzymes shows increased activity with 4-nitrophenyl butyrate as compared to the wild-type enzyme
A66V/N251S/T290A
random mutagenesis, the mutant enzymes shows altered activity with 4-nitrophenyl butyrate as compared to the wild-type enzyme
A66V/N285D/G310G
random mutagenesis, the mutant enzymes shows altered activity with 4-nitrophenyl butyrate as compared to the wild-type enzyme
A66V/T145S/N285D
random mutagenesis, the mutant enzymes shows altered activity with 4-nitrophenyl butyrate as compared to the wild-type enzyme
G108G/Q125L/R230R/K260M/T284S/G310G
random mutagenesis, the mutant enzymes shows altered activity with 4-nitrophenyl butyrate as compared to the wild-type enzyme
N285A
site-directed mutagenesis, mutation at position 285 in the C-terminal domain increases the hydrolytic activity for 4-nitrophenyl esters with carbon chain lengths of C2-C6
N285D/G310G
random mutagenesis, the mutant enzymes shows altered activity with 4-nitrophenyl butyrate as compared to the wild-type enzyme
N285E
site-directed mutagenesis, mutation at position 285 in the C-terminal domain increases the hydrolytic activity for 4-nitrophenyl esters with carbon chain lengths of C2-C6
N285G
site-directed mutagenesis, mutation at position 285 in the C-terminal domain increases the hydrolytic activity for 4-nitrophenyl esters with carbon chain lengths of C2-C6
N285H
site-directed mutagenesis, mutation at position 285 in the C-terminal domain increases the hydrolytic activity for 4-nitrophenyl esters with carbon chain lengths of C2-C6
S445C
-
CD spectra and hydrolytic activities for water-soluble substrates is found to be identical to those of wild-type enzyme, indicating that the mutations has no influence on their structures and their ability to cleave the ester bond. S445C has higher poly((R)-3-hydroxybutyrate)-degrading activity than wild-type. Surface plasmon resonance (SPR) analysis reveal that the mutation alters the association phase rather than the dissociation phase in the enzyme adsorption to the polymer surface
S92S/G180D/I292F
random mutagenesis, the mutant enzymes shows altered activity with 4-nitrophenyl butyrate as compared to the wild-type enzyme
S92S/T145S/N285Y
random mutagenesis, the mutant enzymes shows altered activity with 4-nitrophenyl butyrate as compared to the wild-type enzyme
T145S/S246T/T252T/S257T
random mutagenesis, the mutant enzymes shows altered activity with 4-nitrophenyl butyrate as compared to the wild-type enzyme
T252T/S257T/N285D
random mutagenesis, the mutant enzymes shows altered activity with 4-nitrophenyl butyrate as compared to the wild-type enzyme
T37A/C51C/N285Y
random mutagenesis, the mutant enzymes shows altered activity with 4-nitrophenyl butyrate as compared to the wild-type enzyme
T37A/N285D
random mutagenesis, the mutant enzymes shows altered activity with 4-nitrophenyl butyrate as compared to the wild-type enzyme
Y443H
-
CD spectra and hydrolytic activities for water-soluble substrates is found to be identical to those of wild-type enzyme, indicating that the mutations has no influence on their structures and their ability to cleave the ester bond. L441H and Y443H enzymes have lower poly((R)-3-hydroxybutyrate)-degrading activity than their wild-type counterpart. Surface plasmon resonance (SPR) analysis reveal that the mutation alters the association phase rather than the dissociation phase in the enzyme adsorption to the polymer surface
A66V
-
random mutagenesis, the mutant enzymes shows increased activity with 4-nitrophenyl butyrate as compared to the wild-type enzyme
-
L441H
-
mutant enzyme with lower degradation of denatured poly(R)-3-hydroxybutyrate and adsorption abilities. Lowering the affinity of the substrate-binding domain towards denatured poly(R)-3-hydroxybutyrate causes a decrease in the degradation rate without the loss of its hydrolytic activity for the polymer chain
-
N285A
-
site-directed mutagenesis, mutation at position 285 in the C-terminal domain increases the hydrolytic activity for 4-nitrophenyl esters with carbon chain lengths of C2-C6
-
N285D/G310G
-
random mutagenesis, the mutant enzymes shows altered activity with 4-nitrophenyl butyrate as compared to the wild-type enzyme
-
N285G
-
site-directed mutagenesis, mutation at position 285 in the C-terminal domain increases the hydrolytic activity for 4-nitrophenyl esters with carbon chain lengths of C2-C6
-
N285Y
-
site-directed mutagenesis, mutation at position 285 in the C-terminal domain increases the hydrolytic activity for 4-nitrophenyl esters with carbon chain lengths of C2-C6
-
T37A/C51C/N285Y
-
random mutagenesis, the mutant enzymes shows altered activity with 4-nitrophenyl butyrate as compared to the wild-type enzyme
-
D209N
site-directed mutagenesis, inactive mutant
H269E
site-directed mutagenesis, inactive mutant
H269Q
site-directed mutagenesis, inactive mutant
S131A
site-directed mutagenesis, inactive mutant
S131C
site-directed mutagenesis, inactive mutant
D209N
-
site-directed mutagenesis, inactive mutant
-
H269E
-
site-directed mutagenesis, inactive mutant
-
H269Q
-
site-directed mutagenesis, inactive mutant
-
S131A
-
site-directed mutagenesis, inactive mutant
-
S131C
-
site-directed mutagenesis, inactive mutant
-
S39A
-
inactive mutant, pdb accession code 2D81
S136A
-
no PHB depolymerase activity
S136A
site-directed mutagenesis, active site mutation, inactive mutant
Y105E
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
Y105E
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Y105E
mutant displays reduced binding to olyhydroxybutanoate
Y105E/Y189E
site-directed mutagenesis
Y105E/Y189E
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Y105E/Y190E
site-directed mutagenesis
Y105E/Y190E
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Y189E
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
Y189E
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Y190E
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
Y190E
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
L441H
mutant enzyme with lower degradation of denatured poly(R)-3-hydroxybutyrate and adsorption abilities. Lowering the affinity of the substrate-binding domain towards denatured poly(R)-3-hydroxybutyrate causes a decrease in the degradation rate without the loss of its hydrolytic activity for the polymer chain
L441H
-
CD spectra and hydrolytic activities for water-soluble substrates is found to be identical to those of wild-type enzyme, indicating that the mutations has no influence on their structures and their ability to cleave the ester bond. L441H and Y443H enzymes have lower poly((R)-3-hydroxybutyrate)-degrading activity than their wild-type counterpart. Surface plasmon resonance (SPR) analysis reveal that the mutation alters the association phase rather than the dissociation phase in the enzyme adsorption to the polymer surface
N285D
site-directed mutagenesis, mutation at position 285 in the C-terminal domain increases the hydrolytic activity for 4-nitrophenyl esters with carbon chain lengths of C2-C6
N285D
site-directed mutagenesis, the mutant enzymes shows increased activity with 4-nitrophenyl butyrate as compared to the wild-type enzyme
N285Y
random mutagenesis, the mutant enzymes shows increased activity with 4-nitrophenyl butyrate as compared to the wild-type enzyme
N285Y
site-directed mutagenesis, mutation at position 285 in the C-terminal domain increases the hydrolytic activity for 4-nitrophenyl esters with carbon chain lengths of C2-C6
N285D
-
site-directed mutagenesis, mutation at position 285 in the C-terminal domain increases the hydrolytic activity for 4-nitrophenyl esters with carbon chain lengths of C2-C6
-
N285D
-
site-directed mutagenesis, the mutant enzymes shows increased activity with 4-nitrophenyl butyrate as compared to the wild-type enzyme
-
additional information
-
construction of GST-catalytic domain fusionproteins, strong adsorption to polyester granules of poly(3-hydroxybutyrate), poly(3-hydroxypropionate) and poly(2-hydroxypropionate)
additional information
construction of a single knockout mutant or double and quadruple knockout mutants
additional information
construction of a single knockout mutant or double and quadruple knockout mutants
additional information
construction of a single knockout mutant or double and quadruple knockout mutants
additional information
construction of a single knockout mutant or double and quadruple knockout mutants
additional information
construction of a single knockout mutant or double and quadruple knockout mutants
additional information
construction of a single knockout mutant or double and quadruple knockout mutants
additional information
construction of a single knockout mutant or double and quadruple knockout mutants
additional information
-
construction of a single knockout mutant or double and quadruple knockout mutants
additional information
construction of a single knockout mutant or double and quadruple knockout mutants, complementation analysis of Ralstonia eutropha strain Re2005 (DELTAphaZ1DELTAphaZ2DELTAphaZ3DELTAphaZ5) cells
additional information
construction of a single knockout mutant or double and quadruple knockout mutants, complementation analysis of Ralstonia eutropha strain Re2005 (DELTAphaZ1DELTAphaZ2DELTAphaZ3DELTAphaZ5) cells
additional information
construction of a single knockout mutant or double and quadruple knockout mutants, complementation analysis of Ralstonia eutropha strain Re2005 (DELTAphaZ1DELTAphaZ2DELTAphaZ3DELTAphaZ5) cells
additional information
construction of a single knockout mutant or double and quadruple knockout mutants, complementation analysis of Ralstonia eutropha strain Re2005 (DELTAphaZ1DELTAphaZ2DELTAphaZ3DELTAphaZ5) cells
additional information
construction of a single knockout mutant or double and quadruple knockout mutants, complementation analysis of Ralstonia eutropha strain Re2005 (DELTAphaZ1DELTAphaZ2DELTAphaZ3DELTAphaZ5) cells
additional information
construction of a single knockout mutant or double and quadruple knockout mutants, complementation analysis of Ralstonia eutropha strain Re2005 (DELTAphaZ1DELTAphaZ2DELTAphaZ3DELTAphaZ5) cells
additional information
construction of a single knockout mutant or double and quadruple knockout mutants, complementation analysis of Ralstonia eutropha strain Re2005 (DELTAphaZ1DELTAphaZ2DELTAphaZ3DELTAphaZ5) cells
additional information
-
construction of a single knockout mutant or double and quadruple knockout mutants, complementation analysis of Ralstonia eutropha strain Re2005 (DELTAphaZ1DELTAphaZ2DELTAphaZ3DELTAphaZ5) cells
additional information
construction of a single knockout mutant or double and quadruple knockout mutants, for deletion of the phaZ3 gene, Ralstonia eutropha strains H16 and Re1111 are used as parental strains, complementation analysis of Ralstonia eutropha strain Re2005 (DELTAphaZ1DELTAphaZ2DELTAphaZ3DELTAphaZ5) cells
additional information
construction of a single knockout mutant or double and quadruple knockout mutants, for deletion of the phaZ3 gene, Ralstonia eutropha strains H16 and Re1111 are used as parental strains, complementation analysis of Ralstonia eutropha strain Re2005 (DELTAphaZ1DELTAphaZ2DELTAphaZ3DELTAphaZ5) cells
additional information
construction of a single knockout mutant or double and quadruple knockout mutants, for deletion of the phaZ3 gene, Ralstonia eutropha strains H16 and Re1111 are used as parental strains, complementation analysis of Ralstonia eutropha strain Re2005 (DELTAphaZ1DELTAphaZ2DELTAphaZ3DELTAphaZ5) cells
additional information
construction of a single knockout mutant or double and quadruple knockout mutants, for deletion of the phaZ3 gene, Ralstonia eutropha strains H16 and Re1111 are used as parental strains, complementation analysis of Ralstonia eutropha strain Re2005 (DELTAphaZ1DELTAphaZ2DELTAphaZ3DELTAphaZ5) cells
additional information
construction of a single knockout mutant or double and quadruple knockout mutants, for deletion of the phaZ3 gene, Ralstonia eutropha strains H16 and Re1111 are used as parental strains, complementation analysis of Ralstonia eutropha strain Re2005 (DELTAphaZ1DELTAphaZ2DELTAphaZ3DELTAphaZ5) cells
additional information
construction of a single knockout mutant or double and quadruple knockout mutants, for deletion of the phaZ3 gene, Ralstonia eutropha strains H16 and Re1111 are used as parental strains, complementation analysis of Ralstonia eutropha strain Re2005 (DELTAphaZ1DELTAphaZ2DELTAphaZ3DELTAphaZ5) cells
additional information
construction of a single knockout mutant or double and quadruple knockout mutants, for deletion of the phaZ3 gene, Ralstonia eutropha strains H16 and Re1111 are used as parental strains, complementation analysis of Ralstonia eutropha strain Re2005 (DELTAphaZ1DELTAphaZ2DELTAphaZ3DELTAphaZ5) cells
additional information
-
construction of a single knockout mutant or double and quadruple knockout mutants, for deletion of the phaZ3 gene, Ralstonia eutropha strains H16 and Re1111 are used as parental strains, complementation analysis of Ralstonia eutropha strain Re2005 (DELTAphaZ1DELTAphaZ2DELTAphaZ3DELTAphaZ5) cells
additional information
deletion of phaZd1 without effect on enzyme activity
additional information
deletion of phaZd1 without effect on enzyme activity
additional information
-
deletion of phaZd1 without effect on enzyme activity
additional information
deletion of phaZd2 without effect on enzyme activity
additional information
deletion of phaZd2 without effect on enzyme activity
additional information
-
deletion of phaZd2 without effect on enzyme activity
additional information
generation of a set of phaZ gene deletion strains, i.e. DELTAphaZ1, DELTAphaZ2, DELTAphaZ3, DELTAphaZ1DELTAphaZ2, DELTAphaZ1DELTAphaZ3, DELTAphaZ2DELTAphaZ3, and DELTAphaZ1DELTAphaZ2DELTAphaZ3 from strain H16. All mutant strains are unable to produce poly(hydroxybutyrate)
additional information
-
generation of a set of phaZ gene deletion strains, i.e. DELTAphaZ1, DELTAphaZ2, DELTAphaZ3, DELTAphaZ1DELTAphaZ2, DELTAphaZ1DELTAphaZ3, DELTAphaZ2DELTAphaZ3, and DELTAphaZ1DELTAphaZ2DELTAphaZ3 from strain H16. All mutant strains are unable to produce poly(hydroxybutyrate)
additional information
recombinant Cupriavidus necator strain KNK-005 harbors an NSDG mutant of the PHA synthase gene (phaCAc) from Aeromonas caviae. Deletion of phaZ1 and phaZ2 (EC 3.1.1.22, UniProt ID Q0K7T2) has a significant and slight attenuating effect, respectively, on the reduction in polyhydroxyalkanoate (PHA) content of KNK-005 cells. Regardless of the PHA consumption, its molecular weight does not decrease. The DELTAphaZ1DELTAphaZ2DELTAphaZ6 triple mutant of KNK-005, 005dZ126, is a promising strain capable of producing ultra-high-molecular-weight poly(3-hydroxybutyrate-co-3-hydroxyhexanoate) (PHBHHx) of ultra-high-molecular-weight and barely degrades PHBHHx and polyhydroxyalkanoate enzymatically intracellularly
additional information
-
recombinant Cupriavidus necator strain KNK-005 harbors an NSDG mutant of the PHA synthase gene (phaCAc) from Aeromonas caviae. Deletion of phaZ1 and phaZ2 (EC 3.1.1.22, UniProt ID Q0K7T2) has a significant and slight attenuating effect, respectively, on the reduction in polyhydroxyalkanoate (PHA) content of KNK-005 cells. Regardless of the PHA consumption, its molecular weight does not decrease. The DELTAphaZ1DELTAphaZ2DELTAphaZ6 triple mutant of KNK-005, 005dZ126, is a promising strain capable of producing ultra-high-molecular-weight poly(3-hydroxybutyrate-co-3-hydroxyhexanoate) (PHBHHx) of ultra-high-molecular-weight and barely degrades PHBHHx and polyhydroxyalkanoate enzymatically intracellularly
additional information
-
deletion of phaZd2 without effect on enzyme activity
-
additional information
-
construction of a single knockout mutant or double and quadruple knockout mutants
-
additional information
-
deletion of phaZd1 without effect on enzyme activity
-
additional information
-
construction of a single knockout mutant or double and quadruple knockout mutants, complementation analysis of Ralstonia eutropha strain Re2005 (DELTAphaZ1DELTAphaZ2DELTAphaZ3DELTAphaZ5) cells
-
additional information
-
construction of a single knockout mutant or double and quadruple knockout mutants, for deletion of the phaZ3 gene, Ralstonia eutropha strains H16 and Re1111 are used as parental strains, complementation analysis of Ralstonia eutropha strain Re2005 (DELTAphaZ1DELTAphaZ2DELTAphaZ3DELTAphaZ5) cells
-
additional information
-
GST-catalytic domain fusion protein, high binding capacity on single crystals of poly(3-hydroxybutyrate)
additional information
-
construction of GST-catalytic domain fusionproteins, strong adsorption to polyester granules of poly(3-hydroxybutyrate), poly(3-hydroxypropionate) and poly(2-hydroxypropionate)
additional information
-
C-terminal truncation, poly(3-hydroxybutyrate)-specific binding domain within the C-terminus
additional information
construction of a PhaZ7 variant with deletion of residues 202-208. Exchange of surface-exposed amino acids, Y105, Y176, Y189, Y189, W207, that constitute the substrate binding site of the enzyme, by less hydrophobic, hydrophilic or negatively charged residues reduces binding of the enzyme to substrate poly(3-hydroxybutyrate). Modifications of other residues at the enzyme surface, i.e. F9, Y66, Y103, Y124, Y169, Y172, Y173, F198, Y203, Y204, F251, and W252, have no effect on substrate binding
additional information
-
construction of a PhaZ7 variant with deletion of residues 202-208. Exchange of surface-exposed amino acids, Y105, Y176, Y189, Y189, W207, that constitute the substrate binding site of the enzyme, by less hydrophobic, hydrophilic or negatively charged residues reduces binding of the enzyme to substrate poly(3-hydroxybutyrate). Modifications of other residues at the enzyme surface, i.e. F9, Y66, Y103, Y124, Y169, Y172, Y173, F198, Y203, Y204, F251, and W252, have no effect on substrate binding
additional information
-
construction of several GST-fusion domains, analysis of substrate-binding domains
additional information
-
construction of GST-catalytic domain fusionproteins, strong adsorption to polyester granules of poly(3-hydroxybutyrate), poly(3-hydroxypropionate) and poly(2-hydroxypropionate)
additional information
N17-mutant unable to degrade poly(3-hydroxybutyrate), obtained with the random insertion of a minitransposon, Tn5. Mutant accumulates the poly(3-hydroxybutyrate) depolymerase in the periplasm and cytoplasm, and does not secrete the enzyme into the external medium
additional information
mutated phaZRpiT1 genes generated by error-prone PCR are fused to the oprI gene from Pseudomonas aeruginosa to display them as anchored fusion proteins on Escherichia coli cell surface, screening for activity with 4-nitrophenyl butyrate. The wholecell catalysis is a promising and suitable tool to screen for PHB depolymerases with enhanced catalytic activity
additional information
the poly((R)-3-hydroxybutyrate)-degrading activities of N285X are reciprocally related to their pNPCn-hydrolyzing activities, with the exception of N285A and N285G, and that His residue could functionally substitute for Asn285 on poly((R)-3-hydroxybutyrate) degradation. Among the mutant enzymes, N285E displays the highest hydrolysis rate regardless of substrate concentration or carbon chain length. N285A has comparable hydrolysis rates to N285E at low substrate concentrations (0.1-0.4 mM) for all the substrates regardless of carbon chain lengths. N285H shows one of the lowest hydrolysis rates among the mutant enzymes regardless of substrate concentration or carbon chain length
additional information
-
the poly((R)-3-hydroxybutyrate)-degrading activities of N285X are reciprocally related to their pNPCn-hydrolyzing activities, with the exception of N285A and N285G, and that His residue could functionally substitute for Asn285 on poly((R)-3-hydroxybutyrate) degradation. Among the mutant enzymes, N285E displays the highest hydrolysis rate regardless of substrate concentration or carbon chain length. N285A has comparable hydrolysis rates to N285E at low substrate concentrations (0.1-0.4 mM) for all the substrates regardless of carbon chain lengths. N285H shows one of the lowest hydrolysis rates among the mutant enzymes regardless of substrate concentration or carbon chain length
-
additional information
-
N17-mutant unable to degrade poly(3-hydroxybutyrate), obtained with the random insertion of a minitransposon, Tn5. Mutant accumulates the poly(3-hydroxybutyrate) depolymerase in the periplasm and cytoplasm, and does not secrete the enzyme into the external medium
-
additional information
-
mutated phaZRpiT1 genes generated by error-prone PCR are fused to the oprI gene from Pseudomonas aeruginosa to display them as anchored fusion proteins on Escherichia coli cell surface, screening for activity with 4-nitrophenyl butyrate. The wholecell catalysis is a promising and suitable tool to screen for PHB depolymerases with enhanced catalytic activity
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Asano, Y.; Watanabe, S.
Isolation of poly(3-hydroxybutyrate) (PHB)-degrading microorganisms and characterization of PHB-depolymerase from Arthrobacter sp. strain W6
Biosci. Biotechnol. Biochem.
65
1191-1194
2001
Arthrobacter sp., Pseudomonas alcaligenes
brenda
Schber, U.; Thiel, C.; Jendrossek, D.
Poly(3-hyddoxyvalerate) depolymerase of Pseudomonas lemoignei
Appl. Environ. Microbiol.
66
1385-1392
2000
Paucimonas lemoignei
brenda
Ohura, T.; Kasuya, K.I.; Doi, Y.
Cloning and characterization of the polyhydroxybutyrate depolymerase gene of Pseudomonas stutzeri and analysis of the function of substrate-binding domains
Appl. Environ. Microbiol.
65
189-197
1999
Pseudomonas stutzeri
brenda
Kasuya, K.; Ohura, T.; Masuda, K.; Doi, Y.
Substrate and binding specificities of bacterial polyhydroxybutyrate depolymerases
Int. J. Biol. Macromol.
24
329-336
1999
Alcaligenes faecalis, Delftia acidovorans, Pseudomonas stutzeri
brenda
Kasuya, K.; Inoue, Y.; Tanaka, T.; Akehata, T.; Iwata, T.; Fukui, T.; Doi, Y.
Biochemical and molecular characterization of the polyhydroxybutyrate depolymerase of Comamonas acidovorans YM1609, isolated from freshwater
Appl. Environ. Microbiol.
63
4844-4852
1997
Delftia acidovorans
brenda
Jendrossek, D.; Backhaus, M.; Andermann, M.
Characterization of the extracellular poly(3-hydroxybutyrate) depolymerase of Comamonas sp. and of its structural gene
Can. J. Microbiol.
41
160-169
1995
Comamonas sp.
brenda
Kita, K.; Ishimaru, K.; Teraoka, M.; Yanase, H.; Kato, N.
Properties of poly(3-hydroxybutyrate) depolymerase from a marine bacterium, Alcaligenes faecalis AE122
Appl. Environ. Microbiol.
61
1727-1730
1995
Alcaligenes faecalis, Alcaligenes faecalis AE122
brenda
Muller, B.; Jendrossek, D.
Purification and properties of poly(3-hydroxyvaleric acid) depolymerase from Pseudomonas lemoignei
Appl. Microbiol. Biotechnol.
37-8
487-492
1993
Paucimonas lemoignei
-
brenda
Brucato, C.L.; Wong, S.S.
Extracellular poly(3-hydroxybutyrate) depolymerase from Penicillium funiculosum: General characteristics and active site studies
Arch. Biochem. Biophys.
290
497-502
1991
Talaromyces funiculosus
brenda
Kita, K.; Mashiba, S.; Nagita, M.; Ishimaru, K.; Okamoto, K.; Yanase, H.; Kato, N.
Cloning of poly(3-hydroxybutyrate) depolymerase from a marine bacterium, Alcaligenes faecalis AE122, and characterization of its gene product
Biochim. Biophys. Acta
1352
113-122
1997
Alcaligenes faecalis, Alcaligenes faecalis AE122
brenda
Behrends, A.; Klingbeil, B.; Jendrossek, D.
Poly(3-hydroxybutyrate) depolymerases bind to their substrate by a C-terminal located substrate binding site
FEMS Microbiol. Lett.
143
191-194
1996
Paucimonas lemoignei
brenda
Klingbeil, B.; Kroppenstedt, R.M.; Jendrossek, D.
Taxonomic identification of Streptomyces exfoliatus K10 and characterization of its poly(3-hydroxybutyrate) depolymerase gene
FEMS Microbiol. Lett.
142
215-221
1996
Streptomyces exfoliatus, Streptomyces exfoliatus K10
brenda
Saegusa, H.; Shiraki, M.; Kanai, C.; Saito, T.
Cloning of an intracellular poly[D(-)-3-hydroxybutyrate] depolymerase gene from Ralstonia eutropha H16 and characterization of the gene product
J. Bacteriol.
183
94-100
2001
Cupriavidus necator, Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
brenda
Takeda, M.; Koizumi, J.I.; Yabe, K.; Adachi, K.
Thermostable poly(3-hydroxybutyrate) depolymerase of a thermophilic strain of Leptothrix sp. isolated from a hot spring
J. Ferment. Bioeng.
85
375-380
1998
Leptothrix sp. (in: Bacteria), Leptothrix sp. (in: Bacteria) HS
-
brenda
Scherer.T.M.; Fuller, R.C.; Lenz, R.W.; Goodwin, S.
Production, purification and activity of an extracellular depolymerase from Aspergillus fumigatus
J. Environ. Polym. Degrad.
7
117-125
1999
Aspergillus fumigatus
-
brenda
Sadacco, P.; Nocerino, S.; Dubini-Paglia, E.; Seves, A.; Elegir, G.
Characterization of a poly(3-hydroxybutyrate) depolymerase from Aureobacterium saperdae: Acive site and kinetics of hydrolysis studies
J. Environ. Polym. Degrad.
5
57-65
1997
Microbacterium saperdae
-
brenda
Nojima, S.; Mineki, S.; Iida, M.
Purification and characterization of extracellular poly(3-hydroxybutyrate) depolymerases produced by Agrobacterium sp. K-03
J. Ferment. Bioeng.
81
72-75
1996
Agrobacterium sp., Agrobacterium sp. K-03
-
brenda
Kobayashi, T.; Sugiyama, A.; Kawase, Y.; Saito, T.; Mergaert, J.; Swings, J.
Biochemical and genetic characterization of an extracellular poly(3-hydroxybutyrate) depolymerase from Acidovorax sp. strain TP4
J. Environ. Polym. Degrad.
7
9-18
1999
Acidovorax sp., Sphingomonas paucimobilis, Acidovorax sp. TP4
-
brenda
Kim, T.W.; Park, J.S.; Lee, Y.H.
Enzymatic characteristics of biosynthesis and degradation of poly(beta-hydroxybutyrate) of Alcaligenes latus
J. Microbiol. Biotechnol.
6
425-431
1996
Azohydromonas lata
-
brenda
Garcia, B.; Olivera, E.R.; Minambres, B.; Fernandez-Valverde, M.; Canedo, L.M.; Prieto, M.A.; Garcia, J.L.; Martinez, M.; Luengo, J.M.
Novel biodegradable aromatic plastics from a bacterial source. Genetic and biochemical studies on a route of the phenylacetyl-CoA catabolon
J. Biol. Chem.
274
29228-29241
1999
Pseudomonas putida U
brenda
Kapetaniou, E.G.; Braaz, R.; Jendrossek, D.; Papageorgiou, A.C.
Crystallization and preliminary x-ray analysis of a novel thermoalkalophilic poly(3-hydroxybutyrate) depolymerase (PhaZ7) from Paucimonas lemoignei
Acta Crystallogr. Sect. F
F61
479-481
2005
Paucimonas lemoignei
brenda
Kadouri, D.; Jurkevitch, E.; Okon, Y.
Poly b-hydroxybutyrate depolymerase (PhaZ) in Azospirillum brasilense and characterization of a phaZ mutant
Arch. Microbiol.
180
309-318
2003
Azospirillum brasilense (Q71KW6), Azospirillum brasilense
brenda
Romen, F.; Reinhardt, S.; Jendrossek, D.
Thermotolerant poly(3-hydroxybutyrate)-degrading bacteria from hot compost and characterization of the PHB depolymerase of Schlegelella sp. KB1a
Arch. Microbiol.
182
157-164
2004
Schlegelella sp. (Q5YEW3), Schlegelella sp. KB1a (Q5YEW3)
brenda
Reinhardt, S.; Handrick, R.; Jendrossek, D.
The PHB Depolymerase Inhibitor of Paucimonas lemoignei is a PHB depolymerase
Biomacromolecules
3
823-827
2002
Paucimonas lemoignei
brenda
Sugiyama, A.; Kobayashi, T.; Shiraki, M.; Saito, T.
Roles of poly(3-hydroxybutyrate) depolymerase and 3HB-oligomer hydrolase in bacterial PHB metabolism
Curr. Microbiol.
48
424-427
2004
Acidovorax sp., Cupriavidus necator, Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1, Ralstonia pickettii, Ralstonia pickettii T1
brenda
Kobayashi, T.; Nishikori, K.; Saito, T.
Properties of an intracellular poly(3-hydroxybutyrate) depolymerase (PhaZ1) from Rhodobacter spheroides
Curr. Microbiol.
49
199-202
2004
Cereibacter sphaeroides
brenda
Braaz, R.; Wong, S.L.; Jendrossek, D.
Production of PHA depolymerase A (PhaZ5) from Paucimonas lemoignei in Bacillus subtilis
FEMS Microbiol. Lett.
209
237-241
2002
Paucimonas lemoignei
brenda
Braaz, R.; Handrick, R.; Jendrossek, D.
Identification and characterisation of the catalytic triad of the alkaliphilic thermotolerant PHA depolymerase PhaZ7 of Paucimonas lemoignei
FEMS Microbiol. Lett.
224
107-112
2003
Paucimonas lemoignei
brenda
Kobayashi, T.; Shiraki, M.; Abe, T.; Sugiyama, A.; Saito, T.
Purification and properties of an intracellular 3-hydroxybutyrate-oligomer hydrolase (PhaZ2) in Ralstonia eutropha H16 and its identification as a novel intracellular poly(3-hydroxybutyrate) depolymerase
J. Bacteriol.
185
3485-3490
2003
Cupriavidus necator
brenda
Handrick, R.; Reinhardt, S.; Kimmig, P.; Jendrossek, D.
The "intracellular" poly(3-hydroxybutyrate) (PHB) depolymerase of Rhodospirillum rubrum is a periplasm-located protein with specificity for native PHB and with structural similarity to extracellular PHB depolymerases
J. Bacteriol.
186
7243-7253
2004
Rhodospirillum rubrum
brenda
Abe, T.; Kobayashi, T.; Saito, T.
Properties of a novel intracellular poly(3-hydroxybutyrate) depolymerase with high specific activity (PhaZd) in Wautersia eutropha H16
J. Bacteriol.
187
6982-6990
2005
Cupriavidus necator, Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
brenda
Han, J.S.; Kim, M.N.
Purification and characterization of extracellular poly(3-hydroxybutyrate) depolymerase from Penicillium simplicissimum LAR13
J. Microbiol.
40
20-25
2002
Penicillium simplicissimum, Penicillium simplicissimum LAR13
-
brenda
Hisano, T.; Kasuya, K.I.; Tezuka, Y.; Ishii, N.; Kobayashi, T.; Shiraki, M.; Oroudjev, E.; Hansma, H.; Iwata, T.; Doi, Y.; Saito, T.; Miki, K.
The crystal structure of polyhydroxybutyrate depolymerase from Penicillium funiculosum provides insights into the recognition and degradation of biopolyesters
J. Mol. Biol.
356
993-1004
2006
Talaromyces funiculosus
brenda
Gebauer, B.; Jendrossek, D.
Assay of poly(3-hydroxybutyrate) depolymerase activity and product determination
Appl. Environ. Microbiol.
72
6094-6100
2006
Paucimonas lemoignei
brenda
Hiraishi, T.; Hirahara, Y.; Doi, Y.; Maeda, M.; Taguchi, S.
Effects of mutations in the substrate-binding domain of poly[(R)-3-hydroxybutyrate] (PHB) depolymerase from Ralstonia pickettii T1 on PHB degradation
Appl. Environ. Microbiol.
72
7331-7338
2006
Ralstonia pickettii (P12625), Ralstonia pickettii T1 (P12625)
brenda
Uchino, K.; Saito, T.; Jendrossek, D.
Poly(3-hydroxybutyrate) (PHB) depolymerase PhaZa1 is involved in mobilization of accumulated PHB in Ralstonia eutropha H16
Appl. Environ. Microbiol.
74
1058-1063
2007
Cupriavidus necator, Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
brenda
Numata, K.; Yamashita, K.; Fujita, M.; Tsuge, T.; Kasuya, K.; Iwata, T.; Doi, Y.; Abe, H.
Adsorption and hydrolysis reactions of poly(hydroxybutyric acid) depolymerases secreted from Ralstonia pickettii T1 and Penicillium funiculosum onto poly[(R)-3-hydroxybutyric acid]
Biomacromolecules
8
2276-2281
2007
Talaromyces funiculosus, Ralstonia pickettii, Ralstonia pickettii T1
brenda
Calabia, B.P.; Tokiwa, Y.
A novel PHB depolymerase from a thermophilic Streptomyces sp.
Biotechnol. Lett.
28
383-388
2006
Streptomyces sp.
brenda
Takaku, H.; Kimoto, A.; Kodaira, S.; Nashimoto, M.; Takagi, M.
Isolation of a Gram-positive poly(3-hydroxybutyrate) (PHB)-degrading bacterium from compost, and cloning and characterization of a gene encoding PHB depolymerase of Bacillus megaterium N-18-25-9
FEMS Microbiol. Lett.
264
152-159
2006
Priestia megaterium (A0A8W8), Priestia megaterium N-18-25-9 (A0A8W8)
brenda
Tseng, C.L.; Chen, H.J.; Shaw, G.C.
Identification and characterization of the Bacillus thuringiensis phaZ gene, encoding new intracellular poly-3-hydroxybutyrate depolymerase
J. Bacteriol.
188
7592-7599
2006
Bacillus thuringiensis
brenda
Uchino, K.; Saito, T.; Gebauer, B.; Jendrossek, D.
Isolated poly(3-hydroxybutyrate) (PHB) granules are complex bacterial organelles catalyzing formation of PHB from acetyl coenzyme A (CoA) and degradation of PHB to acetyl-CoA
J. Bacteriol.
189
8250-8256
2007
Cupriavidus necator
brenda
Saha, S.P.; Patra, A.; Paul, A.K.
Studies on intracellular degradation of polyhydroxyalkanoic acid-polyethylene glycol copolymer accumulated by Azotobacter chroococcum MAL-201
J. Biotechnol.
132
325-330
2007
Azotobacter chroococcum, Azotobacter chroococcum MAL-201
brenda
Liu, H.; Zhang, H.; Chen, S.; Liu, D.; Xia, H.
Purification and properties of a poly(beta-hydroxybutyrate) depolymerase from Penicillium sp.
J. Polym. Environ.
14
419-426
2006
Penicillium sp., Penicillium sp. DS9701-09a
-
brenda
Sang, B.; Lee, W.; Hori, K.; Unno, H.
Purification and characterization of fungal poly(3-hydroxybutyrate) depolymerase from Paecilomyces lilacinus F4-5 and enzymatic degradation of poly(3-hydroxybutyrate-co-3-hydroxyvalerate) film
World J. Microbiol. Biotechnol.
22
51-57
2006
Purpureocillium lilacinum, Purpureocillium lilacinum F4-5
brenda
Ci, S.; Shan, C.; Liu, D.; Xia, H.
An extracellular poly(3-hydroxybutyrate) depolymerase from Penicillium sp. DS9713a-01
World J. Microbiol. Biotechnol.
22
729-735
2006
Penicillium sp., Penicillium sp. DS9713a-01
brenda
Sugimoto, A.; Shiraki, M.; Hatakeyama, S.; Saito, T.
Secretion pathway for the poly(3-hydroxybutyrate) depolymerase in Ralstonia pickettii T1
Antonie van Leeuwenhoek
94
223-232
2008
Ralstonia pickettii (P12625), Ralstonia pickettii T1 (P12625), Ralstonia pickettii T1
brenda
Phithakrotchanakoon, C.; Daduang, R.; Thamchaipenet, A.; Wangkam, T.; Srikhirin, T.; Eurwilaichitr, L.; Champreda, V.
Heterologous expression of polyhydroxyalkanoate depolymerase from Thermobifida sp. in Pichia pastoris and catalytic analysis by surface plasmon resonance
Appl. Microbiol. Biotechnol.
82
131-140
2009
Thermobifida sp. BCC23166 (B3VS85)
brenda
Papaneophytou, C.P.; Pantazaki, A.A.; Kyriakidis, D.A.
An extracellular polyhydroxybutyrate depolymerase in Thermus thermophilus HB8
Appl. Microbiol. Biotechnol.
83
659-668
2009
Thermus thermophilus HB8
brenda
Matsumoto, N.; Fujita, M.; Hiraishi, T.; Abe, H.; Maeda, M.
Adsorption characteristics of P(3HB) depolymerase as evaluated by surface plasmon resonance and atomic force microscopy
Biomacromolecules
9
3201-3207
2008
Ralstonia pickettii (P12625), Ralstonia pickettii T1 (P12625), Ralstonia pickettii T1
brenda
Cai, L.; Yuan, M.Q.; Liu, F.; Jian, J.; Chen, G.Q.
Enhanced production of medium-chain-length polyhydroxyalkanoates (PHA) by PHA depolymerase knockout mutant of Pseudomonas putida KT2442
Biores. Technol.
100
2265-2270
2009
Pseudomonas putida
brenda
de Eugenio, L.I.; Garcia, J.L.; Garcia, P.; Prieto, M.A.; Sanz, J.M.
Comparative analysis of the physiological and structural properties of a medium chain length polyhydroxyalkanoate depolymerase from Pseudomonas putida KT2442
Eng. Life Sci.
8
260-267
2008
Pseudomonas putida, Pseudomonas fluorescens (Q51718), Pseudomonas fluorescens GK13 (Q51718)
-
brenda
Park, S.W.; Chung, M.G.; Lee, H.Y.; Kim, J.Y.; Rhee, Y.H.
Stable expression and secretion of polyhydroxybutyrate depolymerase of Paucimonas lemoignei in Escherichia coli
J. Microbiol.
46
662-669
2008
Paucimonas lemoignei (P52090), Paucimonas lemoignei
brenda
Papageorgiou, A.C.; Hermawan, S.; Singh, C.B.; Jendrossek, D.
Structural basis of poly(3-hydroxybutyrate) hydrolysis by PhaZ7 depolymerase from Paucimonas lemoignei
J. Mol. Biol.
382
1184-1194
2008
Paucimonas lemoignei (Q939Q9), Paucimonas lemoignei
brenda
Zhou, H.; Wang, Z.; Chen, S.; Liu, D.; Xia, H.
Purification and characterization of extracellular poly(beta -hydroxybutyrate) depolymerase from Penicillium sp. DS9701-D2
Polym. -Plast. Technol. Eng.
48
58-63
2009
Penicillium sp., Penicillium sp. DS9701-D2
-
brenda
Shah, A.A.; Hasan, F.; Hameed, A.; Ahmed, S.
A novel poly(3-hydroxybutyrate)-degrading Streptoverticillium kashmirense AF1 isolated from soil and purification of PHB-depolymerase
Acta Biol. Hung.
59
489-499
2008
Streptomyces kashimirensis, Streptomyces kashimirensis AF1
brenda
Chen, H.J.; Pan, S.C.; Shaw, G.C.
Identification and characterization of a novel intracellular poly(3-hydroxybutyrate) depolymerase from Bacillus megaterium
Appl. Environ. Microbiol.
75
5290-5299
2009
Priestia megaterium (C7A621), Priestia megaterium
brenda
Hiraishi, T.; Komiya, N.; Matsumoto, N.; Abe, H.; Fujita, M.; Maeda, M.
Degradation and adsorption characteristics of PHB depolymerase as revealed by kinetics of mutant enzymes with amino acid substitution in substrate-binding domain
Biomacromolecules
11
113-119
2010
Ralstonia pickettii
brenda
Trainer, M.A.; Capstick, D.; Zachertowska, A.; Lam, K.N.; Clark, S.R.; Charles, T.C.
Identification and characterization of the intracellular poly-3-hydroxybutyrate depolymerase enzyme PhaZ of Sinorhizobium meliloti
BMC Microbiol.
10
92
2010
Sinorhizobium meliloti
brenda
Garcia-Hidalgo, J.; Hormigo, D.; Prieto, M.A.; Arroyo, M.; de la Mata, I.
Extracellular production of Streptomyces exfoliatus poly(3-hydroxybutyrate) depolymerase in Rhodococcus sp. T104: determination of optimal biocatalyst conditions
Appl. Microbiol. Biotechnol.
93
1975-1988
2012
Streptomyces exfoliatus, Streptomyces exfoliatus DSM Z 41693
brenda
Allen, A.; Anderson, W.; Ayorinde, F.; Eribo, B.
Isolation and characterization of an extracellular thermoalkanophilic P(3HB-co-3HV) depolymerase from Streptomyces sp. IN1
Int. Biodeterior. Biodegradation
65
777-785
2011
Streptomyces sp., Streptomyces sp. IN1
-
brenda
Bhatt, R.; Patel, K.; Trivedi, U.
Purification and properties of extracellular poly(3-hydroxybutyrate) depolymerase produced by Aspergillus fumigatus 202
J. Polym. Environ.
18
141-147
2010
Aspergillus fumigatus, Aspergillus fumigatus 202
-
brenda
Brigham, C.J.; Reimer, E.N.; Rha, C.; Sinskey, A.J.
Examination of PHB depolymerases in Ralstonia eutropha: further elucidation of the roles of enzymes in PHB homeostasis
AMB Express
2
26
2012
Cupriavidus necator (Q0JYJ1), Cupriavidus necator (Q0JZG9), Cupriavidus necator (Q0K2G9), Cupriavidus necator (Q0K4D5), Cupriavidus necator (Q0K7T2), Cupriavidus necator (Q0KCI0), Cupriavidus necator (Q7WXF6), Cupriavidus necator, Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1 (Q0JYJ1), Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1 (Q0JZG9), Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1 (Q0K2G9), Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1 (Q0K4D5), Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1 (Q0K7T2), Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1 (Q0KCI0), Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1 (Q7WXF6)
brenda
Gangoiti, J.; Santos, M.; Prieto, M.A.; de la Mata, I.; Serra, J.L.; Llama, M.J.
Characterization of a novel subgroup of extracellular medium-chain-length polyhydroxyalkanoate depolymerases from actinobacteria
Appl. Environ. Microbiol.
78
7229-7237
2012
Streptomyces atratus, Streptomyces anulatus, Streptomyces omiyaensis, Streptomyces beijiangensis, Streptomyces pulveraceus, Streptomyces roseolus, Streptomyces anulatus SL11, Streptomyces omiyaensis SO2 CECT 7923, Streptomyces roseolus SL3 CECT 7919, Streptomyces atratus SL2, Streptomyces pulveraceus W3, Streptomyces beijiangensis SL15
brenda
Sznajder, A.; Jendrossek, D.
To be or not to be a poly(3-hydroxybutyrate) (PHB) depolymerase: PhaZd1 (PhaZ6) and PhaZd2 (PhaZ7) of Ralstonia eutropha, highly active PHB depolymerases with no detectable role in mobilization of accumulated PHB
Appl. Environ. Microbiol.
80
4936-4946
2014
Cupriavidus necator (Q0JYJ1), Cupriavidus necator (Q0JZG9), Cupriavidus necator, Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1 (Q0JYJ1), Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1 (Q0JZG9)
brenda
Tan, L.T.; Hiraishi, T.; Sudesh, K.; Maeda, M.
Directed evolution of poly[(R)-3-hydroxybutyrate] depolymerase using cell surface display system: functional importance of asparagine at position 285
Appl. Microbiol. Biotechnol.
97
4859-4871
2013
Ralstonia pickettii (P12625), Ralstonia pickettii T1 (P12625), Ralstonia pickettii T1
brenda
Tan, L.T.; Hiraishi, T.; Sudesh, K.; Maeda, M.
Effects of mutation at position 285 of Ralstonia pickettii T1 poly[(R)-3-hydroxybutyrate] depolymerase on its activities
Appl. Microbiol. Biotechnol.
98
7061-7068
2014
Ralstonia pickettii (P12625), Ralstonia pickettii T1 (P12625), Ralstonia pickettii T1
brenda
Mao, H.; Jiang, H.; Su, T.; Wang, Z.
Purification and characterization of two extracellular polyhydroxyalkanoate depolymerases from Pseudomonas mendocina
Biotechnol. Lett.
35
1919-1924
2013
Pseudomonas mendocina, Pseudomonas mendocina DS04-T
brenda
Jendrossek, D.; Hermawan, S.; Subedi, B.; Papageorgiou, A.C.
Biochemical analysis and structure determination of Paucimonas lemoignei poly(3-hydroxybutyrate) (PHB) depolymerase PhaZ7 muteins reveal the PHB binding site and details of substrate-enzyme interactions
Mol. Microbiol.
90
649-664
2013
Paucimonas lemoignei (Q939Q9), Paucimonas lemoignei
brenda
Garcia-Hidalgo, J.; Hormigo, D.; Arroyo, M.; de la Mata, I.
Novel extracellular PHB depolymerase from Streptomyces ascomycinicus: PHB copolymers degradation in acidic conditions
PLoS ONE
8
e71699
2013
Streptomyces ascomycinicus (Q9KIF2), Streptomyces ascomycinicus, Streptomyces ascomycinicus DSM Z 40822 (Q9KIF2)
brenda
Gowda U S, V.; Shivakumar, S.
Poly(-beta-hydroxybutyrate) (PHB) depolymerase PHAZ Pen from Penicillium expansum purification, characterization and kinetic studies
3 Biotech
5
901-909
2015
Penicillium expansum
brenda
Juengert, J.; Patterson, C.; Jendrossek, D.
Poly(3-hydroxybutyrate) (PHB) polymerase PhaC1 and PHB depolymerase PhaZa1 of Ralstonia eutropha are phosphorylated in vivo
Appl. Environ. Microbiol.
84
e00604
2018
Cupriavidus necator (Q0KCI0), Cupriavidus necator
brenda
Martinez-Tobon, D.I.; Gul, M.; Elias, A.L.; Sauvageau, D.
Polyhydroxybutyrate (PHB) biodegradation using bacterial strains with demonstrated and predicted PHB depolymerase activity
Appl. Microbiol. Biotechnol.
102
8049-8067
2018
Comamonas testosteroni, Ralstonia sp., Cupriavidus sp.
brenda
Lee, M.; Liu, E.; Yang, C.; Hsiao, L.; Wu, T.; Li, S.
Co-expression of ORFCma with PHB depolymerase (PhaZCma) in Escherichia coli induces efficient whole-cell biodegradation of polyesters
Biotechnol. J.
13
1700560
2018
Caldimonas manganoxidans (Q9LBN6)
brenda
Vigneswari, S.; Lee, T.; Bhubalan, K.; Amirul, A.
Extracellular polyhydroxyalkanoate depolymerase by Acidovorax sp. DP5
Enzyme Res.
2015
212159
2015
Acidovorax sp. DP5
brenda
Aly, M.; Tork, S.; Qari, H.; Al-Seeni, M.
Poly-beta-hydroxy butyrate depolymerase from Streptomyces lydicus MM10, isolated from wastewater sample
Int. J. Agric. Biol.
17
891-900
2015
Streptomyces lydicus, Streptomyces lydicus MM10
-
brenda
York, G.M.; Lupberger, J.; Tian, J.; Lawrence, A.G.; Stubbe, J.; Sinskey, A.J.
Ralstonia eutropha H16 encodes two and possibly three intracellular poly[D-(-)-3-hydroxybutyrate] depolymerase genes
J. Bacteriol.
185
3788-3794
2003
Cupriavidus necator (Q7WT48), Cupriavidus necator
brenda
Arikawa, H.; Sato, S.; Fujiki, T.; Matsumoto, K.
A study on the relation between poly(3-hydroxybutyrate) depolymerases or oligomer hydrolases and molecular weight of polyhydroxyalkanoates accumulating in Cupriavidus necator H16
J. Biotechnol.
227
94-102
2016
Cupriavidus necator (Q0KCI0), Cupriavidus necator
brenda
Sung, C.; Tachibana, Y.; Kasuya, K.
Characterization of a thermolabile poly(3-hydroxybutyrate) depolymerase from the marine bacterium Shewanella sp. JKCM-AJ-6,1alpha
Polym. Degrad. Stab.
129
212-221
2016
Shewanella sp. JKCM-AJ-6,1A
-
brenda
Jung, H.; Yang, M.; Su, R.
Purification, characterization, and gene cloning of an Aspergillus fumigatus polyhydroxybutyrate depolymerase used for degradation of polyhydroxybutyrate, polyethylene succinate, and polybutylene succinate
Polym. Degrad. Stab.
154
186-194
2018
Aspergillus fumigatus, Aspergillus fumigatus 76T-3
-
brenda
Li, F.; Zhang, C.; Liu, Y.; Liu, D.; Xia, H.; Chen, S.
Efficient production of (R)-3-hydroxybutyric acid by Pseudomonas sp. DS1001a and its extracellular poly(3-hydroxybutyrate) depolymerase
Process Biochem.
51
369-373
2016
Pseudomonas sp. DS1001a
-
brenda
Kellici, T.; Mavromoustakos, T.; Jendrossek, D.; Papageorgiou, A.
Crystal structure analysis, covalent docking, and molecular dynamics calculations reveal a conformational switch in PhaZ7 PHB depolymerase
Proteins
85
1351-1361
2017
Paucimonas lemoignei (Q939Q9)
brenda