The subunit interfaces of oligomeric enzymes are conserved to a similar extent to the overall protein sequences

Research output: Contribution to journalArticle

57 Citations (Scopus)

Abstract

It is well established that, within families of homologous enzymes, amino acid residues that are involved in the chemistry of the reaction are highly conserved. To determine if residues at the subunit interface of oligomeric enzymes with shared active sites are also conserved, comparative analysis of five enzyme families was undertaken. For the chosen enzyme families, sequence data were available for a large number of proteins and a three-dimensional structure was known for at least two members of each family. The analysis indicates that the subunit interface and the hydrophobic core of proteins from all five families have diverged to a similar extent to the overall protein sequences.

Original languageEnglish (US)
Pages (from-to)2455-2458
Number of pages4
JournalProtein Science
Volume3
Issue number12
StatePublished - 1994

Fingerprint

Enzymes
Proteins
Catalytic Domain
Amino Acids

ASJC Scopus subject areas

  • Biochemistry

Cite this

@article{77ab35ea17f04045a89a4c3c2b7a10fb,
title = "The subunit interfaces of oligomeric enzymes are conserved to a similar extent to the overall protein sequences",
abstract = "It is well established that, within families of homologous enzymes, amino acid residues that are involved in the chemistry of the reaction are highly conserved. To determine if residues at the subunit interface of oligomeric enzymes with shared active sites are also conserved, comparative analysis of five enzyme families was undertaken. For the chosen enzyme families, sequence data were available for a large number of proteins and a three-dimensional structure was known for at least two members of each family. The analysis indicates that the subunit interface and the hydrophobic core of proteins from all five families have diverged to a similar extent to the overall protein sequences.",
author = "Grishin, {N. V.} and Phillips, {M. A.}",
year = "1994",
language = "English (US)",
volume = "3",
pages = "2455--2458",
journal = "Protein Science",
issn = "0961-8368",
publisher = "Cold Spring Harbor Laboratory Press",
number = "12",

}

TY - JOUR

T1 - The subunit interfaces of oligomeric enzymes are conserved to a similar extent to the overall protein sequences

AU - Grishin, N. V.

AU - Phillips, M. A.

PY - 1994

Y1 - 1994

N2 - It is well established that, within families of homologous enzymes, amino acid residues that are involved in the chemistry of the reaction are highly conserved. To determine if residues at the subunit interface of oligomeric enzymes with shared active sites are also conserved, comparative analysis of five enzyme families was undertaken. For the chosen enzyme families, sequence data were available for a large number of proteins and a three-dimensional structure was known for at least two members of each family. The analysis indicates that the subunit interface and the hydrophobic core of proteins from all five families have diverged to a similar extent to the overall protein sequences.

AB - It is well established that, within families of homologous enzymes, amino acid residues that are involved in the chemistry of the reaction are highly conserved. To determine if residues at the subunit interface of oligomeric enzymes with shared active sites are also conserved, comparative analysis of five enzyme families was undertaken. For the chosen enzyme families, sequence data were available for a large number of proteins and a three-dimensional structure was known for at least two members of each family. The analysis indicates that the subunit interface and the hydrophobic core of proteins from all five families have diverged to a similar extent to the overall protein sequences.

UR - http://www.scopus.com/inward/record.url?scp=0028566271&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0028566271&partnerID=8YFLogxK

M3 - Article

C2 - 7757001

AN - SCOPUS:0028566271

VL - 3

SP - 2455

EP - 2458

JO - Protein Science

JF - Protein Science

SN - 0961-8368

IS - 12

ER -