Pancrelipase lipase
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Identification
- Summary
Pancrelipase lipase is a lipase used to treat pancreatic exocrine insufficiency.
- Brand Names
- Cotazym, Creon, Pancrease MT, Pancreaze, Pertzye, Viokace, Zenpep
- Generic Name
- Pancrelipase lipase
- DrugBank Accession Number
- DB13147
- Background
Pancrelipase, in general, is composed of a mixture of pancreatic enzymes which include amylases, lipases, and proteases. These enzymes are extracted from porcine pancreatic glands.3 The pancrelipase lipase is an enzyme secreted by the pancreas that is responsible for the hydrolysis of dietary fat molecules in the human digestive system.1 The pancrelipase mixture, including pancrelipase lipase, was developed by Ortho-McNeil-Janssen Pharmaceuticals, Inc and FDA approved on April 12, 2010.4
- Type
- Biotech
- Groups
- Approved
- Biologic Classification
- Protein Based Therapies
Other protein based therapies - Protein Structure
- Protein Chemical Formula
- Not Available
- Protein Average Weight
- 48000.0 Da
- Sequences
>sp|P00591|LIPP_PIG Pancreatic triacylglycerol lipase OS=Sus scrofa OX=9823 GN=PNLIP PE=1 SV=2 SEVCFPRLGCFSDDAPWAGIVQRPLKILPWSPKDVDTRFLLYTNQNQNNYQELVADPSTI TNSNFRMDRKTRFIIHGFIDKGEEDWLSNICKNLFKVESVNCICVDWKGGSRTGYTQASQ NIRIVGAEVAYFVEVLKSSLGYSPSNVHVIGHSLGSHAAGEAGRRTNGTIERITGLDPAE PCFQGTPELVRLDPSDAKFVDVIHTDAAPIIPNLGFGMSQTVGHLDFFPNGGKQMPGCQK NILSQIVDIDGIWEGTRDFVACNHLRSYKYYADSILNPDGFAGFPCDSYNVFTANKCFPC PSEGCPQMGHYADRFPGKTNGVSQVFYLNTGDASNFARWRYKVSVTLSGKKVTGHILVSL FGNEGNSRQYEIYKGTLQPDNTHSDEFDSDVEVGDLQKVKFIWYNNNVINPTLPRVGASK ITVERNDGKVYDFCSQETVREEVLLTLNPC
>sp|P02703|COL_PIG Colipase OS=Sus scrofa OX=9823 GN=CLPS PE=1 SV=3 MEKVLALLLVTLTVAYAVPDPRGIIINLDEGELCLNSAQCKSNCCQHDTILSLSRCALKA RENSECSAFTLYGVYYKCPCERGLTCEGDKSLVGSITNTNFGICHDVGRSSD
Download FASTA Format- Synonyms
- Lipase, pancreatic
- Pancreatic lipase
Pharmacology
- Indication
Please refer to Pancrelipase.
Reduce drug development failure ratesBuild, train, & validate machine-learning modelswith evidence-based and structured datasets.Build, train, & validate predictive machine-learning models with structured datasets.- Associated Conditions
Indication Type Indication Combined Product Details Approval Level Age Group Patient Characteristics Dose Form Used in combination to treat Exocrine pancreatic insufficiency Combination Product in combination with: Pancrelipase amylase (DB11065), Pancrelipase protease (DB11066) •••••••••••• •••••••• ••••••• ••••••• Used in combination to treat Exocrine pancreatic insufficiency Combination Product in combination with: Pancrelipase amylase (DB11065), Pancrelipase protease (DB11066) •••••••••••• •••••••• ••••••• ••••••• Used in combination to treat Exocrine pancreatic insufficiency Combination Product in combination with: Pancrelipase protease (DB11066), Pancrelipase amylase (DB11065) •••••••••••• •••••••• ••••••• ••••••• Used in combination to treat Exocrine pancreatic insufficiency Combination Product in combination with: Pancrelipase protease (DB11066), Pancrelipase amylase (DB11065) •••••••••••• •••••••• ••••••• ••••••• Used in combination to treat Exocrine pancreatic insufficiency Combination Product in combination with: Pancrelipase amylase (DB11065), Pancrelipase protease (DB11066) •••••••••••• •••••••• ••••••• ••••••• - Associated Therapies
- Contraindications & Blackbox Warnings
- Prevent Adverse Drug Events TodayTap into our Clinical API for life-saving information on contraindications & blackbox warnings, population restrictions, harmful risks, & more.Avoid life-threatening adverse drug events with our Clinical API
- Pharmacodynamics
Please refer to Pancrelipase.
- Mechanism of action
Pancrelipase lipase catalyzes the hydrolysis of triglycerides to monoglycerides, glycerol, and fatty acids. This activity is performed by the hydrolyzation of the esters of fatty acids. The hydrolysis is started by the action of colipase which helps to anchor lipase to the lipid-water membrane of the micelle producing a surface change on lipase. The hydrophobic active site is exposed for the binding of triglycerides and further interaction with the catalytic triad. In this triad, the function of the three amino acids allows the formation of a deprotonated serine which becomes a nucleophile and act on the ester carbonyl of the fatty acids for the later formation of monoglyceride and fatty acid monomers.2
Target Actions Organism ADietary fat cleavageHumans - Absorption
Please refer to Pancrelipase.
- Volume of distribution
Please refer to Pancrelipase.
- Protein binding
Please refer to Pancrelipase.
- Metabolism
Please refer to Pancrelipase.
- Route of elimination
Please refer to Pancrelipase.
- Half-life
Please refer to Pancrelipase.
- Clearance
Please refer to Pancrelipase.
- Adverse Effects
- Improve decision support & research outcomesWith structured adverse effects data, including: blackbox warnings, adverse reactions, warning & precautions, & incidence rates. View sample adverse effects data in our new Data Library!Improve decision support & research outcomes with our structured adverse effects data.
- Toxicity
Please refer to Pancrelipase.
- Pathways
- Not Available
- Pharmacogenomic Effects/ADRs
- Not Available
Interactions
- Drug Interactions
- This information should not be interpreted without the help of a healthcare provider. If you believe you are experiencing an interaction, contact a healthcare provider immediately. The absence of an interaction does not necessarily mean no interactions exist.Not Available
- Food Interactions
- Take with food.
Products
- Drug product information from 10+ global regionsOur datasets provide approved product information including:dosage, form, labeller, route of administration, and marketing period.Access drug product information from over 10 global regions.
- Product Images
- Over the Counter Products
Name Dosage Strength Route Labeller Marketing Start Marketing End Region Image Formula C & E Tablet 150 unit Oral Abundance Naturally Ltd 1998-01-05 2006-06-16 Canada - Mixture Products
Name Ingredients Dosage Route Labeller Marketing Start Marketing End Region Image Cotazym Pancrelipase lipase (10000 units) + Pancrelipase amylase (40000 units) + Pancrelipase protease (35000 units) Capsule Oral Organon Canada Inc. 1973-12-31 Not applicable Canada Cotazym Ecs 20 Pancrelipase lipase (25000 units) + Pancrelipase amylase (100000 units) + Pancrelipase protease (100000 units) Capsule, delayed release Oral Organon Canada Inc. 1989-12-31 Not applicable Canada Cotazym Ecs 4 Pancrelipase lipase (4000 unit) + Pancrelipase amylase (11000 unit) + Pancrelipase protease (11000 unit) Capsule Oral Merck Ltd. 1997-08-18 2012-01-23 Canada Cotazym Ecs 8 Pancrelipase lipase (10800 units) + Pancrelipase amylase (42000 units) + Pancrelipase protease (45000 units) Capsule, delayed release Oral Organon Canada Inc. 1980-12-31 Not applicable Canada Creon Pancrelipase lipase (36000 [USP'U]/1) + Pancrelipase amylase (180000 [USP'U]/1) + Pancrelipase protease (114000 [USP'U]/1) Capsule, delayed release pellets Oral AbbVie Inc. 2023-10-12 Not applicable US - Unapproved/Other Products
Name Ingredients Dosage Route Labeller Marketing Start Marketing End Region Image Creon 10 Minimicrospheres Pancrelipase lipase (10000 [USP'U]/1) + Pancrelipase amylase (33200 [USP'U]/1) + Pancrelipase protease (37500 [USP'U]/1) Capsule, delayed release Oral Physicians Total Care, Inc. 2006-09-12 2009-09-30 US Creon 20 Minimicrospheres Pancrelipase lipase (20000 [USP'U]/1) + Pancrelipase amylase (66400 [USP'U]/1) + Pancrelipase protease (75000 [USP'U]/1) Capsule, delayed release Oral Physicians Total Care, Inc. 1995-01-17 2009-09-30 US Pancrelipase Pancrelipase lipase (20000 [USP'U]/1) + Pancrelipase amylase (56000 [USP'U]/1) + Pancrelipase protease (44000 [USP'U]/1) Capsule, delayed release Oral Kaiser Foundations Hospitals 2010-02-01 2010-12-31 US
Categories
- Drug Categories
- Chemical TaxonomyProvided by Classyfire
- Description
- Not Available
- Kingdom
- Organic Compounds
- Super Class
- Organic Acids
- Class
- Carboxylic Acids and Derivatives
- Sub Class
- Amino Acids, Peptides, and Analogues
- Direct Parent
- Peptides
- Alternative Parents
- Not Available
- Substituents
- Not Available
- Molecular Framework
- Not Available
- External Descriptors
- Not Available
- Affected organisms
- Humans and other mammals
Chemical Identifiers
- UNII
- 8MYC33932O
- CAS number
- 9001-62-1
References
- General References
- Chapus C, Rovery M, Sarda L, Verger R: Minireview on pancreatic lipase and colipase. Biochimie. 1988 Sep;70(9):1223-34. [Article]
- Chapus C, Semeriva M, Bovier-Lapierre C, Desnuelle P: Mechanism of pancreatic lipase action. 1. Interfacial activation of pancreatic lipase. Biochemistry. 1976 Nov 16;15(23):4980-7. [Article]
- Creon monograph [Link]
- FDA approval [Link]
- External Links
- PubChem Substance
- 347911431
- 6406
- Wikipedia
- Pancreatic_lipase_family
- FDA label
- Download (483 KB)
- MSDS
- Download (62.3 KB)
Clinical Trials
- Clinical Trials
Clinical Trial & Rare Diseases Add-on Data Package
Explore 4,000+ rare diseases, orphan drugs & condition pairs, clinical trial why stopped data, & more. Preview package Phase Status Purpose Conditions Count Start Date Why Stopped 100+ additional columns Unlock 175K+ rows when you subscribe.View sample dataNot Available Completed Not Available Obesity 1 somestatus stop reason just information to hide Not Available Completed Not Available Pancreatic Fistula 1 somestatus stop reason just information to hide Not Available Completed Not Available Pancreatitis, Chronic 1 somestatus stop reason just information to hide Not Available Completed Basic Science Pancreatitis 1 somestatus stop reason just information to hide Not Available Completed Treatment Cystic Fibrosis (CF) 1 somestatus stop reason just information to hide
Pharmacoeconomics
- Manufacturers
- Not Available
- Packagers
- Not Available
- Dosage Forms
Form Route Strength Capsule, delayed release pellets Oral Capsule, delayed release Oral Capsule, delayed release pellets Not applicable Capsule, delayed release pellets Granule, delayed release Oral Capsule Oral Tablet, coated Oral Capsule, coated pellets Oral Tablet Oral 150 unit Capsule, extended release Oral Capsule, coated Oral 22500 U Ph.Eu Tablet Oral Powder Oral - Prices
- Not Available
- Patents
Patent Number Pediatric Extension Approved Expires (estimated) Region US9198871 No 2015-12-01 2030-02-07 US US8562979 No 2013-10-22 2028-02-20 US US8562980 No 2013-10-22 2028-02-20 US US8562981 No 2013-10-22 2028-02-20 US US8221747 No 2012-07-17 2028-02-20 US US8562978 No 2013-10-22 2028-02-20 US US8246950 No 2012-08-21 2028-02-20 US US7658918 No 2010-02-09 2028-02-20 US
Properties
- State
- Solid
- Experimental Properties
Property Value Source water solubility Slightly soluble 'MSDS' isoelectric point 7.4 Iizuka K. et al. 1991. Ann clin Biochem.
Targets
References
- Chapus C, Semeriva M, Bovier-Lapierre C, Desnuelle P: Mechanism of pancreatic lipase action. 1. Interfacial activation of pancreatic lipase. Biochemistry. 1976 Nov 16;15(23):4980-7. [Article]
Drug created at November 16, 2016 15:28 / Updated at October 03, 2024 04:54