Purple acid phosphatases from bacteria: similarities to mammalian and plant enzymes

Mammalian and plant purple acid phosphatases have similar active site structures despite low sequence identity (

Saved in:
Bibliographic Details
Published in:Gene 2000-09, Vol.255 (2), p.419-424
Main Authors: Schenk, Gerhard, Korsinczky, Michael L.J., Hume, David A., Hamilton, Susan, DeJersey, John
Format: Article
Language:English
Subjects:
Acid Phosphatase - chemistry
Acid Phosphatase - genetics
Amino Acid Sequence
Animals
Bacteria - enzymology
Bacteria - genetics
Binuclear metal centre
Cyanobacteria
Cyanobacteria - enzymology
Cyanobacteria - genetics
Fabaceae - enzymology
Fabaceae - genetics
Fenton-type catalysis
Glycoproteins - chemistry
Glycoproteins - genetics
Mammals - genetics
Molecular Sequence Data
Mycobacteria
Mycobacterium tuberculosis
Mycobacterium tuberculosis - enzymology
Mycobacterium tuberculosis - genetics
Phosphate metabolism
Plants - enzymology
Plants - genetics
Plants, Medicinal
Protein Conformation
Purple acid phosphatase
Sequence Alignment
Sequence Homology, Amino Acid
Swine
Synechocystis
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Mammalian and plant purple acid phosphatases have similar active site structures despite low sequence identity (
ISSN:0378-1119
1879-0038
DOI:10.1016/S0378-1119(00)00305-X