Comparison of the domain-level organization of starch hydrolases and related enzymes

H. M. Jespersen, E. A. MacGregor, Michael Sierks, B. Svensson

Research output: Contribution to journalArticle

189 Citations (Scopus)

Abstract

Structure-prediction and hydrophobic-cluster analysis of several starch hydrolases and related enzymes indicated the organization of eleven domain types. Most enzymes possess a catalytic (β/α)8-barrel and a smaller C-terminal domain as seen in crystal structures of α-amylase and cyclodextrin glucanotransferase. Some also have a starch-granule-binding domain. Enzymes breaking or forming endo-α-1,6 linkages contain domains N-terminal to the (β/α)8-barrel.

Original languageEnglish (US)
Pages (from-to)51-55
Number of pages5
JournalBiochemical Journal
Volume280
Issue number1
StatePublished - 1991
Externally publishedYes

Fingerprint

Hydrolases
Starch
Enzymes
Cluster analysis
Amylases
Cluster Analysis
Crystal structure

ASJC Scopus subject areas

  • Biochemistry

Cite this

Jespersen, H. M., MacGregor, E. A., Sierks, M., & Svensson, B. (1991). Comparison of the domain-level organization of starch hydrolases and related enzymes. Biochemical Journal, 280(1), 51-55.

Comparison of the domain-level organization of starch hydrolases and related enzymes. / Jespersen, H. M.; MacGregor, E. A.; Sierks, Michael; Svensson, B.

In: Biochemical Journal, Vol. 280, No. 1, 1991, p. 51-55.

Research output: Contribution to journalArticle

Jespersen, HM, MacGregor, EA, Sierks, M & Svensson, B 1991, 'Comparison of the domain-level organization of starch hydrolases and related enzymes', Biochemical Journal, vol. 280, no. 1, pp. 51-55.
Jespersen, H. M. ; MacGregor, E. A. ; Sierks, Michael ; Svensson, B. / Comparison of the domain-level organization of starch hydrolases and related enzymes. In: Biochemical Journal. 1991 ; Vol. 280, No. 1. pp. 51-55.
@article{82a5bd79470d494e8738c842e45bf960,
title = "Comparison of the domain-level organization of starch hydrolases and related enzymes",
abstract = "Structure-prediction and hydrophobic-cluster analysis of several starch hydrolases and related enzymes indicated the organization of eleven domain types. Most enzymes possess a catalytic (β/α)8-barrel and a smaller C-terminal domain as seen in crystal structures of α-amylase and cyclodextrin glucanotransferase. Some also have a starch-granule-binding domain. Enzymes breaking or forming endo-α-1,6 linkages contain domains N-terminal to the (β/α)8-barrel.",
author = "Jespersen, {H. M.} and MacGregor, {E. A.} and Michael Sierks and B. Svensson",
year = "1991",
language = "English (US)",
volume = "280",
pages = "51--55",
journal = "Biochemical Journal",
issn = "0264-6021",
publisher = "Portland Press Ltd.",
number = "1",

}

TY - JOUR

T1 - Comparison of the domain-level organization of starch hydrolases and related enzymes

AU - Jespersen, H. M.

AU - MacGregor, E. A.

AU - Sierks, Michael

AU - Svensson, B.

PY - 1991

Y1 - 1991

N2 - Structure-prediction and hydrophobic-cluster analysis of several starch hydrolases and related enzymes indicated the organization of eleven domain types. Most enzymes possess a catalytic (β/α)8-barrel and a smaller C-terminal domain as seen in crystal structures of α-amylase and cyclodextrin glucanotransferase. Some also have a starch-granule-binding domain. Enzymes breaking or forming endo-α-1,6 linkages contain domains N-terminal to the (β/α)8-barrel.

AB - Structure-prediction and hydrophobic-cluster analysis of several starch hydrolases and related enzymes indicated the organization of eleven domain types. Most enzymes possess a catalytic (β/α)8-barrel and a smaller C-terminal domain as seen in crystal structures of α-amylase and cyclodextrin glucanotransferase. Some also have a starch-granule-binding domain. Enzymes breaking or forming endo-α-1,6 linkages contain domains N-terminal to the (β/α)8-barrel.

UR - http://www.scopus.com/inward/record.url?scp=0026040317&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0026040317&partnerID=8YFLogxK

M3 - Article

C2 - 1741756

AN - SCOPUS:0026040317

VL - 280

SP - 51

EP - 55

JO - Biochemical Journal

JF - Biochemical Journal

SN - 0264-6021

IS - 1

ER -