Reaction mechanism underlying CMP-N-acetylneuraminic acid hydroxylation in mouse liver: Formation of a ternary complex of cytochrome b5, CMP-N …

H Takematsu, T Kawano, S Koyama… - The Journal of …, 1994 - jstage.jst.go.jp
We have proposed that CMP-N-acetylneuraminic acid (CMP-NeuAc) hydroxylation is
mediated by an electron transport system consisting of cytochrome b5 (b5), b5 reducing …

Participation of cytochrome b5 in CMP-N-acetylneuraminic acid hydroxylation in mouse liver cytosol

Y Kozutsumi, T Kawano, T Yamakawa… - The Journal of …, 1990 - jstage.jst.go.jp
The activity of CMP-N-acetylneuraminic acid hydroxylase, that converts CMP-N-
acetylneuraminic acid (CMP-NeuAc) to CPM-N-glycolylneuraminic acid (CMP-NeuGc), in …

CMP‐N‐acetylneuraminic acid hydroxylase from mouse liver and pig submandibular glands: Interaction with membrane‐bound and soluble cytochrome b5 …

L Shaw, P Schneckenburger… - European journal of …, 1994 - Wiley Online Library
In this report, the nature of the protein components involved in the functioning of cytidine‐5′‐
monophosphate‐N‐acetylneuraminic acid (CMP‐Neu5 Ac) hydroxylase in high‐speed …

Reconstitution of CMP-N-Acetylneuraminic Acid Hydroxylation Activity Using a Mouse Liver Cytosol Fraction and Soluble Cytochrome b5 Purified from Horse …

Y Kozutsumi, T Kawano, H Kawasaki… - The Journal of …, 1991 - academic.oup.com
The hydroxylation of CMP-N-acetylneuraminic acid (CMP-NeuAc) in the formation of CMP-N-
glycolylneuraminic acid requires several components which comprise an electron transport …

Mouse liver cytidine‐5′‐monophosphate‐N‐acetylneuraminic acid hydroxylase: Catalytic function and regulation

L Shaw, P Schneckenburger, J Carlsen… - European journal of …, 1992 - Wiley Online Library
In this paper, we present the results of an investigation into the catalytic properties of CMP‐
Neu5Ac hydroxylase (Neu5Ac: N‐acetylneuraminic acid) in high‐speed supernatants of …

Purification, characterization and reconstitution of CMP-N-acetylneuraminate hydroxylase from mouse liver

P Schneckenburger, L Shaw, R Schauer - Glycoconjugate Journal, 1994 - Springer
CMP-N-acetylneuraminate hydroxylase was isolated from mouse liver high speed
supernatant with a yield of 0.4% and an apparent 1000-fold purification. The enzyme is a …

Regulation of biosynthesis of N-glycolylneuraminic acid-containing glycoconjugates: characterization of factors required for NADH-dependent cytidine 5 …

T Kawano, Y Kozutsumi, H Takematsu, T Kawasaki… - Glycoconjugate …, 1993 - Springer
The hydroxylation of CMP-NeuAc has been demonstrated to be carried out by several
factors including the soluble form of cytochrome b 5. In the present study, mouse liver cytosol …

Detection of CMP-N-acetylneuraminic acid hydroxylase activity in fractionated mouse liver

L Shaw, R Schauer - Biochemical Journal, 1989 - portlandpress.com
The finding that N-glycoloylneuraminic acid (Neu5Gc) in pig submandibular gland is
synthesized by hydroxylation of the sugar nucleotide CMP-Neu5Ac [Shaw & Schauer (1988) …

Biosynthesis of N-glycolylneuraminic acid-containing glycoconjugates. Purification and characterization of the key enzyme of the cytidine monophospho-N …

T Kawano, Y Kozutsumi, T Kawasaki… - Journal of Biological …, 1994 - Elsevier
We have proposed that cytidine monophospho-N-acetylneuraminic acid (CMP-NeuAc)
hydroxylation is carried out by a multienzyme system involving CMP-NeuAc hydroxylase …

CMP-N-Acetylneuraminic acid hydroxylase is exclusively inactive in humans

A Irie, A Suzuki - Biochemical and biophysical research communications, 1998 - Elsevier
We cloned cDNAs for mouse and human CMP-N-acetylneuraminic acid (CMP-NeuAc)
hydroxylases and showed that the human CMP-NeuAc hydroxylase protein is inactive …