Coagulation Factor IX Human

Identification

Name
Coagulation Factor IX Human
Accession Number
DB13152
Description

Factor IX (or Christmas factor) is one of the serine proteases of the coagulation system; it belongs to peptidase family S1. Deficiency of this protein causes hemophilia B.

Type
Biotech
Groups
Approved
Biologic Classification
Protein Based Therapies
Blood factors
Protein Structure
Db13152
Protein Chemical Formula
C2041H3136N558O641S25
Protein Average Weight
46548.2 Da
Sequences
>DB00100 sequence
YNSGKLEEFVQGNLERECMEEKCSFEEAREVFENTERTTEFWKQYVDGDQCESNPCLNGG
SCKDDINSYECWCPFGFEGKNCELDVTCNIKNGRCEQFCKNSADNKVVCSCTEGYRLAEN
QKSCEPAVPFPCGRVSVSQTSKLTRAEAVFPDVDYVNSTEAETILDNITQSTQSFNDFTR
VVGGEDAKPGQFPWQVVLNGKVDAFCGGSIVNEKWIVTAAHCVETGVKITVVAGEHNIEE
TEHTEQKRNVIRIIPHHNYNAAINKYNHDIALLELDEPLVLNSYVTPICIADKEYTNIFL
KFGSGYVSGWGRVFHKGRSALVLQYLRVPLVDRATCLRSTKFTIYNNMFCAGFHEGGRDS
CQGDSGGPHVTEVEGTSFLTGIISWGEECAMKGKYGIYTKVSRYVNWIKEKTKLT
Download FASTA Format
Synonyms
  • Antihemophilic factor B
  • Coagulation factor IX (human)
  • Factor IX (Human)
  • Factor IX purificado
  • Human coagulation factor IX

Pharmacology

Indication

Factor IX is used to treat Christmas disease. Factor IX deficiency is treated by injection factor IX produced from human plasma. Tranexamic acid may be of value in patients undergoing surgery who have inherited factor IX deficiency in order to reduce the perioperative risk of bleeding.

Associated Conditions
Contraindications & Blackbox Warnings
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Pharmacodynamics

Binds vitamin K and factor VIIIa. Cleaves the Arg-Ile bond in factor X to form active factor Xa. Plays a key role in blood coagulation and clotting. Injections of factor IX are used to treat hemophilia B, which is sometimes called Christmas disease. AlphaNine is injected to increase plasma levels of Factor IX and can temporarily correct this coagulation defect. The activated partial thromboplastin time (aPTT) is prolonged in people with hemophilia B. Treatment with factor IX concentrate may normalize the aPTT by temporarily replacing the factor IX. The administration of BeneFIX increases plasma levels of factor IX, and can temporarily correct the coagulation defect in these patients.

Mechanism of action

Coagulation Factor IX is an important protein in the process of hemostasis and normal blood clotting as it plays a key role within the coagulation cascade. It is located within the blood plasma as a zymogen, an antecedent to enzymatic function, in its inactivated state. Factor IX is dependent on the presence of Vitamin K, and is activated to a serine protease by the function of Coagulation Factor XIa. Factor XIa cleaves the peptide bond associated with protein activation in Factor IX, leaving Factor IX with two exposed chains, a light chain and a heavy chain. These two chains are held together by several disulfide bonds that reinforce the structure of Factor IX's activated form. After being activated, Factor IX forms a complex with calcium ions, membrane phospholipids and Coagulation Factor VIII to activate Coagulation Factor X. The activation of Factor X then performs a similarly integral step in the blood coagulation cascade. The ultimate result of phenotypically normal coagulation factors is the creation of platelets for normal blood clotting.

TargetActionsOrganism
ACoagulation factor X
activator
Humans
ACoagulation factor XI
ligand
Humans
ACoagulation factor VII
ligand
Humans
ACoagulation factor VIII
cofactor
Humans
UProthrombinNot AvailableHumans
UProlow-density lipoprotein receptor-related protein 1Not AvailableHumans
UVitamin K-dependent gamma-carboxylaseNot AvailableHumans
Absorption
Not Available
Volume of distribution
Not Available
Protein binding
Not Available
Metabolism
Not Available
Route of elimination
Not Available
Half-life

18.8 ± 5.4 hours.

Clearance

8.62 ± 1.7.

Adverse Effects
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Toxicity
Not Available
Affected organisms
Not Available
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.
DrugInteraction
AbciximabThe therapeutic efficacy of Coagulation Factor IX Human can be decreased when used in combination with Abciximab.
AcenocoumarolThe therapeutic efficacy of Coagulation Factor IX Human can be decreased when used in combination with Acenocoumarol.
Acetylsalicylic acidThe therapeutic efficacy of Coagulation Factor IX Human can be decreased when used in combination with Acetylsalicylic acid.
Alpha-1-proteinase inhibitorAlpha-1-proteinase inhibitor may increase the thrombogenic activities of Coagulation Factor IX Human.
AlteplaseThe therapeutic efficacy of Coagulation Factor IX Human can be decreased when used in combination with Alteplase.
Aminocaproic acidThe risk or severity of adverse effects can be increased when Aminocaproic acid is combined with Coagulation Factor IX Human.
AncrodThe therapeutic efficacy of Coagulation Factor IX Human can be decreased when used in combination with Ancrod.
AnistreplaseThe therapeutic efficacy of Coagulation Factor IX Human can be decreased when used in combination with Anistreplase.
Antithrombin AlfaThe therapeutic efficacy of Coagulation Factor IX Human can be decreased when used in combination with Antithrombin Alfa.
Antithrombin III humanThe therapeutic efficacy of Coagulation Factor IX Human can be decreased when used in combination with Antithrombin III human.
Additional Data Available
  • Extended Description
    Extended Description

    Extended description of the mechanism of action and particular properties of each drug interaction.

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  • Severity
    Severity

    A severity rating for each drug interaction, from minor to major.

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  • Evidence Level
    Evidence Level

    A rating for the strength of the evidence supporting each drug interaction.

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  • Action
    Action

    An effect category for each drug interaction. Know how this interaction affects the subject drug.

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Food Interactions
Not Available

Products

Brand Name Prescription Products
NameDosageStrengthRouteLabellerMarketing StartMarketing EndRegionImage
BebulinKit30 [iU]/1mLIntravenousBaxalta Incorporated1992-08-192018-11-30US flag
Bebulin VHKit300 [iU]/1mLIntravenousBaxter Laboratories2011-03-162012-09-30US flag
Immunine VhPowder, for solutionIntravenousShire Pharma Canada Ulc1996-10-18Not applicableCanada flag
MononineInjection, powder, lyophilized, for solution100 [iU]/1mLIntravenousCSL BEHRING LLC1992-08-202009-04-06US flag
MononineKit1000 [iU]/10mLIntravenousCSL BEHRING LLC1992-08-20Not applicableUS flag
MononineKit500 [iU]/5mLIntravenousCSL BEHRING LLC1992-08-20Not applicableUS flag
Additional Data Available
  • Application Number
    Application Number

    A unique ID assigned by the FDA when a product is submitted for approval by the labeller.

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  • Product Code
    Product Code

    A governmentally-recognized ID which uniquely identifies the product within its regulatory market.

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Mixture Products
NameIngredientsDosageRouteLabellerMarketing StartMarketing EndRegionImage
AlphaNine SDCoagulation Factor IX Human (1000 [iU]/10mL) + Water (1 mL/1mL)KitIntravenousGRIFOLS USA, LLC1990-12-31Not applicableUS flag
AlphaNine SDCoagulation Factor IX Human (1500 [iU]/10mL) + Water (1 mL/1mL)KitIntravenousGRIFOLS USA, LLC1990-12-31Not applicableUS flag
AlphaNine SDCoagulation Factor IX Human (1000 [iU]/10mL) + Water (1 mL/1mL)KitIntravenousGRIFOLS USA, LLC1990-12-312020-03-31US flag
AlphaNine SDCoagulation Factor IX Human (500 [iU]/10mL) + Water (1 mL/1mL)KitIntravenousGRIFOLS USA, LLC1990-12-31Not applicableUS flag
AlphaNine SDCoagulation Factor IX Human (1500 [iU]/10mL) + Water (1 mL/1mL)KitIntravenousGRIFOLS USA, LLC1990-12-312019-10-31US flag
AlphaNine SDCoagulation Factor IX Human (500 [iU]/10mL) + Water (1 mL/1mL)KitIntravenousGRIFOLS USA, LLC1990-12-312018-10-21US flag
Beriplex P/n 1000Coagulation Factor IX Human (1240 unit) + Coagulation factor VII human (1000 unit) + Coagulation factor X human (2040 unit) + Protein C (1640 unit) + Protein S human (1360 unit) + Prothrombin (1600 unit)Powder, for solutionIntravenousCsl Behring2013-11-21Not applicableCanada flag
Beriplex P/n 500Coagulation Factor IX Human (620 unit) + Coagulation factor VII human (500 unit) + Coagulation factor X human (1020 unit) + Protein C (820 unit) + Protein S human (680 unit) + Prothrombin (800 unit)Powder, for solutionIntravenousCsl Behring2011-07-28Not applicableCanada flag
KcentraCoagulation Factor IX Human (1020 U/40mL) + Coagulation factor VII human (700 U/40mL) + Coagulation factor X human (1520 U/40mL) + Protein C (1240 U/40mL) + Protein S human (920 U/40mL) + Prothrombin (1180 U/40mL)KitIntravenousCSL Behring GmbH2013-12-13Not applicableUS flag
KcentraCoagulation Factor IX Human (510 U/20mL) + Coagulation factor VII human (350 U/20mL) + Coagulation factor X human (760 U/20mL) + Protein C (620 U/20mL) + Protein S human (460 U/20mL) + Prothrombin (590 U/20mL)KitIntravenousCSL Behring GmbH2013-04-29Not applicableUS flag

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

Chemical Identifiers

UNII
6U90Y1795T
CAS number
181054-95-5

References

General References
  1. Zogg T, Brandstetter H: Activation mechanisms of coagulation factor IX. Biol Chem. 2009 May-Jun;390(5-6):391-400. doi: 10.1515/BC.2009.057. [PubMed:19361276]
  2. NCBI [Link]
PubChem Substance
347911436
RxNav
221099
AHFS Codes
  • 20:28.16 — Hemostatics
FDA label
Download (1000 KB)
MSDS
Download (34.9 KB)

Clinical Trials

Clinical Trials
PhaseStatusPurposeConditionsCount
4CompletedTreatmentHemophilia B1
4Enrolling by InvitationTreatmentBleeding / Blood Loss,Surgical / Cardiovascular Surgical Procedures / Fresh Frozen Plasma / Prothrombin Complex Concentrates1
4Not Yet RecruitingTreatmentCoagulation Disorders / Massive Hemorrhage / Traumatic haemorrhage1
4WithdrawnTreatmentPostpartum Haemorrhage (PPH)1
3CompletedTreatmentAcute Major Bleeding / Disorders, Blood Coagulation1
3CompletedTreatmentReversal of Anticoagulant Treatment1
3CompletedTreatmentReversal of Coagulopathy1
3RecruitingTreatmentCongestive Heart Failure (CHF) / Heart Disease End Stage1
3RecruitingTreatmentSignificant Bleeding Risk1
2Not Yet RecruitingTreatmentTrauma Injury1

Pharmacoeconomics

Manufacturers
Not Available
Packagers
Not Available
Dosage Forms
FormRouteStrength
Injection, solutionIntravenous500 IU/10mL
Injection, powder, for solutionIntravenous100 IU
Injection, solutionIntravenous1000 U.I.
Injection, solutionIntravenous500 U.I.
Powder, for solutionParenteral1000 U.I.
Powder, for solutionParenteral1500 UI/10ML
Powder, for solutionParenteral1500 U.I.
Powder, for solutionParenteral500 U.I.
Injection, powder, lyophilized, for solutionIntravenous50 IU
Injection, powder, for solutionIntravenous; Parenteral1000 IU
Injection, powder, for solutionIntravenous; Parenteral2000 IU
Injection, powder, for solutionIntravenous; Parenteral250 IU
Injection, powder, for solutionIntravenous; Parenteral3000 IU
Injection, powder, for solutionIntravenous; Parenteral500 IU
KitIntravenous30 [iU]/1mL
KitIntravenous300 [iU]/1mL
Injection, powder, for solutionIntravenous1500 IU
Injection, powder, for solutionIntravenous3000 UI
Injection, powder, lyophilized, for solution600 iu
Powder, for solutionIntravenous
Injection, powder, lyophilized, for solutionIntravenous500 iu/10ml
InjectionIntravenous245 IU
InjectionIntravenous490 IU
Injection, powder, for solutionParenteral1200 U.I.
Injection, powder, for solutionParenteral200 U.I.
Injection, powder, for solutionParenteral600 U.I.
Injection, powder, for solutionIntravenous; Parenteral1000 UI
Injection, powder, for solutionIntravenous; Parenteral2000 UI
Injection, powder, for solutionIntravenous; Parenteral250 UI
Injection, powder, for solutionIntravenous; Parenteral500 UI
Powder, for solutionIntravenous
Powder, for solutionParenteral1000 UI/10ML
Powder, for solutionParenteral200 UI/5ML
Powder, for solutionParenteral500 UI/10ML
KitIntravenous
Injection, powder, lyophilized, for solutionIntravenous100 [iU]/1mL
KitIntravenous1000 [iU]/10mL
KitIntravenous500 [iU]/5mL
InjectionIntravenous1000 iu/10ml
Injection, powder, for solutionParenteral1000 IU
Injection, powder, for solutionParenteral500 IU
Kit; powder, for solutionIntravenous
Injection, powder, for solutionIntravenous1000 UI
Injection, powder, for solutionIntravenous2000 UI
Injection, powder, for solutionIntravenous500 UI
Injection, powder, for solutionIntravenous; Parenteral3000 UI
Prices
Not Available
Patents
Not Available

Properties

State
Liquid
Experimental Properties
PropertyValueSource
melting point (°C)54 °CLink, R.P., Castellino, F.J. Arch. Biochem. Biophsy. 227:259-265 (1983)
hydrophobicity-0.431Not Available
isoelectric point5.20Not Available

Targets

Kind
Protein
Organism
Humans
Pharmacological action
Yes
Actions
Activator
General Function
Serine-type endopeptidase activity
Specific Function
Factor Xa is a vitamin K-dependent glycoprotein that converts prothrombin to thrombin in the presence of factor Va, calcium and phospholipid during blood clotting.
Gene Name
F10
Uniprot ID
P00742
Uniprot Name
Coagulation factor X
Molecular Weight
54731.255 Da
References
  1. Worfolk LA, Robinson RA, Tracy PB: Factor Xa interacts with two sites on monocytes with different functional activities. Blood. 1992 Oct 15;80(8):1989-97. [PubMed:1391956]
  2. Jones KC, Mann KG: A model for the tissue factor pathway to thrombin. II. A mathematical simulation. J Biol Chem. 1994 Sep 16;269(37):23367-73. [PubMed:8083242]
  3. Ambrosini G, Plescia J, Chu KC, High KA, Altieri DC: Activation-dependent exposure of the inter-EGF sequence Leu83-Leu88 in factor Xa mediates ligand binding to effector cell protease receptor-1. J Biol Chem. 1997 Mar 28;272(13):8340-5. [PubMed:9079657]
  4. London FS, Walsh PN: Zymogen factor IX potentiates factor IXa-catalyzed factor X activation. Biochemistry. 2000 Aug 15;39(32):9850-8. [PubMed:10933803]
  5. Scandella DH: Properties of anti-factor VIII inhibitor antibodies in hemophilia A patients. Semin Thromb Hemost. 2000;26(2):137-42. [PubMed:10919405]
  6. Chen X, Ji ZL, Chen YZ: TTD: Therapeutic Target Database. Nucleic Acids Res. 2002 Jan 1;30(1):412-5. [PubMed:11752352]
  7. Di Scipio RG, Kurachi K, Davie EW: Activation of human factor IX (Christmas factor). J Clin Invest. 1978 Jun;61(6):1528-38. [PubMed:659613]
Kind
Protein
Organism
Humans
Pharmacological action
Yes
Actions
Ligand
General Function
Serine-type endopeptidase activity
Specific Function
Factor XI triggers the middle phase of the intrinsic pathway of blood coagulation by activating factor IX.
Gene Name
F11
Uniprot ID
P03951
Uniprot Name
Coagulation factor XI
Molecular Weight
70108.56 Da
References
  1. Sun MF, Zhao M, Gailani D: Identification of amino acids in the factor XI apple 3 domain required for activation of factor IX. J Biol Chem. 1999 Dec 17;274(51):36373-8. [PubMed:10593931]
  2. Gailani D, Ho D, Sun MF, Cheng Q, Walsh PN: Model for a factor IX activation complex on blood platelets: dimeric conformation of factor XIa is essential. Blood. 2001 May 15;97(10):3117-22. [PubMed:11342438]
  3. Di Scipio RG, Kurachi K, Davie EW: Activation of human factor IX (Christmas factor). J Clin Invest. 1978 Jun;61(6):1528-38. [PubMed:659613]
Kind
Protein
Organism
Humans
Pharmacological action
Yes
Actions
Ligand
General Function
Serine-type peptidase activity
Specific Function
Initiates the extrinsic pathway of blood coagulation. Serine protease that circulates in the blood in a zymogen form. Factor VII is converted to factor VIIa by factor Xa, factor XIIa, factor IXa, o...
Gene Name
F7
Uniprot ID
P08709
Uniprot Name
Coagulation factor VII
Molecular Weight
51593.465 Da
References
  1. Baker DC, Robbe SL, Jacobson L, Manco-Johnson MJ, Holler L, Lefkowitz J: Hereditary deficiency of vitamin-K-dependent coagulation factors in Rambouillet sheep. Blood Coagul Fibrinolysis. 1999 Mar;10(2):75-80. [PubMed:10192655]
  2. Hertzberg MS, Facey SL, Hogg PJ: An Arg/Ser substitution in the second epidermal growth factor-like module of factor IX introduces an O-linked carbohydrate and markedly impairs activation by factor XIa and factor VIIa/Tissue factor and catalytic efficiency of factor IXa. Blood. 1999 Jul 1;94(1):156-63. [PubMed:10381508]
  3. Butenas S, van't Veer C, Mann KG: "Normal" thrombin generation. Blood. 1999 Oct 1;94(7):2169-78. [PubMed:10498586]
  4. Celie PH, Lenting PJ, Mertens K: Hydrophobic contact between the two epidermal growth factor-like domains of blood coagulation factor IX contributes to enzymatic activity. J Biol Chem. 2000 Jan 7;275(1):229-34. [PubMed:10617609]
  5. Shord SS, Lindley CM: Coagulation products and their uses. Am J Health Syst Pharm. 2000 Aug 1;57(15):1403-17; quiz 1418-20. [PubMed:10938981]
  6. Di Scipio RG, Kurachi K, Davie EW: Activation of human factor IX (Christmas factor). J Clin Invest. 1978 Jun;61(6):1528-38. [PubMed:659613]
Kind
Protein
Organism
Humans
Pharmacological action
Yes
Actions
Cofactor
General Function
Oxidoreductase activity
Specific Function
Factor VIII, along with calcium and phospholipid, acts as a cofactor for factor IXa when it converts factor X to the activated form, factor Xa.
Gene Name
F8
Uniprot ID
P00451
Uniprot Name
Coagulation factor VIII
Molecular Weight
267007.42 Da
References
  1. Neels JG, Bovenschen N, van Zonneveld AJ, Lenting PJ: Interaction between factor VIII and LDL receptor-related protein. Modulation of coagulation? Trends Cardiovasc Med. 2000 Jan;10(1):8-14. [PubMed:11150722]
  2. Carr ME Jr, Martin EJ, Kuhn JG, Seremetis SV: Effects of recombinant factor VIIa on platelet function and clot structure in blood with deficient prothrombin conversion. Thromb Haemost. 2003 May;89(5):803-11. [PubMed:12719776]
  3. Federici AB: The factor VIII/von Willebrand factor complex: basic and clinical issues. Haematologica. 2003 Jun;88(6):EREP02. [PubMed:12826528]
  4. Kalashnikova LA, Berkovskii AL, Dobrynina LA, Sergeeva EV, Kozlov AA, Aleksandrova EN, Nasonov EL: [Clotting factor VIII in Sneddon syndrome]. Klin Med (Mosk). 2003;81(9):42-5. [PubMed:14598591]
  5. Johansen RF, Sorensen B, Ingerslev J: Acquired haemophilia: dynamic whole blood coagulation utilized to guide haemostatic therapy. Haemophilia. 2006 Mar;12(2):190-7. [PubMed:16476097]
  6. Di Scipio RG, Kurachi K, Davie EW: Activation of human factor IX (Christmas factor). J Clin Invest. 1978 Jun;61(6):1528-38. [PubMed:659613]
Kind
Protein
Organism
Humans
Pharmacological action
Unknown
General Function
Thrombospondin receptor activity
Specific Function
Thrombin, which cleaves bonds after Arg and Lys, converts fibrinogen to fibrin and activates factors V, VII, VIII, XIII, and, in complex with thrombomodulin, protein C. Functions in blood homeostas...
Gene Name
F2
Uniprot ID
P00734
Uniprot Name
Prothrombin
Molecular Weight
70036.295 Da
References
  1. Butenas S, van't Veer C, Mann KG: "Normal" thrombin generation. Blood. 1999 Oct 1;94(7):2169-78. [PubMed:10498586]
  2. Kohler M: Thrombogenicity of prothrombin complex concentrates. Thromb Res. 1999 Aug 15;95(4 Suppl 1):S13-7. [PubMed:10499904]
  3. Seitz R, Dodt J: Virus safety of prothrombin complex concentrates and factor IX concentrates. Thromb Res. 1999 Aug 15;95(4 Suppl 1):S19-23. [PubMed:10499905]
  4. Samis JA, Ramsey GD, Walker JB, Nesheim ME, Giles AR: Proteolytic processing of human coagulation factor IX by plasmin. Blood. 2000 Feb 1;95(3):943-51. [PubMed:10648407]
  5. Bauer KA, Humphries S, Smillie B, Li L, Cooper JA, Barzegar S, Rosenberg RD, Miller GJ: Prothrombin activation is increased among asymptomatic carriers of the prothrombin G20210A and factor V Arg506Gln mutations. Thromb Haemost. 2000 Sep;84(3):396-400. [PubMed:11019961]
Kind
Protein
Organism
Humans
Pharmacological action
Unknown
General Function
Receptor activity
Specific Function
Endocytic receptor involved in endocytosis and in phagocytosis of apoptotic cells. Required for early embryonic development. Involved in cellular lipid homeostasis. Involved in the plasma clearance...
Gene Name
LRP1
Uniprot ID
Q07954
Uniprot Name
Prolow-density lipoprotein receptor-related protein 1
Molecular Weight
504601.695 Da
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed:17139284]
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed:17016423]
  3. Rohlena J, Kolkman JA, Boertjes RC, Mertens K, Lenting PJ: Residues Phe342-Asn346 of activated coagulation factor IX contribute to the interaction with low density lipoprotein receptor-related protein. J Biol Chem. 2003 Mar 14;278(11):9394-401. Epub 2003 Jan 9. [PubMed:12522212]
Kind
Protein
Organism
Humans
Pharmacological action
Unknown
General Function
Gamma-glutamyl carboxylase activity
Specific Function
Mediates the vitamin K-dependent carboxylation of glutamate residues to calcium-binding gamma-carboxyglutamate (Gla) residues with the concomitant conversion of the reduced hydroquinone form of vit...
Gene Name
GGCX
Uniprot ID
P38435
Uniprot Name
Vitamin K-dependent gamma-carboxylase
Molecular Weight
87560.065 Da
References
  1. Lin PJ, Straight DL, Stafford DW: Binding of the factor IX gamma-carboxyglutamic acid domain to the vitamin K-dependent gamma-glutamyl carboxylase active site induces an allosteric effect that may ensure processive carboxylation and regulate the release of carboxylated product. J Biol Chem. 2004 Feb 20;279(8):6560-6. Epub 2003 Dec 2. [PubMed:14660587]
  2. Wu SM, Mutucumarana VP, Geromanos S, Stafford DW: The propeptide binding site of the bovine gamma-glutamyl carboxylase. J Biol Chem. 1997 May 2;272(18):11718-22. [PubMed:9115224]
  3. Rehemtulla A, Roth DA, Wasley LC, Kuliopulos A, Walsh CT, Furie B, Furie BC, Kaufman RJ: In vitro and in vivo functional characterization of bovine vitamin K-dependent gamma-carboxylase expressed in Chinese hamster ovary cells. Proc Natl Acad Sci U S A. 1993 May 15;90(10):4611-5. [PubMed:8506307]
  4. Stanley TB, Wu SM, Houben RJ, Mutucumarana VP, Stafford DW: Role of the propeptide and gamma-glutamic acid domain of factor IX for in vitro carboxylation by the vitamin K-dependent carboxylase. Biochemistry. 1998 Sep 22;37(38):13262-8. [PubMed:9748333]
  5. Stanley TB, Stafford DW, Olivera BM, Bandyopadhyay PK: Identification of a vitamin K-dependent carboxylase in the venom duct of a Conus snail. FEBS Lett. 1997 Apr 21;407(1):85-8. [PubMed:9141486]

Drug created on November 18, 2016 14:36 / Updated on September 25, 2020 15:13

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