Identification of a novel conserved sequence motif in flavoprotein hydroxylases with a putative dual function in FAD/NADPH binding.

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

Keywords

@article{6802d9abe92c4a309103e54472db301a,

title = "Identification of a novel conserved sequence motif in flavoprotein hydroxylases with a putative dual function in FAD/NADPH binding.",

keywords = "Fingerprint, Flavoprotein family, NADPH-binding, p-hydroxybenzoate hydroxylase, Sequence alignment",

author = "M.H.M. Eppink and H.A. Schreuder and {van Berkel}, W.J.H.",

year = "1997",

language = "English",

volume = "6",

pages = "2454--2458",

journal = "Protein Science",

issn = "0961-8368",

publisher = "Wiley",

}

TY - JOUR

T1 - Identification of a novel conserved sequence motif in flavoprotein hydroxylases with a putative dual function in FAD/NADPH binding.

AU - Eppink, M.H.M.

AU - Schreuder, H.A.

AU - van Berkel, W.J.H.

PY - 1997

Y1 - 1997

KW - Fingerprint

KW - Flavoprotein family

KW - NADPH-binding

KW - p-hydroxybenzoate hydroxylase

KW - Sequence alignment

M3 - Article

SN - 0961-8368

VL - 6

SP - 2454

EP - 2458

JO - Protein Science

JF - Protein Science

ER -