Serine biosynthesis in human hair follicles by the phosphorylated pathway: follicular 3-phosphoglycerate dehydrogenase.

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Goldsmith LA, O'Barr T

Serine biosynthesis in human hair follicles by the phosphorylated pathway: follicular 3-phosphoglycerate dehydrogenase.

J Invest Dermatol. 1976 Jun;66(6):360-6.

PubMed ID
945314 [ View in PubMed
]
Abstract

The phosphorylated pathway of serine biosynthesis was demonstrated in human hair bulbs and sheaths by the formation of phosphoserine and serine from (14C)3-phosphoglyceric acid. The initial and rate limiting enzyme of the pathway, 3-phosphoglycerate dehydrogenase (3-PGDH) was demonstrated by enzyme determinations in human and rat hair follicles, human epidermis, and chicken epidermis. Follicular 3-PGDH was characterized using a sensitive fluorometric assay with NADH as a co-substrate. Monovalent cations (Na+, K+, Li+, or NH4+) were necessary for full enzyme activity. p-Hydroxymercuribenzoate inhibited activity, and activity was 3 times higher with NADH as a co-substrate than with NADPH. The apparent Km for the substrate hydroxyphosphopyruvic acid was 32.8 muM, and the apparent Km for NADH 4.8 muM similar to the Kms for other mammalian 3-PGDHs. Enzyme activity was not altered by parenteral corticosteroids, a high carbohydrate diet, low protein diet, or starvation. Enzyme activity decreased over the first 12 days of life in newborn rats. The phosphorylated pathway of serine synthesis provides a potential nondietary and nonhepatic source of serine, glycine, and their products in keratinizing tissues.

DrugBank Data that Cites this Article

Drug Targets
DrugTargetKindOrganismPharmacological ActionActions
NADHD-3-phosphoglycerate dehydrogenaseProteinHumans
Unknown
Not AvailableDetails