3.4.23.42: thermopsin
This is an abbreviated version!
For detailed information about thermopsin, go to the full flat file.
Word Map on EC 3.4.23.42
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3.4.23.42
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hallux
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metatarsophalangeal
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valgus
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acidocaldarius
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rigidus
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forefoot
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dorsiflexion
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nonunion
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screw
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pepstatin-insensitive
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intermetatarsal
- 3.4.23.42
- hallux
-
metatarsophalangeal
- valgus
- acidocaldarius
-
rigidus
-
forefoot
-
dorsiflexion
-
nonunion
-
screw
-
pepstatin-insensitive
-
intermetatarsal
Reaction
similar in specificity to pepsin A preferring bulky hydrophobic amino acids in P1 and P1' =
Synonyms
EC 3.4.99.43, More, MTP-1, SsMTP, SSO1175, SSO2045, Sulfolobus solfataricus multidomain thermopsin-like protease, thpS
ECTree
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Substrates Products
Substrates Products on EC 3.4.23.42 - thermopsin
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REACTION DIAGRAM
FVNQHLCGSHLVEALYLVCGERGFFYTPKA + H2O
FVNQHLCGSHL + VEAL + YLVCGERGF + L-Phe + YTPKA
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substrate insulin B chain
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-
?
Lys-Pro-Ala-Glu-Phe-Nph-Ala-Leu + H2O
Lys-Pro-Ala-Glu-Phe + Nph-Ala-Leu
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synthetic chromogenic substrate
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-
?
oxidized insulin B + H2O
?
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following bonds are hydrolyzed: Leu-Val, Leu-Tyr, Phe-Phe, Phe-Tyr, Tyr-Thr
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-
?
?
the preferential peptide bonds hydrolyzed are: Phe-Phe, Tyr-Leu, Phe-Tyr, Leu-Val and Tyr-Thr
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-
?
Bovine insulin B-chain + H2O
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the preferential peptide bonds hydrolyzed are: Phe-Phe, Tyr-Leu, Phe-Tyr, Leu-Val and Tyr-Thr
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-
?
Hemoglobin + H2O
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the preferential peptide bonds hydrolyzed are: Phe-Phe, Tyr-Leu, Phe-Tyr, Leu-Val and Tyr-Thr
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-
?
Hemoglobin + H2O
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the preferential peptide bonds hydrolyzed are: Phe-Phe, Tyr-Leu, Phe-Tyr, Leu-Val and Tyr-Thr
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-
?
?
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cleavage sites are Val-Asn, Cys-Gly, Leu-Tyr, Glu-Arg, Gly-Phe and Pro-Lys
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?
insulin B chain + H2O
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cleavage sites are Val-Asn, Cys-Gly, Leu-Tyr, Glu-Arg, Gly-Phe and Pro-Lys
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?
insulin B chain + H2O
?
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cleavage sites are Val-Asn, Cys-Gly, Leu-Tyr, Glu-Arg, Gly-Phe and Pro-Lys
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?
Lys-Pro-Ala-Glu-Phe + (4-nitro)Phe-Ala-Leu
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-
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?
Lys-Pro-Ala-Glu-Phe-(4-nitro)Phe-Ala-Leu + H2O
Lys-Pro-Ala-Glu-Phe + (4-nitro)Phe-Ala-Leu
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-
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?
N-CBZ-Gly + 4-nitrophenol
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-
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?
N-CBZ-glycine 4-nitrophenyl ester + H2O
N-CBZ-Gly + 4-nitrophenol
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?
N-CBZ-glycine 4-nitrophenyl ester + H2O
N-CBZ-Gly + 4-nitrophenol
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-
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?
?
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the enzyme shows no sequence similarity to aspartic proteases of the pepsin family or to pepstatin-insensitive acid protease. The characteristic active site amino acid sequence for aspartic proteases, Asp-Thr-Gly, which is present in all aspartic proteases even with only distant evolutionary relatedness, is absent in SsMTP from Sulfolobus solfataricus as in Sulfolobus acidocaldarius thermopsin, suggesting that different catalytic mechanisms are employed by these proteases
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-
?
additional information
?
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the enzyme shows no sequence similarity to aspartic proteases of the pepsin family or to pepstatin-insensitive acid protease. The characteristic active site amino acid sequence for aspartic proteases, Asp-Thr-Gly, which is present in all aspartic proteases even with only distant evolutionary relatedness, is absent in SsMTP from Sulfolobus solfataricus as in Sulfolobus acidocaldarius thermopsin, suggesting that different catalytic mechanisms are employed by these proteases
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-
?
additional information
?
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the enzyme shows no sequence similarity to aspartic proteases of the pepsin family or to pepstatin-insensitive acid protease. The characteristic active site amino acid sequence for aspartic proteases, Asp-Thr-Gly, which is present in all aspartic proteases even with only distant evolutionary relatedness, is absent in SsMTP from Sulfolobus solfataricus as in Sulfolobus acidocaldarius thermopsin, suggesting that different catalytic mechanisms are employed by these proteases
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-
?
additional information
?
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the enzyme shows a broad protein substrate specificity, it is involved in supply of nutrients from protein substrates
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?
additional information
?
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the enzyme shows a broad protein substrate specificity
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?
additional information
?
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The characteristic active site amino acid sequence for aspartic proteases, Asp Thr Gly, which is present in all aspartic proteases even with only distant evolutionary relatedness, is absent in thermopsin from Sulfolobus acidocaldarius, suggesting that a different catalytic mechanisms is employed.
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?