Phytanic acid oxidation: topographical localization of phytanoyl-CoA ligase and transport of phytanic acid into human peroxisomes.

To understand the possible role of phytanoyl-CoA ligase, present in the membrane, in the oxidation of phytanic acid in the matrix of peroxisomes (Pahan, K. and I. Singh. 1993. FEBS Lett. 333: 154-158) we examined the transport of phytanic acid/phytanoyl-CoA into peroxisomes and the topology of the active site of phytanoyl-CoA ligase in the peroxisomal membrane. The increase in lignoceroyl-CoA ligase as compared to no change in the activities of palmitoyl-CoA and phytanoyl-CoA ligases when peroxisomes were disrupted with detergent or sonication and inhibition of the activities of both palmitoyl-CoA and phytanoyl-CoA ligase by impermeable inhibitor of acyl-CoA ligases (mercury-dextran) and trypsin treatment in the intact peroxisomes. On the other hand, the lignoceroyl-CoA ligase activity was inhibited by mercury-dextran and trypsin only in the disrupted peroxisomes. Taken together, these studies support the conclusion that the enzymatic site of phytanoyl-CoA ligase is on the cytoplasmic surface of peroxisomal membrane. This implies that phytanoyl-CoA is synthesized on the cytoplasmic surface of peroxisomal membrane and is translocated through the membrane for its alpha-oxidation to pristanic acid in the matrix of peroxisomes. To delineate the transport for phytanic acid through the peroxisomal membrane, we examined cofactors and energy requirements for its transport into peroxisomes. The similar rates of transport of phytanoyl-CoA and phytanic acid under conditions favorable for fatty acid activation (presence of ATP, CoASH, and MgCl2) and the lack of transport of phytanic acid when ATP and/or CoASH were removed or replaced with their inactive analogues (ATP and/or CoASH) from assay medium clearly demonstrates that the transport of phytanic acid requires prior synthesis of phytanoyl-CoA by phytanoyl-CoA ligase. The prerequisite activation of phytanic acid to phytanoyl-CoA for its alpha-oxidation only in intact peroxisomes, and oxidation of free phytanic acid in digitonin-permealized peroxisomes or isolated matrix, suggests that phytanoyl-CoA ligase (in peroxisomal membrane) regulates the oxidation of phytanic acid in peroxisomes by providing phytanoyl-CoA for its transport into peroxisomes. Ausführliche Beschreibung

Gespeichert in:

Autor*in:	K Pahan [verfasserIn] I Singh [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	1995

Übergeordnetes Werk:	In: Journal of Lipid Research - Elsevier, 2021, 36(1995), 5, Seite 986-997
Übergeordnetes Werk:	volume:36 ; year:1995 ; number:5 ; pages:986-997

Links:	Link aufrufen Link aufrufen Link aufrufen Journal toc

DOI / URN:	10.1016/S0022-2275(20)39856-4

Katalog-ID:	DOAJ067435483

Internformat


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allfields	10.1016/S0022-2275(20)39856-4 doi (DE-627)DOAJ067435483 (DE-599)DOAJ6e16974eb93e475ab3e39665c2362c21 DE-627 ger DE-627 rakwb eng QD415-436 K Pahan verfasserin aut Phytanic acid oxidation: topographical localization of phytanoyl-CoA ligase and transport of phytanic acid into human peroxisomes. 1995 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier To understand the possible role of phytanoyl-CoA ligase, present in the membrane, in the oxidation of phytanic acid in the matrix of peroxisomes (Pahan, K. and I. Singh. 1993. FEBS Lett. 333: 154-158) we examined the transport of phytanic acid/phytanoyl-CoA into peroxisomes and the topology of the active site of phytanoyl-CoA ligase in the peroxisomal membrane. The increase in lignoceroyl-CoA ligase as compared to no change in the activities of palmitoyl-CoA and phytanoyl-CoA ligases when peroxisomes were disrupted with detergent or sonication and inhibition of the activities of both palmitoyl-CoA and phytanoyl-CoA ligase by impermeable inhibitor of acyl-CoA ligases (mercury-dextran) and trypsin treatment in the intact peroxisomes. On the other hand, the lignoceroyl-CoA ligase activity was inhibited by mercury-dextran and trypsin only in the disrupted peroxisomes. Taken together, these studies support the conclusion that the enzymatic site of phytanoyl-CoA ligase is on the cytoplasmic surface of peroxisomal membrane. This implies that phytanoyl-CoA is synthesized on the cytoplasmic surface of peroxisomal membrane and is translocated through the membrane for its alpha-oxidation to pristanic acid in the matrix of peroxisomes. To delineate the transport for phytanic acid through the peroxisomal membrane, we examined cofactors and energy requirements for its transport into peroxisomes. The similar rates of transport of phytanoyl-CoA and phytanic acid under conditions favorable for fatty acid activation (presence of ATP, CoASH, and MgCl2) and the lack of transport of phytanic acid when ATP and/or CoASH were removed or replaced with their inactive analogues (ATP and/or CoASH) from assay medium clearly demonstrates that the transport of phytanic acid requires prior synthesis of phytanoyl-CoA by phytanoyl-CoA ligase. The prerequisite activation of phytanic acid to phytanoyl-CoA for its alpha-oxidation only in intact peroxisomes, and oxidation of free phytanic acid in digitonin-permealized peroxisomes or isolated matrix, suggests that phytanoyl-CoA ligase (in peroxisomal membrane) regulates the oxidation of phytanic acid in peroxisomes by providing phytanoyl-CoA for its transport into peroxisomes. Biochemistry I Singh verfasserin aut In Journal of Lipid Research Elsevier, 2021 36(1995), 5, Seite 986-997 (DE-627)26601593X (DE-600)1466675-3 15397262 nnns volume:36 year:1995 number:5 pages:986-997 https://doi.org/10.1016/S0022-2275(20)39856-4 kostenfrei https://doaj.org/article/6e16974eb93e475ab3e39665c2362c21 kostenfrei http://www.sciencedirect.com/science/article/pii/S0022227520398564 kostenfrei https://doaj.org/toc/0022-2275 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_252 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2006 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 36 1995 5 986-997
spelling	10.1016/S0022-2275(20)39856-4 doi (DE-627)DOAJ067435483 (DE-599)DOAJ6e16974eb93e475ab3e39665c2362c21 DE-627 ger DE-627 rakwb eng QD415-436 K Pahan verfasserin aut Phytanic acid oxidation: topographical localization of phytanoyl-CoA ligase and transport of phytanic acid into human peroxisomes. 1995 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier To understand the possible role of phytanoyl-CoA ligase, present in the membrane, in the oxidation of phytanic acid in the matrix of peroxisomes (Pahan, K. and I. Singh. 1993. FEBS Lett. 333: 154-158) we examined the transport of phytanic acid/phytanoyl-CoA into peroxisomes and the topology of the active site of phytanoyl-CoA ligase in the peroxisomal membrane. The increase in lignoceroyl-CoA ligase as compared to no change in the activities of palmitoyl-CoA and phytanoyl-CoA ligases when peroxisomes were disrupted with detergent or sonication and inhibition of the activities of both palmitoyl-CoA and phytanoyl-CoA ligase by impermeable inhibitor of acyl-CoA ligases (mercury-dextran) and trypsin treatment in the intact peroxisomes. On the other hand, the lignoceroyl-CoA ligase activity was inhibited by mercury-dextran and trypsin only in the disrupted peroxisomes. Taken together, these studies support the conclusion that the enzymatic site of phytanoyl-CoA ligase is on the cytoplasmic surface of peroxisomal membrane. This implies that phytanoyl-CoA is synthesized on the cytoplasmic surface of peroxisomal membrane and is translocated through the membrane for its alpha-oxidation to pristanic acid in the matrix of peroxisomes. To delineate the transport for phytanic acid through the peroxisomal membrane, we examined cofactors and energy requirements for its transport into peroxisomes. The similar rates of transport of phytanoyl-CoA and phytanic acid under conditions favorable for fatty acid activation (presence of ATP, CoASH, and MgCl2) and the lack of transport of phytanic acid when ATP and/or CoASH were removed or replaced with their inactive analogues (ATP and/or CoASH) from assay medium clearly demonstrates that the transport of phytanic acid requires prior synthesis of phytanoyl-CoA by phytanoyl-CoA ligase. The prerequisite activation of phytanic acid to phytanoyl-CoA for its alpha-oxidation only in intact peroxisomes, and oxidation of free phytanic acid in digitonin-permealized peroxisomes or isolated matrix, suggests that phytanoyl-CoA ligase (in peroxisomal membrane) regulates the oxidation of phytanic acid in peroxisomes by providing phytanoyl-CoA for its transport into peroxisomes. Biochemistry I Singh verfasserin aut In Journal of Lipid Research Elsevier, 2021 36(1995), 5, Seite 986-997 (DE-627)26601593X (DE-600)1466675-3 15397262 nnns volume:36 year:1995 number:5 pages:986-997 https://doi.org/10.1016/S0022-2275(20)39856-4 kostenfrei https://doaj.org/article/6e16974eb93e475ab3e39665c2362c21 kostenfrei http://www.sciencedirect.com/science/article/pii/S0022227520398564 kostenfrei https://doaj.org/toc/0022-2275 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_252 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2006 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 36 1995 5 986-997
allfields_unstemmed	10.1016/S0022-2275(20)39856-4 doi (DE-627)DOAJ067435483 (DE-599)DOAJ6e16974eb93e475ab3e39665c2362c21 DE-627 ger DE-627 rakwb eng QD415-436 K Pahan verfasserin aut Phytanic acid oxidation: topographical localization of phytanoyl-CoA ligase and transport of phytanic acid into human peroxisomes. 1995 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier To understand the possible role of phytanoyl-CoA ligase, present in the membrane, in the oxidation of phytanic acid in the matrix of peroxisomes (Pahan, K. and I. Singh. 1993. FEBS Lett. 333: 154-158) we examined the transport of phytanic acid/phytanoyl-CoA into peroxisomes and the topology of the active site of phytanoyl-CoA ligase in the peroxisomal membrane. The increase in lignoceroyl-CoA ligase as compared to no change in the activities of palmitoyl-CoA and phytanoyl-CoA ligases when peroxisomes were disrupted with detergent or sonication and inhibition of the activities of both palmitoyl-CoA and phytanoyl-CoA ligase by impermeable inhibitor of acyl-CoA ligases (mercury-dextran) and trypsin treatment in the intact peroxisomes. On the other hand, the lignoceroyl-CoA ligase activity was inhibited by mercury-dextran and trypsin only in the disrupted peroxisomes. Taken together, these studies support the conclusion that the enzymatic site of phytanoyl-CoA ligase is on the cytoplasmic surface of peroxisomal membrane. This implies that phytanoyl-CoA is synthesized on the cytoplasmic surface of peroxisomal membrane and is translocated through the membrane for its alpha-oxidation to pristanic acid in the matrix of peroxisomes. To delineate the transport for phytanic acid through the peroxisomal membrane, we examined cofactors and energy requirements for its transport into peroxisomes. The similar rates of transport of phytanoyl-CoA and phytanic acid under conditions favorable for fatty acid activation (presence of ATP, CoASH, and MgCl2) and the lack of transport of phytanic acid when ATP and/or CoASH were removed or replaced with their inactive analogues (ATP and/or CoASH) from assay medium clearly demonstrates that the transport of phytanic acid requires prior synthesis of phytanoyl-CoA by phytanoyl-CoA ligase. The prerequisite activation of phytanic acid to phytanoyl-CoA for its alpha-oxidation only in intact peroxisomes, and oxidation of free phytanic acid in digitonin-permealized peroxisomes or isolated matrix, suggests that phytanoyl-CoA ligase (in peroxisomal membrane) regulates the oxidation of phytanic acid in peroxisomes by providing phytanoyl-CoA for its transport into peroxisomes. Biochemistry I Singh verfasserin aut In Journal of Lipid Research Elsevier, 2021 36(1995), 5, Seite 986-997 (DE-627)26601593X (DE-600)1466675-3 15397262 nnns volume:36 year:1995 number:5 pages:986-997 https://doi.org/10.1016/S0022-2275(20)39856-4 kostenfrei https://doaj.org/article/6e16974eb93e475ab3e39665c2362c21 kostenfrei http://www.sciencedirect.com/science/article/pii/S0022227520398564 kostenfrei https://doaj.org/toc/0022-2275 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_252 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2006 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 36 1995 5 986-997
allfieldsGer	10.1016/S0022-2275(20)39856-4 doi (DE-627)DOAJ067435483 (DE-599)DOAJ6e16974eb93e475ab3e39665c2362c21 DE-627 ger DE-627 rakwb eng QD415-436 K Pahan verfasserin aut Phytanic acid oxidation: topographical localization of phytanoyl-CoA ligase and transport of phytanic acid into human peroxisomes. 1995 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier To understand the possible role of phytanoyl-CoA ligase, present in the membrane, in the oxidation of phytanic acid in the matrix of peroxisomes (Pahan, K. and I. Singh. 1993. FEBS Lett. 333: 154-158) we examined the transport of phytanic acid/phytanoyl-CoA into peroxisomes and the topology of the active site of phytanoyl-CoA ligase in the peroxisomal membrane. The increase in lignoceroyl-CoA ligase as compared to no change in the activities of palmitoyl-CoA and phytanoyl-CoA ligases when peroxisomes were disrupted with detergent or sonication and inhibition of the activities of both palmitoyl-CoA and phytanoyl-CoA ligase by impermeable inhibitor of acyl-CoA ligases (mercury-dextran) and trypsin treatment in the intact peroxisomes. On the other hand, the lignoceroyl-CoA ligase activity was inhibited by mercury-dextran and trypsin only in the disrupted peroxisomes. Taken together, these studies support the conclusion that the enzymatic site of phytanoyl-CoA ligase is on the cytoplasmic surface of peroxisomal membrane. This implies that phytanoyl-CoA is synthesized on the cytoplasmic surface of peroxisomal membrane and is translocated through the membrane for its alpha-oxidation to pristanic acid in the matrix of peroxisomes. To delineate the transport for phytanic acid through the peroxisomal membrane, we examined cofactors and energy requirements for its transport into peroxisomes. The similar rates of transport of phytanoyl-CoA and phytanic acid under conditions favorable for fatty acid activation (presence of ATP, CoASH, and MgCl2) and the lack of transport of phytanic acid when ATP and/or CoASH were removed or replaced with their inactive analogues (ATP and/or CoASH) from assay medium clearly demonstrates that the transport of phytanic acid requires prior synthesis of phytanoyl-CoA by phytanoyl-CoA ligase. The prerequisite activation of phytanic acid to phytanoyl-CoA for its alpha-oxidation only in intact peroxisomes, and oxidation of free phytanic acid in digitonin-permealized peroxisomes or isolated matrix, suggests that phytanoyl-CoA ligase (in peroxisomal membrane) regulates the oxidation of phytanic acid in peroxisomes by providing phytanoyl-CoA for its transport into peroxisomes. Biochemistry I Singh verfasserin aut In Journal of Lipid Research Elsevier, 2021 36(1995), 5, Seite 986-997 (DE-627)26601593X (DE-600)1466675-3 15397262 nnns volume:36 year:1995 number:5 pages:986-997 https://doi.org/10.1016/S0022-2275(20)39856-4 kostenfrei https://doaj.org/article/6e16974eb93e475ab3e39665c2362c21 kostenfrei http://www.sciencedirect.com/science/article/pii/S0022227520398564 kostenfrei https://doaj.org/toc/0022-2275 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_252 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2006 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 36 1995 5 986-997
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title_sort	phytanic acid oxidation: topographical localization of phytanoyl-coa ligase and transport of phytanic acid into human peroxisomes
callnumber	QD415-436
title_auth	Phytanic acid oxidation: topographical localization of phytanoyl-CoA ligase and transport of phytanic acid into human peroxisomes.
abstract	To understand the possible role of phytanoyl-CoA ligase, present in the membrane, in the oxidation of phytanic acid in the matrix of peroxisomes (Pahan, K. and I. Singh. 1993. FEBS Lett. 333: 154-158) we examined the transport of phytanic acid/phytanoyl-CoA into peroxisomes and the topology of the active site of phytanoyl-CoA ligase in the peroxisomal membrane. The increase in lignoceroyl-CoA ligase as compared to no change in the activities of palmitoyl-CoA and phytanoyl-CoA ligases when peroxisomes were disrupted with detergent or sonication and inhibition of the activities of both palmitoyl-CoA and phytanoyl-CoA ligase by impermeable inhibitor of acyl-CoA ligases (mercury-dextran) and trypsin treatment in the intact peroxisomes. On the other hand, the lignoceroyl-CoA ligase activity was inhibited by mercury-dextran and trypsin only in the disrupted peroxisomes. Taken together, these studies support the conclusion that the enzymatic site of phytanoyl-CoA ligase is on the cytoplasmic surface of peroxisomal membrane. This implies that phytanoyl-CoA is synthesized on the cytoplasmic surface of peroxisomal membrane and is translocated through the membrane for its alpha-oxidation to pristanic acid in the matrix of peroxisomes. To delineate the transport for phytanic acid through the peroxisomal membrane, we examined cofactors and energy requirements for its transport into peroxisomes. The similar rates of transport of phytanoyl-CoA and phytanic acid under conditions favorable for fatty acid activation (presence of ATP, CoASH, and MgCl2) and the lack of transport of phytanic acid when ATP and/or CoASH were removed or replaced with their inactive analogues (ATP and/or CoASH) from assay medium clearly demonstrates that the transport of phytanic acid requires prior synthesis of phytanoyl-CoA by phytanoyl-CoA ligase. The prerequisite activation of phytanic acid to phytanoyl-CoA for its alpha-oxidation only in intact peroxisomes, and oxidation of free phytanic acid in digitonin-permealized peroxisomes or isolated matrix, suggests that phytanoyl-CoA ligase (in peroxisomal membrane) regulates the oxidation of phytanic acid in peroxisomes by providing phytanoyl-CoA for its transport into peroxisomes.
abstractGer	To understand the possible role of phytanoyl-CoA ligase, present in the membrane, in the oxidation of phytanic acid in the matrix of peroxisomes (Pahan, K. and I. Singh. 1993. FEBS Lett. 333: 154-158) we examined the transport of phytanic acid/phytanoyl-CoA into peroxisomes and the topology of the active site of phytanoyl-CoA ligase in the peroxisomal membrane. The increase in lignoceroyl-CoA ligase as compared to no change in the activities of palmitoyl-CoA and phytanoyl-CoA ligases when peroxisomes were disrupted with detergent or sonication and inhibition of the activities of both palmitoyl-CoA and phytanoyl-CoA ligase by impermeable inhibitor of acyl-CoA ligases (mercury-dextran) and trypsin treatment in the intact peroxisomes. On the other hand, the lignoceroyl-CoA ligase activity was inhibited by mercury-dextran and trypsin only in the disrupted peroxisomes. Taken together, these studies support the conclusion that the enzymatic site of phytanoyl-CoA ligase is on the cytoplasmic surface of peroxisomal membrane. This implies that phytanoyl-CoA is synthesized on the cytoplasmic surface of peroxisomal membrane and is translocated through the membrane for its alpha-oxidation to pristanic acid in the matrix of peroxisomes. To delineate the transport for phytanic acid through the peroxisomal membrane, we examined cofactors and energy requirements for its transport into peroxisomes. The similar rates of transport of phytanoyl-CoA and phytanic acid under conditions favorable for fatty acid activation (presence of ATP, CoASH, and MgCl2) and the lack of transport of phytanic acid when ATP and/or CoASH were removed or replaced with their inactive analogues (ATP and/or CoASH) from assay medium clearly demonstrates that the transport of phytanic acid requires prior synthesis of phytanoyl-CoA by phytanoyl-CoA ligase. The prerequisite activation of phytanic acid to phytanoyl-CoA for its alpha-oxidation only in intact peroxisomes, and oxidation of free phytanic acid in digitonin-permealized peroxisomes or isolated matrix, suggests that phytanoyl-CoA ligase (in peroxisomal membrane) regulates the oxidation of phytanic acid in peroxisomes by providing phytanoyl-CoA for its transport into peroxisomes.
abstract_unstemmed	To understand the possible role of phytanoyl-CoA ligase, present in the membrane, in the oxidation of phytanic acid in the matrix of peroxisomes (Pahan, K. and I. Singh. 1993. FEBS Lett. 333: 154-158) we examined the transport of phytanic acid/phytanoyl-CoA into peroxisomes and the topology of the active site of phytanoyl-CoA ligase in the peroxisomal membrane. The increase in lignoceroyl-CoA ligase as compared to no change in the activities of palmitoyl-CoA and phytanoyl-CoA ligases when peroxisomes were disrupted with detergent or sonication and inhibition of the activities of both palmitoyl-CoA and phytanoyl-CoA ligase by impermeable inhibitor of acyl-CoA ligases (mercury-dextran) and trypsin treatment in the intact peroxisomes. On the other hand, the lignoceroyl-CoA ligase activity was inhibited by mercury-dextran and trypsin only in the disrupted peroxisomes. Taken together, these studies support the conclusion that the enzymatic site of phytanoyl-CoA ligase is on the cytoplasmic surface of peroxisomal membrane. This implies that phytanoyl-CoA is synthesized on the cytoplasmic surface of peroxisomal membrane and is translocated through the membrane for its alpha-oxidation to pristanic acid in the matrix of peroxisomes. To delineate the transport for phytanic acid through the peroxisomal membrane, we examined cofactors and energy requirements for its transport into peroxisomes. The similar rates of transport of phytanoyl-CoA and phytanic acid under conditions favorable for fatty acid activation (presence of ATP, CoASH, and MgCl2) and the lack of transport of phytanic acid when ATP and/or CoASH were removed or replaced with their inactive analogues (ATP and/or CoASH) from assay medium clearly demonstrates that the transport of phytanic acid requires prior synthesis of phytanoyl-CoA by phytanoyl-CoA ligase. The prerequisite activation of phytanic acid to phytanoyl-CoA for its alpha-oxidation only in intact peroxisomes, and oxidation of free phytanic acid in digitonin-permealized peroxisomes or isolated matrix, suggests that phytanoyl-CoA ligase (in peroxisomal membrane) regulates the oxidation of phytanic acid in peroxisomes by providing phytanoyl-CoA for its transport into peroxisomes.
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title_short	Phytanic acid oxidation: topographical localization of phytanoyl-CoA ligase and transport of phytanic acid into human peroxisomes.
url	https://doi.org/10.1016/S0022-2275(20)39856-4 https://doaj.org/article/6e16974eb93e475ab3e39665c2362c21 http://www.sciencedirect.com/science/article/pii/S0022227520398564 https://doaj.org/toc/0022-2275
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up_date	2024-07-04T00:53:10.725Z
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Phytanic acid oxidation: topographical localization of phytanoyl-CoA ligase and transport of phytanic acid into human peroxisomes.

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