Literature summary for 3.4.22.B49 extracted from

Stack, C.M.; Donnelly, S.; Lowther, J.; Xu, W.; Collins, P.R.; Brinen, L.S.; Dalton, J.P.
The major secreted cathepsin L1 protease of the liver fluke, Fasciola hepatica: a Leu-12 to Pro-12 replacement in the nonconserved C-terminal region of the prosegment prevents complete enzyme autoactivation and allows definition of the molecular events in (2007), J. Biol. Chem., 282, 16532-16543.

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Protein Variants

Protein Variants	Comment	Organism
C26G	active site variant FheproCL1C26G cannot autocatalytically process. It is susceptible to trans-processing at a Leu12-Ser11/His10 sequence by preactivated FheCL1	Fasciola hepatica
L12P	the autoactivation of the variant enzyme FheproCL1L12P is very slow but is increased 40fold in the presence of FheCL2	Fasciola hepatica
L12P/C26G	active site variant FheproCL1L12P/C26G cannot autocatalytically process. It is not susceptible to trans-processing at a Leu12-Ser11/His10 sequence by preactivated FheCL1. Another Fasciola hepatica secreted protease FheCL2, which, unlike FheCL1, can readily accept proline in the S2 subsite of its active site, can trans-process the double variant FheproCL1L12P/C26G by cleavage at the Pro12-Ser11/His10 sequence	Fasciola hepatica

Organism

Organism	UniProt	Comment	Textmining
Fasciola hepatica	-	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
proteolytic modification	procathepsin L1 autocatalytically processes and activates to its mature enzyme (FheCL1) over a wide pH range 4.0-7.3. Activation is more rapid at low pH. Maturation initiates with cleavages of a small proportion of molecules within the central region of the prosegment, possibly by intramolecular events. Activation to fully mature enzymes is achieved by a precise intermolecular cleavage at a Leu12-Ser11/His10 sequence within the nonconserved C-terminal region of the prosegment. Active site variant FheproCL1C26G and a double variant FheproCL1L12P/C26G cannot autocatalytically process. The former is susceptible to trans-processing at a Leu12-Ser11/His10 sequence by preactivated FheCL1, but the latter is not. Another Fasciola hepatica secreted protease FheCL2, which, unlike FheCL1, can readily accept proline in the S2 subsite of its active site, can trans-process the double variant FheproCL1L12P/C26G by cleavage at the Pro12-Ser11/His10 sequence. The autoactivation of a variant enzyme with a single replacement, FheproCL1L12P, is very slow but is increased 40fold in the presence of FheCL2	Fasciola hepatica
proteolytic modification	procathepsin L1 autocatalytically processes and activates to its mature enzyme (FheCL1) over a wide pH range 4.0-7.3. Activation is more rapid at low pH. Maturation initiates with cleavages of a small proportion of molecules within the central region of the prosegment, possibly by intramolecular events. Activation to fully mature enzymes is achieved by a precise intermolecular cleavage at a Leu12-Ser11/His10 sequence within the nonconserved C-terminal region of the prosegment. Active site variant FheproCL1C26G and a double variant FheproCL1L12P/C26G cannot autocatalytically process. The former is susceptible to trans-processing at a Leu12-Ser11-/-His10 sequence by preactivated FheCL1, but the latter is not. Another Fasciola hepatica secreted protease FheCL2, which, unlike FheCL1, can readily accept proline in the S2 subsite of its active site, can trans-process the double variant FheproCL1L12P/C26G by cleavage at the Pro12-Ser11-/-His10 sequence. The autoactivation of a variant enzyme with a single replacement, FheproCL1L12P, is very slow but is increased 40fold in the presence of FheCL2	Fasciola hepatica

Source Tissue

Source Tissue	Comment	Organism	Textmining

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
procathepsin L1 + H2O	procathepsin L1 autocatalytically processes and activates to its mature enzyme (FheCL1) over a wide pH range 4.0-7.3. Activation is more rapid at low pH. Maturation initiates with cleavages of a small proportion of molecules within the central region of the prosegment, possibly by intramolecular events. Activation to fully mature enzymes is achieved by a precise intermolecular cleavage at a Leu12-Ser11-/-His10 sequence within the nonconserved C-terminal region of the prosegment. Active site variant FheproCL1C26G and a double variant FheproCL1L12P/C26G cannot autocatalytically process. The former is susceptible to trans-processing at a Leu12-Ser11-/-His10 sequence by preactivated FheCL1, but the latter is not	Fasciola hepatica	?	-	?

Synonyms

Synonyms	Comment	Organism
cathepsin L1 protease	-	Fasciola hepatica
FheCL1	-	Fasciola hepatica

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Release 2023.1 (January 2023)