.

Carnitine palmitoyltransferase I (CPT I) is localized to the outer mitochondrial membrane and catalyzes the esterification reaction between carnitine and palmitoyl-CoA to produce palmitoylcarnitine.  Three tissue-specific isoforms (liver, muscle, brain) have been identified.
Carnitine-acylcarnitine translocase (CACT) is an integral inner mitochondrial membrane protein that transports palmitoylcarnitine from the intermembrane space into the matrix in exchange for a molecule of free carnitine that is subsequently moved back out of the mitochondria into the cytosol.
Carnitine palmitoyltransferase II (CPT II) is a peripheral inner mitochondrial membrane protein ubiquitously found as a monomeric protein in all tissues that oxidize fatty acids. It catalyzes the transesterification of palmitoylcarnitine back into palmitoyl-CoA which is now an activated substrate for β-oxidation inside the matrix.

Molecular genetics

CPT II deficiency has an autosomal recessive pattern of inheritance. 
CPT2 is the gene that encodes the CPT II enzyme, and it has been mapped to chromosomal locus 1p32.  This gene is composed of 5 exons that encode a protein 658 amino acids in length.  To date, sixty disease-causing mutations within the coding sequence of CPT2 have been reported in the literature, of which 41 are thought to result in amino acid substitutions or deletions at critical residues.

Amino acid consequences of some reported mutations
Ser113Leu (338C>T) is the most common mild mutation observed in adult cases, it has an observed allelic frequency of 65% in adult cases, and both homozygous and heterozygous cases have been documented.
Pro50His (149C>A) is also relatively common in the adult form, with an allelic frequency of 6.5%.
Arg161Trp, Glu174Lys and Ile502Thr are other homozygous mild mutations associated with the adult form 
Arg151Gln and Pro227Leu are examples of severe homozygous mutations that have been associated with the mutisystemic infantile/neonatal form of the disorder.
The 18 known severe mutations that result in prematurely truncated proteins lack residual CPT II activity are associated with the neonatal onset and are likely incompatible with life in most circumstances.
Val368Ile and Met647Val
. 

 Carnitine palmitoyltransferase I (CPT I) is localized to the outer mitochondrial membrane and catalyzes the esterification reaction between carnitine and palmitoyl - CoA to grow palmitoylcarnitine.   Three tissue - specific isoforms (liver, muscleman, brain) have been identified. 
 Carnitine - acylcarnitine translocase (CACT) is an integral inside mitochondrial membrane protein that transports palmitoylcarnitine from the intermembrane space into the matrix in exchange for a atom of barren carnitine that is subsequently moved back out of the mitochondrion into the cytosol. 
 Carnitine palmitoyltransferase II (CPT II) is a peripheral inside mitochondrial membrane protein ubiquitously found as a monomeric protein in all tissues that oxidise fatty acids. It catalyze the transesterification of palmitoylcarnitine back into palmitoyl - CoA which is now an activated substrate for β - oxidation inside the matrix. 

 Molecular genetics 

 CPT II deficiency has an autosomal recessive pattern of inheritance. 
 CPT2 is the gene that encodes the CPT II enzyme, and it has been map to chromosomal locus 1p32.   This gene is composed of 5 exons that encode a protein 658 amino acid in length.   To date, sixty disease - causing mutations within the coding succession of CPT2 have been reported in the literature, of which 41 are remember to result in amino acid substitutions or deletions at critical residue. 

 Amino acid consequences of some reported mutations 
 Ser113Leu (338C > T) is the most common mild mutation observed in adult cases, it has an observed allelic frequency of 65% in adult cases, and both homozygous and heterozygous cases have been documented. 
 Pro50His (149C > A) is also relatively common in the adult kind, with an allelic frequency of 6.5% . 
 Arg161Trp, Glu174Lys and Ile502Thr are other homozygous mild mutation associated with the adult form 
 Arg151Gln and Pro227Leu are examples of severe homozygous mutation that have been associated with the mutisystemic infantile / neonatal form of the disorder. 
 The 18 know severe mutations that result in prematurely truncated proteins lack residual CPT II bodily process are associated with the neonatal onset and are likely incompatible with biography in most circumstances. 
 Val368Ile and Met647Val
.

Carjitine palmitoyltransferxse I (CPT I) is localizxd to tge outer mitochondrial membrane and rataoyzes the esterification rexction benween carbitiie and palmitoyl-RkA to pvjducs palkmtoylcarnitine.  Three tisvue-specific ismfurls (liver, muscle, brain) have been idegtified.
Vagnitine-acylcargitimq trznslocase (CACT) is an integral inned mitociondrial membrame protein that transports pallitoylcarnitine frlm the intetjemfeane space ivto the maurnx in exchahge for a molecule of free carnktine that is soyweqkgntly moved uack olt of the mitochondrid into yhe cytosol.
Carkitinx paomitoyltransferase II (CPT II) is a peripreral innar mitochondrial menbeane krotehn ucuquktohsky found as a monomerjc protein un all tissues that ovpcize fatty adids. Ie satalyzes the transesterification of panmifoylcarnitine back into palmitoyl-CoA which id now an wctivated substrate for β-oxidation inside the matrhx.

Molxcjlax genegucd

CPT II deficiency has an autosomal recessive lautegn of inheritance. 
CPT2 is the gfnr that encodes the C'F JI enzyme, and it hws been mappwd to chrjmospmal locus 1p32.  This gene is xomposed of 5 wxons that encode c protein 658 aoino acidx in length.  To date, sirty diaease-causinh mutatiohr within the codkng saquence of CPT2 have been rqported ii the literagure, of whych 41 are tjoughb to result in aminl acib subvtitutions or deletions at critical residnxs.

Amino acid votsexuences jf soke reported mttations
Ser113Leu (338C>T) is che mort common jild muvation obserded in adult wwses, it has en observqd aoleluc freqjdncy of 65% in adilt cases, and both yomozygous and hetcrozyekus cases have yten documented.
Pro50Hos (149Z>A) ys aksj relatively wommun km the adult form, dith an allelic frequencf of 6.5%.
Arg161Trp, Glu174Lys and Ije502Thr arg other hjmozygous milc mutations associwted xith tie adukt sorm 
Arg151Gln and Pro227Leu are exajples of devcre homozygouf mubatijns that hcve been associated with the mutisystemir infantile/neonatal fotm of the disorder.
The 18 known sevece mutwtions thdt result in prematueely truncated prpteins lack residual DPT II actigity are associated with the neonatal onset and are likely incompatible wuth lihe in most cidcumxtancvs.
Vcl368Ike and Met647Tau
. Carnitine palmitoyltransferase I (CPT I) is the mitochondrial membrane catalyzes the esterification to palmitoylcarnitine. Three tissue-specific (liver, muscle, brain) been identified. Carnitine-acylcarnitine translocase (CACT) is integral inner mitochondrial membrane protein that transports palmitoylcarnitine from the intermembrane space into matrix in exchange for a molecule of free carnitine that is subsequently moved out the into cytosol. Carnitine palmitoyltransferase II (CPT II) is a peripheral inner mitochondrial membrane protein ubiquitously found as monomeric protein in all tissues that oxidize fatty It catalyzes the transesterification palmitoylcarnitine back into palmitoyl-CoA which now activated substrate β-oxidation the Molecular genetics CPT deficiency has an autosomal recessive pattern of inheritance. CPT2 is the gene that encodes the CPT II and it mapped to locus This is composed of that encode a protein 658 amino To date, sixty disease-causing mutations within the coding of CPT2 been reported in the literature, of 41 are thought to result in amino acid or deletions at critical residues. Amino acid consequences of some reported mutations Ser113Leu (338C>T) is common mild mutation observed adult cases, it an allelic of in adult and both homozygous and heterozygous cases have been documented. Pro50His (149C>A) also relatively common in the adult form, with an allelic 6.5%. Glu174Lys and Ile502Thr other homozygous mild mutations with adult form Arg151Gln and examples severe have associated the mutisystemic infantile/neonatal form the disorder. The 18 known mutations that result in CPT II activity are associated with the neonatal and are likely incompatible with life in circumstances. Val368Ile and Met647Val
.

Carnitine palmitoyltransfeRase I (CPT I) iS locaLizEd tO tHe ouTer mItochondrial meMBranE and catalyzes the esteriFicatIoN ReacTIoN betwEen carnITiNE And PaLmItoYl-cOA To proDucE palmitOylcarnitiNe.  THrEe tissue-specIFiC isoforms (lIveR, muscle, brain) HavE been iDeNtiFIed.
CaRniTine-aCylcarNItine tRanslocasE (CacT) is an INtegral INNeR mitOchondrial membranE PrOTein that transpOrts paLmIToYLCarNitIne from the InTermeMBrane spACe INTO thE Matrix in exchaNge for a moleCUle Of free CaRniTIne thaT is suBsEQueNtly moved baCk ouT of the mitOchondRIa into tHE cytosoL.
CarniTinE paLmitOYlTrAnsFeRAse ii (CpT Ii) Is a PeripherAl InNer miTochONDRIal mEmbRane ProteIn ubiquitouslY foUnd aS A moNomerIc proTein In All tiSsues tHat oxIdIze fatty acids. It CataLyzes the tRanSeSteRiFicatIOn of paLmiToyLcarnitIne back INto PaLMIToYl-CoA which is now an aCtIVAtEd substrAte for Β-OxIdATion insiDe The MatrIX.

molecUlar GEnEtics

CPT iI defiCIeNcY has an aUtOsomal ReCesSivE pattERn of InheriTance. 
CPT2 Is the GEne that encodes THe CPT II enzyme, ANd IT HaS Been MapPed to chromoSomaL LocuS 1p32.  ThIS gEne IS compOsed oF 5 eXOnS That encode a protein 658 aMiNo acidS in leNgth.  To date, sixTy disease-cAUSIng mutatIons WItHIn the coding seqUence Of CPT2 have bEEn reportEd in tHe literaTure, of whiCH 41 Are thougHt tO reSulT in AMInO acid substituTIOns oR dEletionS at CriticaL reSidUes.

amiNo Acid conseQuences oF sOmE rEpOrtEd mutATions
Ser113leU (338C>T) Is The Most cOMmon miLd mutAtioN oBsERveD in adulT CaSES, it hAs An ObseRveD aLleliC freQUenCy of 65% in aDult cases, And BOth hOmOzYgous anD heterozygous CaSes have beeN dOcuMented.
pRO50His (149C>A) is Also relatively common in tHE adult fOrm, With aN allElic frequEncY of 6.5%.
Arg161trp, gLu174Lys aNd Ile502THr are OtHer HOMozygOUS mIld MuTations assOCIatEd witH tHe adUlt form 
arg151Gln and Pro227Leu are EXamPles of severe hOmoZygoUS MuTatIOnS ThaT hAVe bEEN associated with The mutisysTeMIc Infantile/nEOnaTaL form of The disoRder.
THE 18 known sEvere mutaTions that ReSult IN PreMaturely trUncated pRoteins laCK resiDUaL CPT Ii acTivity ArE asSociaTed witH The NeonaTal onsEt And are LikelY iNcompatiBle with life in most circumStanceS.
Val368ILe aNd Met647Val
.

Carnitine palmitoyltran sferase I(CPTI)islo cali zedto the outer m i toch ondrial membrane and c ataly ze s  the es terif ication re a c tio nbe twe en ca rniti neand pal mitoyl-CoA  to  p roduce palmi t oy lcarnitine . Three tissue -sp ecific  i sof o rms ( liv er, m uscle, brain)  have bee ni dentif i ed.
Car n i ti ne-a cylcarnitine tran s lo c ase (CACT) isan int eg r al i nne r m itochondri al  memb r ane pro t ei n t hat transports pa lmitoylcarn i tin e from  t hei nterme mbran es pac e into thematr ix in exc hangef or a mo l ecule o f free  ca rni tine th at  is  s u bse q ue ntl y  mo ved back  o ut  of t he m i t o c hond ria  int o the  cytosol.
Car nit inep alm itoyl trans fera se  II ( CPT II ) isaperipheral inne r mi tochondri alme mbr an e pro t ein ub iqu ito usly fo und asa  mo no m e r ic  protein in all ti ss u e sthat oxi dize f a tt ya cids. It  c ata lyze s the t rans e st erificat ion of pa lm itoylca rn itineba ckint o pal m itoy l-CoAwhich is  nowa n activated su b strate for β- o xi d a ti o n in sid e the matri x.
M olec ular ge net i cs

C PT II  d e fi c iency has an autoso ma l rece ssive  pattern of i nheritance . CPT2 istheg en e  that encodesthe C PT II enzy m e, and i t has  been ma pped to c h r omosomal  lo cus  1p 32. Th is gene is co m p osed  o f 5 exo nsthat en cod e a  pr ote in  658 amin o acidsin  l en gt h. To d a te, sixt ydis ea se- causi n g muta tions  wit hi nt hecodings eq u e nceof  C PT2hav ebeenrepo r ted  in the  literatu re, of w hi ch  41 are  thought to r es ult in ami no  ac id sub s t itutions  or deletions at critic a l resid ues .

Am inoacid cons equ encesofs ome re ported  muta ti ons S er113 L e u(33 8C >T) is the m ost  comm on  mil d mutat ion observed in ad u ltcases, it has  an  obs e r ve d a l le l icfr e que n c y of 65% in adu lt cases,an d  b oth homozy g ous  a nd hete rozygou s cas e s havebeen docu mented.
P ro 50Hi s (14 9C>A) is a lso rela tively co m mon i n  t he ad ult  form,  w ith  an a llelic fre quenc y of 6 .5 %.
Arg 161Tr p,  Glu174L ys and Ile502Thr are ot her ho mozyg ous  mild mut ati o nsassociate d wi th the adu ltfor m 
Ar g15 1 Gln a nd P r o2 27L e u are  exa m ples of s e ve reh o mo zygous muta t i o nsthathav e  beenasso ciated with the m u tisystemic inf anti l e /ne ona t al f or m of the disor der .T h e 18 kno wn  severe mut ations t ha t  resu lt inpremat urely t r u nc a ted pr otei nslack resi dua lC PT II a ct iv i ty are  ass oc iatedwith t h e ne o n atal onset and a re li k e ly in c omp atibl ewith li f e in  most circ umstances.Val368 Ileand M et647Va l
.

Carnitine palmitoyltransferase_I (CPT_I) is localized to_the outer_mitochondrial_membrane and_catalyzes_the esterification reaction_between carnitine and_palmitoyl-CoA to produce palmitoylcarnitine._ Three tissue-specific_isoforms_(liver, muscle, brain) have been identified.
Carnitine-acylcarnitine translocase (CACT) is an integral inner mitochondrial membrane_protein_that transports_palmitoylcarnitine_from_the intermembrane space into the_matrix in exchange for a_molecule of_free carnitine that is subsequently moved back out_of_the mitochondria into_the cytosol.
Carnitine palmitoyltransferase II (CPT II) is a peripheral_inner mitochondrial membrane protein ubiquitously found_as a monomeric_protein_in_all tissues that oxidize_fatty acids. It catalyzes the transesterification_of palmitoylcarnitine back into palmitoyl-CoA which_is now an activated substrate for β-oxidation_inside the matrix.

Molecular genetics

CPT II deficiency_has an autosomal recessive pattern_of inheritance._
CPT2 is the gene that_encodes the CPT_II enzyme,_and it has_been mapped to chromosomal locus 1p32._ This gene_is composed of 5 exons that_encode_a protein 658_amino_acids_in length._ To date,_sixty_disease-causing mutations_within_the coding sequence of CPT2 have_been_reported in the literature, of which 41_are thought to result_in_amino acid substitutions or_deletions at critical residues.

Amino acid_consequences of some reported mutations
Ser113Leu (338C>T)_is the_most common_mild mutation observed in adult cases, it has an observed allelic_frequency of 65% in adult cases,_and both homozygous and_heterozygous cases_have_been documented.
Pro50His (149C>A)_is_also relatively_common in the adult form, with an_allelic frequency_of 6.5%.
Arg161Trp, Glu174Lys and Ile502Thr are_other homozygous mild mutations_associated_with the adult form 
Arg151Gln and_Pro227Leu are examples of severe homozygous_mutations that have been associated_with_the_mutisystemic infantile/neonatal form of the_disorder.
The 18 known severe mutations that_result in prematurely_truncated proteins lack residual CPT II activity_are_associated with the neonatal onset and_are_likely incompatible with life in most_circumstances.
Val368Ile_and_Met647Val