Studies on the structure of lecithin: Cholesterol acyltransferase (LCAT)-comparisons of the active site region and secondary structure of the human and the porcine enzymes

K. Ümit Yüksel; Yong B. Park; Jinha Jung; Robert W. Gracy; Andras G. Lacko

doi:10.1016/0305-0491(89)90361-1

Studies on the structure of lecithin: Cholesterol acyltransferase (LCAT)-comparisons of the active site region and secondary structure of the human and the porcine enzymes

K. Ümit Yüksel, Yong B. Park, Jinha Jung, Robert W. Gracy, Andras G. Lacko

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3 Scopus citations

Abstract

1. 1. Chemical modification of essential serine, histidine and cysteine residues of porcine LCAT were accompanied by loss of enzymatic activity. 2. 2. Modification of cysteine with DTNB inactivated the enzyme which could not be reactivated by KCN suggesting direct involvement of the cysteine residue(s) in catalysis. 3. 3. About half of the primary structure of the procine enzyme was determined. 4. 4. Respective regions of the human and porcine LCAT are highly homologous; especially, the amino-terminus and the region surrounding the DFP-labeled serine residues. 5. 5. The observed primary structure differences represent amino acid substitution that are projected to induce significant changes in secondary structure.

Original language	English
Pages (from-to)	389-394
Number of pages	6
Journal	Comparative Biochemistry and Physiology -- Part B: Biochemistry and
Volume	94
Issue number	2
DOIs	https://doi.org/10.1016/0305-0491(89)90361-1
State	Published - 1989

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Yüksel, K. Ü., Park, Y. B., Jung, J., Gracy, R. W., & Lacko, A. G. (1989). Studies on the structure of lecithin: Cholesterol acyltransferase (LCAT)-comparisons of the active site region and secondary structure of the human and the porcine enzymes. Comparative Biochemistry and Physiology -- Part B: Biochemistry and, 94(2), 389-394. https://doi.org/10.1016/0305-0491(89)90361-1

Yüksel, K. Ümit ; Park, Yong B. ; Jung, Jinha ; Gracy, Robert W. ; Lacko, Andras G. / Studies on the structure of lecithin : Cholesterol acyltransferase (LCAT)-comparisons of the active site region and secondary structure of the human and the porcine enzymes. In: Comparative Biochemistry and Physiology -- Part B: Biochemistry and. 1989 ; Vol. 94, No. 2. pp. 389-394.

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title = "Studies on the structure of lecithin: Cholesterol acyltransferase (LCAT)-comparisons of the active site region and secondary structure of the human and the porcine enzymes",

abstract = "1. 1. Chemical modification of essential serine, histidine and cysteine residues of porcine LCAT were accompanied by loss of enzymatic activity. 2. 2. Modification of cysteine with DTNB inactivated the enzyme which could not be reactivated by KCN suggesting direct involvement of the cysteine residue(s) in catalysis. 3. 3. About half of the primary structure of the procine enzyme was determined. 4. 4. Respective regions of the human and porcine LCAT are highly homologous; especially, the amino-terminus and the region surrounding the DFP-labeled serine residues. 5. 5. The observed primary structure differences represent amino acid substitution that are projected to induce significant changes in secondary structure.",

author = "Y{\"u}ksel, {K. {\"U}mit} and Park, {Yong B.} and Jinha Jung and Gracy, {Robert W.} and Lacko, {Andras G.}",

note = "Funding Information: Acknowledgements--Trheisse archw as supportedb y funds from the National Instituteso f Health (HL-27620, AG-01274a nd AM-14638,B RSG-S07R R 05870)T, he Robert A. Welch Foundation(B -502 and B-935),T he Organized ResearchF und at TCOM and by the Texas Advanced ResearchT echnologyP rogram(Applied Enzyme Tech-nologyP rogram)T. he authorsa rei ndebtedto Amy Moore for secretariaals sistance.",

year = "1989",

doi = "10.1016/0305-0491(89)90361-1",

language = "English",

volume = "94",

pages = "389--394",

journal = "Comparative Biochemistry and Physiology -- Part B: Biochemistry and",

issn = "0305-0491",

publisher = "Elsevier BV",

number = "2",

}

Yüksel, KÜ, Park, YB, Jung, J, Gracy, RW & Lacko, AG 1989, 'Studies on the structure of lecithin: Cholesterol acyltransferase (LCAT)-comparisons of the active site region and secondary structure of the human and the porcine enzymes', Comparative Biochemistry and Physiology -- Part B: Biochemistry and, vol. 94, no. 2, pp. 389-394. https://doi.org/10.1016/0305-0491(89)90361-1

Studies on the structure of lecithin : Cholesterol acyltransferase (LCAT)-comparisons of the active site region and secondary structure of the human and the porcine enzymes. / Yüksel, K. Ümit; Park, Yong B.; Jung, Jinha; Gracy, Robert W.; Lacko, Andras G.

In: Comparative Biochemistry and Physiology -- Part B: Biochemistry and, Vol. 94, No. 2, 1989, p. 389-394.

Research output: Contribution to journal › Article › peer-review

TY - JOUR

T1 - Studies on the structure of lecithin

T2 - Cholesterol acyltransferase (LCAT)-comparisons of the active site region and secondary structure of the human and the porcine enzymes

AU - Yüksel, K. Ümit

AU - Park, Yong B.

AU - Jung, Jinha

AU - Gracy, Robert W.

AU - Lacko, Andras G.

N1 - Funding Information: Acknowledgements--Trheisse archw as supportedb y funds from the National Instituteso f Health (HL-27620, AG-01274a nd AM-14638,B RSG-S07R R 05870)T, he Robert A. Welch Foundation(B -502 and B-935),T he Organized ResearchF und at TCOM and by the Texas Advanced ResearchT echnologyP rogram(Applied Enzyme Tech-nologyP rogram)T. he authorsa rei ndebtedto Amy Moore for secretariaals sistance.

PY - 1989

Y1 - 1989

N2 - 1. 1. Chemical modification of essential serine, histidine and cysteine residues of porcine LCAT were accompanied by loss of enzymatic activity. 2. 2. Modification of cysteine with DTNB inactivated the enzyme which could not be reactivated by KCN suggesting direct involvement of the cysteine residue(s) in catalysis. 3. 3. About half of the primary structure of the procine enzyme was determined. 4. 4. Respective regions of the human and porcine LCAT are highly homologous; especially, the amino-terminus and the region surrounding the DFP-labeled serine residues. 5. 5. The observed primary structure differences represent amino acid substitution that are projected to induce significant changes in secondary structure.

AB - 1. 1. Chemical modification of essential serine, histidine and cysteine residues of porcine LCAT were accompanied by loss of enzymatic activity. 2. 2. Modification of cysteine with DTNB inactivated the enzyme which could not be reactivated by KCN suggesting direct involvement of the cysteine residue(s) in catalysis. 3. 3. About half of the primary structure of the procine enzyme was determined. 4. 4. Respective regions of the human and porcine LCAT are highly homologous; especially, the amino-terminus and the region surrounding the DFP-labeled serine residues. 5. 5. The observed primary structure differences represent amino acid substitution that are projected to induce significant changes in secondary structure.

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JO - Comparative Biochemistry and Physiology -- Part B: Biochemistry and

JF - Comparative Biochemistry and Physiology -- Part B: Biochemistry and

SN - 0305-0491

IS - 2

ER -

Studies on the structure of lecithin: Cholesterol acyltransferase (LCAT)-comparisons of the active site region and secondary structure of the human and the porcine enzymes

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