B. N-acetylglucoamidase Inhibitors
N-acetylglucoamidase is an enzyme that separates N-acetylglucosamine from the
sugar chains in glycoproteins and glycolipids present on the cell surface. Rising
levels of activity in the urine, however, indicate disorders in the kidney’s renal
tubules. Its activity is also known to increase in the blood of patients with diabetes,
leukemia, and other forms of cancer.
Because they inhibit the activity of this enzyme, N-acetylglucoamidase inhibitors
have potential treatment applications.
Recently, N-acetylglucoamidase inhibitor-producing strains have been sought
through isolation of marine actinomycetes. The N-acetylglucoamidase inhibitors
pyrostatin A and B have been isolated from these marine actinomycetes and their
structures identified (Fig. 11.9).
11.5.3 Tyrosinase Inhibitors Produced by Marine
Filamentous Bacteria
Tyrosinase inhibitors are metallic enzymes with copper at the center of their
activity. They are a form of quinone-oxidizing enzyme found across a wide range of
animals, plants, and microorganisms (Fig. 11.10).
These enzymes work by catalyzing oxidation of the essential amino acid tyrosine
into dopa (3,4-dihydroxy phenylalanine) and dopa quinone. In dermatology,
tyrosinase is involved in the early stages of melanin production, indicating its
importance as an enzyme for melanin formation (Fig. 11.11).
Human skin is a membrane that covers the organism, consisting of an epidermis
and dermis. Epidermal cells include keratinocytes and melanocytes. Following cell
division, keratinocytes differentiate into four distinct layers: the stratum basale, the
stratum spinosum, the granular layer, and the stratum corneum (Fig. 11.12) (Mayer
and Hamann 2005).
The process of epidermal basal cells developing into their final granular layer
(epidermal turnover) takes approximately four weeks.
At the same time, melanocytes do not move from the basal layer; the melanin
that is formed is degraded by surrounding keratinocytes, which participate in
Fig. 11.9 Chemical structures of the N-acetylglucoamidase inhibitors pyrostatin A and B
11.5 Enzyme Inhibitors Produced by Marine Microorganisms
409
N-acetylglucoamidase is an enzyme that separates N-acetylglucosamine from the
sugar chains in glycoproteins and glycolipids present on the cell surface. Rising
levels of activity in the urine, however, indicate disorders in the kidney’s renal
tubules. Its activity is also known to increase in the blood of patients with diabetes,
leukemia, and other forms of cancer.
Because they inhibit the activity of this enzyme, N-acetylglucoamidase inhibitors
have potential treatment applications.
Recently, N-acetylglucoamidase inhibitor-producing strains have been sought
through isolation of marine actinomycetes. The N-acetylglucoamidase inhibitors
pyrostatin A and B have been isolated from these marine actinomycetes and their
structures identified (Fig. 11.9).
11.5.3 Tyrosinase Inhibitors Produced by Marine
Filamentous Bacteria
Tyrosinase inhibitors are metallic enzymes with copper at the center of their
activity. They are a form of quinone-oxidizing enzyme found across a wide range of
animals, plants, and microorganisms (Fig. 11.10).
These enzymes work by catalyzing oxidation of the essential amino acid tyrosine
into dopa (3,4-dihydroxy phenylalanine) and dopa quinone. In dermatology,
tyrosinase is involved in the early stages of melanin production, indicating its
importance as an enzyme for melanin formation (Fig. 11.11).
Human skin is a membrane that covers the organism, consisting of an epidermis
and dermis. Epidermal cells include keratinocytes and melanocytes. Following cell
division, keratinocytes differentiate into four distinct layers: the stratum basale, the
stratum spinosum, the granular layer, and the stratum corneum (Fig. 11.12) (Mayer
and Hamann 2005).
The process of epidermal basal cells developing into their final granular layer
(epidermal turnover) takes approximately four weeks.
At the same time, melanocytes do not move from the basal layer; the melanin
that is formed is degraded by surrounding keratinocytes, which participate in
Fig. 11.9 Chemical structures of the N-acetylglucoamidase inhibitors pyrostatin A and B
11.5 Enzyme Inhibitors Produced by Marine Microorganisms
409