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Human Metabolome Database Version 2.5

 

Showing metabocard for Phosphocreatine (HMDB01511)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-11-05 11:49:50
Accession Number HMDB01511
Secondary Accession Numbers Not Available
Common Name Phosphocreatine
Description Phosphocreatine undergoes irreversible cyclization and dehydration to form creatinine at a fractional rate of 0.026 per day, thus forming approximately 2 g creatinine/day in an adult male. This is the amount of creatine that must be provided either from dietary sources or by endogenous synthesis to maintain the body pool of (creatine and) phosphocreatine. Creatine is an amino acid that plays a vital role as phosphocreatine in regenerating adenosine triphosphate in skeletal muscle to energize muscle contraction. Creatine is phosphorylated to phosphocreatine in muscle in a reaction that is catalyzed by the enzyme creatine kinase. This enzyme is in highest concentration in muscle and nerve. Oral administration increases muscle stores. During the past decade, creatine has assumed prominence as an ergogenic (and legal) aid for professional and elite athletes. Most (~ 95%) of the total body creatine-phosphocreatine pool is in muscle (more in skeletal muscle than in smooth muscle) and amounts to 120 g (or 925 mmol) in a 70 kg adult male. Approximately 60-67% of the content in resting muscle is in the phosphorylated form. This generates enough ATP at the myofibrillar apparatus to power about 4 seconds of muscle contraction in exercise. Phosphocreatine reacts with ADP to yield ATP and creatine; the reversible reaction is catalyzed by creatine kinase. phosphocreatine is the chief store of high-energy phosphates in muscle. Thus, this reaction, which permits the rephosphorylation of ADP to ATP, is the immediate source of energy in muscle contraction. During rest, metabolic processes regenerate phosphocreatine stores. In normal muscle, ATP that is broken down to ADP is immediately rephosphorylated to ATP. Thus, phosphocreatine serves as a reservoir of ATP-synthesizing potential. phosphocreatine is the only fuel available to precipitously regenerate ATP during episodes of rapid fluctuations in demand. The availability of phosphocreatine likely limits muscle performance during brief, high-power exercise, i.e., maximal exercise of short duration. With near maximal isometric contraction, the rate of utilization of phosphocreatine declines after 1-2 seconds of contraction, prior to the glycolysis peak at approximately 3 seconds. (PMID: 10079702, Nutr Rev. 1999 Feb;57(2):45-50.)
Synonyms
  1. Creatine phosphate
  2. Creatine phosphic acid
  3. creatine-P
  4. creatine-phosphate
  5. Creatinephosphoric acid
  6. N-(phosphonoamidino)-Sarcosine
  7. N-(Phosphonoamidino)sarcosine
  8. N-phosphocreatine
  9. N-Phosphorocreatine
  10. N-Phosphorylcreatine
  11. N-[imino(phosphonoamino)methyl]-N-methyl-Glycine
  12. neo-ton
  13. P-creatine
  14. phosphocreatine
  15. phosphorylcreatine
Chemical IUPAC Name 2-[methyl-(N'-phosphonocarbamimidoyl)amino]acetic acid
Chemical Formula C4H10N3O5P
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Amino acids and Amino Acid conjugates
Class
  • Amino Acid Phosphates
Sub Class
  • Non-protetypic phospho-amino acids
Family
  • Mammalian Metabolite
Species
  • carboxylic acid
  • guanidine
  • phosphoric acid amide
Biofunction
  • Component of Arginine and proline metabolism
Application
—
Source
  • Endogenous
Average Molecular Weight 211.113
Monoisotopic Molecular Weight 211.035812
Isomeric SMILES CN(CC(O)=O)C(=N)NP(O)(O)=O
Canonical SMILES CN(CC(O)=O)C(=N)NP(O)(O)=O
KEGG Compound ID C02305 Link Image
BioCyc ID CREATINE-P Link Image
BiGG ID 1594794 Link Image
Wikipedia Link Creatine phosphate Link Image
NuGOwiki Link HMDB01511 Link Image
Metagene Link HMDB01511 Link Image
METLIN ID 6288 Link Image
PubChem Compound 5359254 Link Image
PubChem Substance 7986835 Link Image
ChEBI ID 17287 Link Image
CAS Registry Number 67-07-2
InChI Identifier InChI=1/C4H10N3O5P/c1-7(2-3(8)9)4(5)6-13(10,11)12/h2H2,1H3,(H,8,9)(H4,5,6,10,11,12)
Synthesis Reference Hou, Lixiang. Method for producing creatine phosphate. Faming Zhuanli Shenqing Gongkai Shuomingshu (2004), 7 pp.
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 1000 mg/mL at 25 oC [MEYLAN,WM et al. (1996)]; 3.52 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -3
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -4.22 [MEYLAN,WM & HOWARD,PH (1995)]; -2.01 [Predicted by ALOGPS]; -2.3 [Predicted by PubChem via XLOGP] Calculated using ALOGPS
Material Safety Data Sheet (MSDS)
MOL File Show
SDF File Show
PDB File Show
2D Structure
3D Structure
Experimental PDB ID Not Available
Experimental 1H NMR Spectrum Download Spectrum
Download FID (Varian)
Show Experimental Conditions Link Image
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum
Low Energy
Download File
Show Experimental Conditions Link Image
Medium Energy
Download File
Show Experimental Conditions Link Image
High Energy
Download File
Show Experimental Conditions Link Image
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Show Image
Show Peaklist
Cellular Location
  • Cytoplasm (Predicted from LogP)
  • mitochondria
Biofluid Location Not Available
Tissue Location
Tissue References
Adipose Tissue —
Basal Ganglia —
Brain —
Fibroblasts —
Hippocampus —
Kidney —
Muscle —
Neuron —
Skeletal Muscle —
Skin —
Testes —
Concentrations (Normal) Not Available
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Arginine and Proline Metabolism SMP00020 Link Image map00330 Link Image
General References
  1. Pastoris O, Dossena M, Foppa P, Catapano M, Arbustini E, Bellini O, Dal Bello B, Minzioni G, Ceriana P, Barzaghi N: Effect of L-carnitine on myocardial metabolism: results of a balanced, placebo-controlled, double-blind study in patients undergoing open heart surgery. Pharmacol Res. 1998 Feb;37(2):115-22. [PubMed Link Image]
  2. Green AL, Hultman E, Macdonald IA, Sewell DA, Greenhaff PL: Carbohydrate ingestion augments skeletal muscle creatine accumulation during creatine supplementation in humans. Am J Physiol. 1996 Nov;271(5 Pt 1):E821-6. [PubMed Link Image]
  3. Skare OC, Skadberg, Wisnes AR: Creatine supplementation improves sprint performance in male sprinters. Scand J Med Sci Sports. 2001 Apr;11(2):96-102. [PubMed Link Image]
  4. Greenhaff PL, Soderlund K, Ren JM, Hultman E: Energy metabolism in single human muscle fibres during intermittent contraction with occluded circulation. J Physiol. 1993 Jan;460:443-53. [PubMed Link Image]
  5. Greiner A, Esterhammer R, Pilav S, Arnold W, Santner W, Neuhauser B, Fraedrich G, Jaschke WR, Schocke MF: High-energy phosphate metabolism in the calf muscle during moderate isotonic exercise under different degrees of cuff compression: a phosphorus 31 magnetic resonance spectroscopy study. J Vasc Surg. 2005 Aug;42(2):259-67. [PubMed Link Image]
  6. Murphy AJ, Watsford ML, Coutts AJ, Richards DA: Effects of creatine supplementation on aerobic power and cardiovascular structure and function. J Sci Med Sport. 2005 Sep;8(3):305-13. [PubMed Link Image]
  7. Braegger CP, Schlattner U, Wallimann T, Utiger A, Frank F, Schaefer B, Heizmann CW, Sennhauser FH: Effects of creatine supplementation in cystic fibrosis: results of a pilot study. J Cyst Fibros. 2003 Dec;2(4):177-82. [PubMed Link Image]
  8. Kemp GJ, Hands LJ, Ramaswami G, Taylor DJ, Nicolaides A, Amato A, Radda GK: Calf muscle mitochondrial and glycogenolytic ATP synthesis in patients with claudication due to peripheral vascular disease analysed using 31P magnetic resonance spectroscopy. Clin Sci (Lond). 1995 Dec;89(6):581-90. [PubMed Link Image]
  9. Taylor DJ, Thompson CH, Kemp GJ, Barnes PR, Sanderson AL, Radda GK, Phillips DI: A relationship between impaired fetal growth and reduced muscle glycolysis revealed by 31P magnetic resonance spectroscopy. Diabetologia. 1995 Oct;38(10):1205-12. [PubMed Link Image]
  10. Schmidt A, Marescau B, Boehm EA, Renema WK, Peco R, Das A, Steinfeld R, Chan S, Wallis J, Davidoff M, Ullrich K, Waldschutz R, Heerschap A, De Deyn PP, Neubauer S, Isbrandt D: Severely altered guanidino compound levels, disturbed body weight homeostasis and impaired fertility in a mouse model of guanidinoacetate N-methyltransferase (GAMT) deficiency. Hum Mol Genet. 2004 May 1;13(9):905-21. Epub 2004 Mar 17. [PubMed Link Image]
  11. Ferguson RA, Ball D, Krustrup P, Aagaard P, Kjaer M, Sargeant AJ, Hellsten Y, Bangsbo J: Muscle oxygen uptake and energy turnover during dynamic exercise at different contraction frequencies in humans. J Physiol. 2001 Oct 1;536(Pt 1):261-71. [PubMed Link Image]
  12. Ferguson RA, Krustrup P, Kjaer M, Mohr M, Ball D, Bangsbo J: Effect of temperature on skeletal muscle energy turnover during dynamic knee-extensor exercise in humans. J Appl Physiol. 2006 Jul;101(1):47-52. Epub 2006 Mar 2. [PubMed Link Image]
  13. Duffield R, Dawson B, Goodman C: Energy system contribution to 1500- and 3000-metre track running. J Sports Sci. 2005 Oct;23(10):993-1002. [PubMed Link Image]
  14. Hargreaves M: Skeletal muscle metabolism during exercise in humans. Clin Exp Pharmacol Physiol. 2000 Mar;27(3):225-8. [PubMed Link Image]
  15. Crowther GJ, Kemper WF, Carey MF, Conley KE: Control of glycolysis in contracting skeletal muscle. II. Turning it off. Am J Physiol Endocrinol Metab. 2002 Jan;282(1):E74-9. [PubMed Link Image]
  16. Preen D, Dawson B, Goodman C, Beilby J, Ching S: Creatine supplementation: a comparison of loading and maintenance protocols on creatine uptake by human skeletal muscle. Int J Sport Nutr Exerc Metab. 2003 Mar;13(1):97-111. [PubMed Link Image]
  17. Raymer GH, Marsh GD, Kowalchuk JM, Thompson RT: Metabolic effects of induced alkalosis during progressive forearm exercise to fatigue. J Appl Physiol. 2004 Jun;96(6):2050-6. Epub 2004 Feb 6. [PubMed Link Image]
  18. Krustrup P, Mohr M, Amstrup T, Rysgaard T, Johansen J, Steensberg A, Pedersen PK, Bangsbo J: The yo-yo intermittent recovery test: physiological response, reliability, and validity. Med Sci Sports Exerc. 2003 Apr;35(4):697-705. [PubMed Link Image]
  19. Gideon P, Henriksen O, Sperling B, Christiansen P, Olsen TS, Jorgensen HS, Arlien-Soborg P: Early time course of N-acetylaspartate, creatine and phosphocreatine, and compounds containing choline in the brain after acute stroke. A proton magnetic resonance spectroscopy study. Stroke. 1992 Nov;23(11):1566-72. [PubMed Link Image]
  20. Iyo M, Sekine Y, Mori N: Neuromechanism of developing methamphetamine psychosis: a neuroimaging study. Ann N Y Acad Sci. 2004 Oct;1025:288-95. [PubMed Link Image]
  21. Wikipedia Link Image
Metabolic Enzymes
  1. Creatine kinase, sarcomeric mitochondrial precursor
  2. Creatine kinase B-type
  3. Creatine kinase, ubiquitous mitochondrial precursor
  4. Creatine kinase M-type
  5. cDNA FLJ78469, highly similar to Homo sapiens creatine kinase, brain
Enzyme 1 [top]
Enzyme 1 ID 5993
Enzyme 1 Name Creatine kinase, sarcomeric mitochondrial precursor
Enzyme 1 Synonyms
  1. S- MtCK
  2. Mib-CK
  3. Basic-type mitochondrial creatine kinase
Enzyme 1 Gene Name CKMT2
Enzyme 1 Protein Sequence >Creatine kinase, sarcomeric mitochondrial precursor 
MASIFSKLLTGRNASLLFATMGTSVLTTGYLLNRQKVCAEVREQPRLFPPSADYPDLRKH
NNCMAECLTPAIYAKLRNKVTPNGYTLDQCIQTGVDNPGHPFIKTVGMVAGDEESYEVFA
DLFDPVIKLRHNGYDPRVMKHTTDLDASKITQGQFDEHYVLSSRVRTGRSIRGLSLPPAC
TRAERREVENVAITALEGLKGDLAGRYYKLSEMTEQDQQRLIDDHFLFDKPVSPLLTCAG
MARDWPDARGIWHNYDKTFLIWINEEDHTRVISMEKGGNMKRVFERFCRGLKEVERLIQE
RGWEFMWNERLGYILTCPSNLGTGLRAGVHVRIPKLSKDPRFSKILENLRLQKRGTGGVD
TAAVADVYDISNIDRIGRSEVELVQIVIDGVNYLVDCEKKLERGQDIKVPPPLPQFGKK
Enzyme 1 Number of Residues 419
Enzyme 1 Molecular Weight 47505
Enzyme 1 Theoretical pI 8.31
Enzyme 1 GO Classification
Function
  • catalytic activity
  • kinase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
—
Component
—
Enzyme 1 General Function Not Available
Enzyme 1 Specific Function Reversibly catalyzes the transfer of phosphate between ATP and various phosphogens (e.g. creatine phosphate). Creatine kinase isoenzymes play a central role in energy transduction in tissues with large, fluctuating energy demands, such as skeletal muscle, heart, brain and spermatozoa
Enzyme 1 Pathways
Enzyme 1 Reactions
  • ATP + creatine = ADP + phosphocreatine
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • 1-27
Enzyme 1 Transmembrane Regions Not Available
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 338237 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P17540 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name KCRS_HUMAN Link Image
Enzyme 1 PDB ID 1CRK Link Image
Enzyme 1 PDB File Show
Enzyme 1 3D Structure
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >1260 bp 
ATGGCCAGTATCTTTTCTAAGTTGCTAACTGGCCGCAATGCTTCTCTGCTGTTTGCTACC
ATGGGCACCAGTGTCCTGACCACCGGGTACCTGCTGAACCGGCAGAAAGTGTGTGCCGAG
GTCCGGGAGCAGCCTAGGCTATTTCCTCCAAGCGCAGACTACCCAGACCTGCGCAAGCAC
AACAACTGCATGGCCGAGTGCCTCACCCCCGCCATTTATTCCAAGCTTCGCAACAAGGTG
ACACCCAACGGCTACACGCTGGACCAGTGCATCCAGACTGGAGTGGACAACCCTGGCCAC
CCCTTCATAAAGACTGTGGGCATGGTGGCTGGTGACGAGGAGTCCTATGAGGTGTTTGCT
GACCTTTTTGACCCCGTCATCAAACTAAGACACAACGGCTATGACCCCAGGGTGATGAAG
CACACAACGGATCTGGATGCATCAAAGATCACCCAAGGGCAGTTCGACGAGCATTACGTG
CTGTCTTCTCGGGTGCGCACTGGCCGCAGCATCCGTGGGCTGAGCCTGCCTCCAGCCTGC
ACCCGGGCCGAGCGAAGGGAGGTAGAGAACGTGGCCATCACTGCCCTGGAGGGCCTCAAG
GGGGACCTGGCTGGCCGCTACTACAAGCTGTCCGAGATGACGGAGCAGGACCAGCAGCGG
CTCATCGATGACCACTTTCTGTTTGATAAGCCAGTGTCCCCTTTATTAACATGTGCTGGG
ATGGCCCGTGACTGGCCAGATGCCAGGGGAATCTGGCATAATTATGATAAGACATTTCTC
ATCTGGATAAATGAGGAGGATCACACCAGGGTAATCTCAATGGAAAAAGGAGGCAATATG
AAACGAGTATTTGAGCGATTCTGTCGTGGACTAAAAGAAGTAGAACGGTTAATCCAAGAA
CGAGGCTGGGAGTTCATGTGGAATGAGCGCCTAGGATACATTTTGACCTGTCCTTCGAAC
CTTGGAACAGGACTACGAGCTGGTGTCCACGTTAGGATCCCAAAGCTCAGCAAGGACCCA
CGCTTTTCTAAGATCCTGGAAAACCTAAGACTCCAGAAGCGTGGCACAGGTGGTGTGGAC
ACTGCCGCGGTCGCAGATGTGTACGACATTTCCAACATAGATAGAATTGGTCGATCAGAG
GTTGAGCTTGTTCAGATAGTCATCGATGGAGTCAATTACCTGGTGGATTGTGAAAAGAAG
TTGGAGAGAGGCCAAGATATTAAGGTGCCACCCCCTCTGCCTCAGTTTGGCAAAAAGTAA
Enzyme 1 GenBank Gene ID J05401 Link Image
Enzyme 1 GeneCard ID CKMT2 Link Image
Enzyme 1 GenAtlas ID CKMT2 Link Image
Enzyme 1 HGNC ID HGNC:1996 Link Image
Enzyme 1 Chromosome Location 5
Enzyme 1 Locus 5q13.3
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Haas RC, Strauss AW: Separate nuclear genes encode sarcomere-specific and ubiquitous human mitochondrial creatine kinase isoenzymes. J Biol Chem. 1990 Apr 25;265(12):6921-7. [PubMed Link Image]
  2. Haas RC, Korenfeld C, Zhang ZF, Perryman B, Roman D, Strauss AW: Isolation and characterization of the gene and cDNA encoding human mitochondrial creatine kinase. J Biol Chem. 1989 Feb 15;264(5):2890-7. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5994
Enzyme 2 Name Creatine kinase B-type
Enzyme 2 Synonyms
  1. Creatine kinase B chain
  2. B-CK
Enzyme 2 Gene Name CKB
Enzyme 2 Protein Sequence >Creatine kinase B-type 
MPFSNSHNALKLRFPAEDEFPDLSAHNNHMAKVLTPELYAELRAKSTPSGFTLDDVIQTG
VDNPGHPYIMTVGCVAGDEESYEVFKDLFDPIIEDRHGGYKPSDEHKTDLNPDNLQGGDD
LDPNYVLSSRVRTGRSIRGFCLPPHCSRGERRAIEKLAVEALSSLDGDLAGRYYALKSMT
EAEQQQLIDDHFLFDKPVSPLLLASGMARDWPDARGIWHNDNKTFLVWVNEEDHLRVISM
QKGGNMKEVFTRFCTGLTQIETLFKSKDYEFMWNPHLGYILTCPSNLGTGLRAGVHIKLP
NLGKHEKFSEVLKRLRLQKRGTGGVDTAAVGGVFDVSNADRLGFSEVELVQMVVDGVKLL
IEMEQRLEQGQAIDDLMPAQK
Enzyme 2 Number of Residues 381
Enzyme 2 Molecular Weight 42645
Enzyme 2 Theoretical pI 5.30
Enzyme 2 GO Classification
Function
  • catalytic activity
  • kinase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
—
Component
—
Enzyme 2 General Function Not Available
Enzyme 2 Specific Function Reversibly catalyzes the transfer of phosphate between ATP and various phosphogens (e.g. creatine phosphate). Creatine kinase isoenzymes play a central role in energy transduction in tissues with large, fluctuating energy demands, such as skeletal muscle, heart, brain and spermatozoa
Enzyme 2 Pathways
Enzyme 2 Reactions
  • ATP + creatine = ADP + phosphocreatine
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 180572 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID P12277 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name KCRB_HUMAN Link Image
Enzyme 2 PDB ID 1G0W Link Image
Enzyme 2 PDB File Show
Enzyme 2 3D Structure
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >1146 bp 
ATGCCCTTCTCCAACAGCCACAACGCACTGAAGCTGCGCTTCCCGGCCGAGGACGAGTTC
CCCGACCTGAGCGCCCACAACAACCACATGGCCAAGGTGCTGACCCCCGAGCTGTACGCG
GACGTGCGCGCCAAGAGCACGCCGAGCGGCTTCACGCTGGACGACGTCATCCAGACAGGC
GTGGACAACCCGGGCCACCCGTACATCATGACCGTGGGCTGCGTGGCGGGCGACGAGGAG
TCCTACGAAGTGTTCAAGGATCTCTTCGACCCCATCATCGAGGACCGGCACCGGCGCTAC
AAGCCCAGCGATGACGACAAGACCGACCTCAACCCCGACAACCTGCAGGGCGGCGACGAC
CTGGACCCCAACTACGTGCTGAGCTCGCGGGTGGCCACGGGCCGCAGCATCCGTGGCTTC
TGCCTCCCCCCGCACTGCAGCCGCGGGGAGCGCCGAGCCATCGAGAAGCTCGCGGTGGAA
GCCCTGTCCAGCCTGGACGGCGACCTGGCGGGCCGATACTACGCGCTCAAGAGCATGACG
GAGGCGGAGCAGCAGCAGCTCATCGACGACCACTTCCTCTTCGACAAGCCCGTGTCGCCC
CTGCTGCTGGCCTCGGGCATGGCCCGCGACTGGCCCGACGCCGCGCGTATCTGGCACAAT
GACAATAAGACCTTCCTGGTGTGGGTCAACGAGGAGGACCACCTGCGGGTCATCTCCATG
CAGAAGGGGGGCAACATGAAGGAGGTGTTCACCCGCTTCTGCACCGGCCTCACCCAGATT
GAAACTCTCTTCAAGTCTAAGGACTATGAGTTCATGTGGAACCCTCACCTGGGCTACATC
CTCACCTGCCCATCCAACCTGGGCACCGGGCTGCGGGCAGGTGTCGATATCAAGCTGCCC
AACCTGGGCAAGCATGAGAAGTTCTCGGAGGTGCTTAAGCGGCTGCGACTTCAGAAGCGA
GGCACAGGCGGTGTGGACACGGCTGCGGTGGGCGGGGTCTTCGACGTCTCCAACGCTGAC
CGCCTGGGCTTCTCAGAGGTGGAGCTGGTGCAGATGGTGGTGGACGGAGTGAAGCTGCTC
ATCGAGATGGAACAGCGGCTGGAGCAGGGCCAGGCCATCGACGACCTCATGCCTGCCCAG
AAATGA
Enzyme 2 GenBank Gene ID M16451 Link Image
Enzyme 2 GeneCard ID CKB Link Image
Enzyme 2 GenAtlas ID CKB Link Image
Enzyme 2 HGNC ID HGNC:1991 Link Image
Enzyme 2 Chromosome Location 14
Enzyme 2 Locus 14q32
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Villarreal-Levy G, Ma TS, Kerner SA, Roberts R, Perryman MB: Human creatine kinase: isolation and sequence analysis of cDNA clones for the B subunit, development of subunit specific probes and determination of gene copy number. Biochem Biophys Res Commun. 1987 May 14;144(3):1116-27. [PubMed Link Image]
  2. Mariman EC, Broers CA, Claesen CA, Tesser GI, Wieringa B: Structure and expression of the human creatine kinase B gene. Genomics. 1987 Oct;1(2):126-37. [PubMed Link Image]
  3. Kaye FJ, McBride OW, Battey JF, Gazdar AF, Sausville EA: Human creatine kinase-B complementary DNA. Nucleotide sequence, gene expression in lung cancer, and chromosomal assignment to two distinct loci. J Clin Invest. 1987 May;79(5):1412-20. [PubMed Link Image]
  4. Mariman EC, Schepens JT, Wieringa B: Complete nucleotide sequence of the human creatine kinase B gene. Nucleic Acids Res. 1989 Aug 11;17(15):6385. [PubMed Link Image]
  5. Daouk GH, Kaddurah-Daouk R, Putney S, Kingston R, Schimmel P: Isolation of a functional human gene for brain creatine kinase. J Biol Chem. 1988 Feb 15;263(5):2442-6. [PubMed Link Image]
  6. Lin L, Perryman MB, Friedman D, Roberts R, Ma TS: Determination of the catalytic site of creatine kinase by site-directed mutagenesis. Biochim Biophys Acta. 1994 May 18;1206(1):97-104. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 5995
Enzyme 3 Name Creatine kinase, ubiquitous mitochondrial precursor
Enzyme 3 Synonyms
  1. U- MtCK
  2. Mia-CK
  3. Acidic-type mitochondrial creatine kinase
Enzyme 3 Gene Name CKMT1A
Enzyme 3 Protein Sequence >Creatine kinase, ubiquitous mitochondrial precursor 
MAGPFSRLLSARPGLRLLALAGAGSLAAGFLLRPEPVRAASERRRLYPPSAEYPDLRKHN
NCMASHLTPAVYARLCDKTTPTGWTLDQCIQTGVDNPGHPFIKTVGMVAGDEETYEVFAD
LFDPVIQERHNGYDPRTMKHTTDLDASKIRSGYFDERYVLSSRVRTGRSIRGLSLPPACT
RAERREVERVVVDALSGLKGDLAGRYYRLSEMTEAEQQQLIDDHFLFDKPVSPLLTAAGM
ARDWPDARGIWHNNEKSFLIWVNEEDHTRVISMEKGGNMKRVFERFCRGLKEVERLIQER
GWEFMWNERLGYILTCPSNLGTGLRAGVHIKLPLLSKDSRFPKILENLRLQKRGTGGVDT
AATGGVFDISNLDRLGKSEVELVQLVIDGVNYLIDCERRLERGQDIRIPTPVIHTKH
Enzyme 3 Number of Residues 417
Enzyme 3 Molecular Weight 47037
Enzyme 3 Theoretical pI 8.47
Enzyme 3 GO Classification
Function
  • catalytic activity
  • kinase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
—
Component
—
Enzyme 3 General Function Not Available
Enzyme 3 Specific Function Reversibly catalyzes the transfer of phosphate between ATP and various phosphogens (e.g. creatine phosphate). Creatine kinase isoenzymes play a central role in energy transduction in tissues with large, fluctuating energy demands, such as skeletal muscle, heart, brain and spermatozoa
Enzyme 3 Pathways
Enzyme 3 Reactions
  • ATP + creatine = ADP + phosphocreatine
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • 1-29
Enzyme 3 Transmembrane Regions Not Available
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 180590 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID P12532 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name KCRU_HUMAN Link Image
Enzyme 3 PDB ID 1QK1 Link Image
Enzyme 3 PDB File Show
Enzyme 3 3D Structure
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >1254 bp 
ATGGCTGGTCCCTTCTCCCGTCTGCTGTCCGCCCGCCCGGGACTCAGGCTCCTGGCTTTG
GCCGGAGCGGGGTCTCTAGCCGCTGGGTTTCTGCTCCGACCGGAACCTGTACGAGCTGCC
AGTGAACGACGGAGGCTGTATCCCCCGAGCGCTGAGTACCCAGACCTCCGAAAGCACAAC
AACTGCATGGCCAGTCACCTGACCCCAGCAGTCTATGCACGGCTCTGCGACAAGACCACA
CCCACTGGTTGGACGCTAGATCAGTGTATCCAGACTGGCGTGGACAACCCTGGCCACCCC
TTCATCAAGACTGTGGGCATGGTGGCTGGAGATGAGGAGACCTATGAGGTATTTGCTGAC
CTGTTTGACCCTGTGATCCAAGAGCGACACAATGGATATGACCCCCGGACAATGAAGCAC
ACCACGGATCTAGATGCCAGTAAAATCCGTTCTGGCTACTTTGATGAGAGGTATGTATTG
TCCTCTAGAGTCAGAACTGGCCGAAGCATCCGAGGACTCAGTCTGCCTCCAGCTTGCACT
CGAGCAGAGCGACGAGAGGTGGAACGTGTTGTGGTGGATGCACTGAGTGGCCTGAAGGGT
GACCTGGCTGGACGTTACTATAGGCTCAGTGAGATGACAGAGGCTGAACAGCAGCAGCTT
ATTGATGACCACTTTCTGTTTGATAAGCCTGTGTCCCCGTTGCTGACTGCAGCAGGAATG
GCTCGAGACTGGCCAGATGCTCGTGGAATTTGGCACAACAATGAGAAGAGCTTCCTGATC
TGGGTGAATGAGGAGGATCATACACGGGTGATCTCCATGGAGAAGGGTGGTAACATGAAG
AGAGTGTTTGAAAGATTCTGCCGAGGCCTCAAAGAGGTGGAGAGACTTATCCAAGAACGT
GGCTGGGAGTTCATGTGGAATGAGCGTTTGGGATACATCTTGACCTGTCCATCTAACCTG
GGCACTGGACTTCGGGCAGGAGTGCACATCAAACTGCCCCTGCTAAGCAAAGATAGCCGC
TTCCCAAAGATCCTGGAGAACCTAAGACTCCAAAAACGTGGTACTGGAGGAGTGGACACT
GCTGCTACAGGCGGTGTCTTTGATATTTCTAATTTGGACCGACTAGGCAAATCAGAGGTG
GAGCTGGTGCAACTGGTCATCGATGGAGTAAACTATTTGATTGATTGTGAACGGCGTCTG
GAGAGAGGCCAGGATATCCGCATCCCCACACCTGTCATCCACACCAAGCATTAA
Enzyme 3 GenBank Gene ID J04469 Link Image
Enzyme 3 GeneCard ID CKMT1A Link Image
Enzyme 3 GenAtlas ID CKMT1A Link Image
Enzyme 3 HGNC ID HGNC:31736 Link Image
Enzyme 3 Chromosome Location 15
Enzyme 3 Locus 15q15
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Haas RC, Korenfeld C, Zhang ZF, Perryman B, Roman D, Strauss AW: Isolation and characterization of the gene and cDNA encoding human mitochondrial creatine kinase. J Biol Chem. 1989 Feb 15;264(5):2890-7. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 5996
Enzyme 4 Name Creatine kinase M-type
Enzyme 4 Synonyms
  1. Creatine kinase M chain
  2. M-CK
Enzyme 4 Gene Name CKM
Enzyme 4 Protein Sequence >Creatine kinase M-type 
MPFGNTHNKFKLNYKPEEEYPDLSKHNNHMAKVLTLELYKKLRDKETPSGFTVDDVIQTG
VDNPGHPFIMTVGCVAGDEESYEVFKELFDPIISDRHGGYKPTDKHKTDLNHENLKGGDD
LDPNYVLSSRVRTGRSIKGYTLPPHCSRGERRAVEKLSVEALNSLTGEFKGKYYPLKSMT
EKEQQQLIDDHFLFDKPVSPLLLASGMARDWPDARGIWHNDNKSFLVWVNEEDHLRVISM
EKGGNMKEVFRRFCVGLQKIEEIFKKAGHPFMWNQHLGYVLTCPSNLGTGLRGGVHVKLA
HLSKHPKFEEILTRLRLQKRGTGGVDTAAVGSVFDVSNADRLGSSEVEQVQLVVDGVKLM
VEMEKKLEKGQSIDDMIPAQK
Enzyme 4 Number of Residues 381
Enzyme 4 Molecular Weight 43102
Enzyme 4 Theoretical pI 7.28
Enzyme 4 GO Classification
Function
  • catalytic activity
  • kinase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
—
Component
—
Enzyme 4 General Function Not Available
Enzyme 4 Specific Function Reversibly catalyzes the transfer of phosphate between ATP and various phosphogens (e.g. creatine phosphate). Creatine kinase isoenzymes play a central role in energy transduction in tissues with large, fluctuating energy demands, such as skeletal muscle, heart, brain and spermatozoa
Enzyme 4 Pathways
Enzyme 4 Reactions
  • ATP + creatine = ADP + phosphocreatine
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 180576 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID P06732 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name KCRM_HUMAN Link Image
Enzyme 4 PDB ID 1I0E Link Image
Enzyme 4 PDB File Show
Enzyme 4 3D Structure
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >1146 bp 
ATGCCATTCGGTAACACCCACAACAAGTTCAAGCTGAATTACAAGCCTGAGGAGGAGTAC
CCCGACCTCAGCAAACATAACAACCACATGGCCAAGGTACTGACCCTTGAACTCTACAAG
AAGCTGCGGGACAAGGAGATCCCATCTGGCTTCACTGTAGACGATGTCATCCAGACAGGA
GTGGACAACCCAGGTCACCCCTTCATCATGACCGTGGGCTGCGTGGCTGGTGATGAGGAG
TCCTACGAAGTTTTCAAGGAACTCTTTGACCCCATCATCTCGGATCGCCACGGGGGCTAC
AAACCCACTGACAAGCACAAGACTGACCTCAACCATGAAAACCTCAAGGGTGGAGACGAC
CTGGACCCCAACTACGTGCTCAGCAGCCCGGTCCGCACTGGCCGCAGCATCAAGGGCTAC
ACGTTGCCCCCACACTGCTCCCGTGGCGAGCGCCGGGCGGTGGAGAAGCTCTCTGTGGAA
GCTCTCAACAGCCTGACGGGCGAGTTCAAAGGGAAGTACTACCCTCTGAAGAGCATGACG
GAGAAGGAGCAGCAGCAGCTCATCGATGACCACTTCCAGTTCGACAAGCCCGTGTCCCCG
CTGCTGCTGGCCTCAGGCATGGCCCGCCACTGGCCCGACGCCCCTGGCATCTGGCACAAT
GACAACAAGAGCTTCCTGGTGTGGGTGAACGAGGAGGATCACCTCCGGGTCATCTCCATG
GAGAAGGGGGGCAACATGAAGGAGGTTTTCCGCCGCTTCTGCGTAGGGCTGCAGAAGATT
GAGGAGATCTTTAAGAAAGCTGGCCACCCCTTCATGTGGAACCAGCACCTGGGCTACGTG
CTCACCTGCCCATCCAACCTGGGCACTGGGCTGCGTGGAGGCGTGCATGTGAAGCTGGCG
CACCTGAGCAAGCACCCCAAGTTCGAGGAGATCCTCACCCGCCTGCGTCTGCAGAAGAGG
GGTACAGGTGCGGTGGACACAGCTGCCGTGGGCTCAGTATTTGACGTGTCCAACGCTGAT
CGGCTGGGCTCGTCCGAAGTAGAACAGGTGCAGCTGGTGGTGGATGGTGTGAAGCTCATG
GTGGAAATGGAGAAGAAGTTGGAGAAAGGCCAGTCCATCGACGACATGATCCCCGCCCAG
AAGTAG
Enzyme 4 GenBank Gene ID M14780 Link Image
Enzyme 4 GeneCard ID CKM Link Image
Enzyme 4 GenAtlas ID CKM Link Image
Enzyme 4 HGNC ID HGNC:1994 Link Image
Enzyme 4 Chromosome Location 19
Enzyme 4 Locus 19q13.2-q13.3
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Perryman MB, Kerner SA, Bohlmeyer TJ, Roberts R: Isolation and sequence analysis of a full-length cDNA for human M creatine kinase. Biochem Biophys Res Commun. 1986 Nov 14;140(3):981-9. [PubMed Link Image]
  2. Trask RV, Strauss AW, Billadello JJ: Developmental regulation and tissue-specific expression of the human muscle creatine kinase gene. J Biol Chem. 1988 Nov 15;263(32):17142-9. [PubMed Link Image]
  3. Nigro JM, Schweinfest CW, Rajkovic A, Pavlovic J, Jamal S, Dottin RP, Hart JT, Kamarck ME, Rae PM, Carty MD, et al.: cDNA cloning and mapping of the human creatine kinase M gene to 19q13. Am J Hum Genet. 1987 Feb;40(2):115-25. [PubMed Link Image]
  4. Hamburg RJ, Friedman DL, Olson EN, Ma TS, Cortez MD, Goodman C, Puleo PR, Perryman MB: Muscle creatine kinase isoenzyme expression in adult human brain. J Biol Chem. 1990 Apr 15;265(11):6403-9. [PubMed Link Image]
  5. Tang L, Zhou HM, Lin ZJ: Crystallization and preliminary X-ray analysis of human muscle creatine kinase. Acta Crystallogr D Biol Crystallogr. 1999 Mar;55(Pt 3):669-70. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 12998
Enzyme 5 Name cDNA FLJ78469, highly similar to Homo sapiens creatine kinase, brain
Enzyme 5 Synonyms
  1. CKB, mRNA
  2. Creatine kinase, brain, isoform CRA_c
Enzyme 5 Gene Name CKB
Enzyme 5 Protein Sequence >cDNA FLJ78469, highly similar to Homo sapiens creatine kinase, brain 
MPFSNSHNALKLRFPAEDEFPDLSAHNNHMAKVLTPELYAELRAKSTPSGFTLDDVIQTG
VDNPGHPYIMTVGCVAGDEESYEVFKDLFDPIIEDRHGGYKPSDEHKTDLNPDNLQGGDD
LDPNYVLSSRVRTGRSIRGFCLPPHCSRGERRAIEKLAVEALSSLDGDLAGRYYALKSMT
EAEQQQLIDDHFLFDKPVSPLLLASGMARDWPDARGIWHNDNKTFLVWVNEEDHLRVISM
QKGGNMKEVFTRFCTGLTQIETLFKSKDYEFMWNPHLGYILTCPSNLGTGLRAGVHIKLP
NLGKHEKFSEVLKRLRLQKRGTGGVDTAAVGGVFDVSNADRLGFSEVELVQMVVDGVKLL
IEMEQRLEQGQAIDDLMPAQK
Enzyme 5 Number of Residues 381
Enzyme 5 Molecular Weight 42645
Enzyme 5 Theoretical pI 5.30
Enzyme 5 GO Classification Not Available
Enzyme 5 General Function Not Available
Enzyme 5 Specific Function Not Available
Enzyme 5 Pathways Not Available
Enzyme 5 Reactions Not Available
Enzyme 5 Pfam Domain Function Not Available
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 158261225 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID A8K236 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name A8K236_HUMAN Link Image
Enzyme 5 PDB ID 1G0W Link Image
Enzyme 5 PDB File Show
Enzyme 5 3D Structure
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence Not Available
Enzyme 5 GenBank Gene ID AK290101 Link Image
Enzyme 5 GeneCard ID A8K236 Link Image
Enzyme 5 GenAtlas ID Not Available
Enzyme 5 HGNC ID Not Available
Enzyme 5 Chromosome Location Not Available
Enzyme 5 Locus Not Available
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References Not Available
Enzyme 5 Metabolite References Not Available