Which enzymes metabolize gelatide and are there known drug interactions?
Executive summary
There is no direct reporting in the supplied documents about a drug or compound named “gelatide”; available sources instead discuss gelatin and gelatinases — the enzymes that break down gelatin — and broader mechanisms for protein hydrolysis and possible enzymatic cross‑reactions [1] [2]. The supplied literature shows gelatin is cleaved by proteolytic enzymes including gelatinases (MMP‑2/MMP‑9) and many other proteases [1] [2], but the sources do not mention metabolism of a molecule called “gelatide” or any drug–drug interactions involving it (available sources do not mention gelatide).
1. What the sources actually cover: gelatin and gelatinases, not “gelatide”
The material in the search results repeatedly treats gelatin — the denatured form of collagen — and gelatinases, a subgroup of matrix metalloproteinases (notably gelatinase A/MMP‑2 and gelatinase B/MMP‑9) that hydrolyze gelatin and related extracellular matrix proteins [1] [3]. Several laboratory protocols and reviews describe how gelatinase activity is assayed (gelatin hydrolysis tests, zymography) and note that many proteolytic enzymes can hydrolyze gelatin into peptides and amino acids [4] [5] [3] [2]. The searched corpus contains no report that defines or characterizes a drug or substance named “gelatide” (available sources do not mention gelatide).
2. Which enzymes break down gelatin in the literature
The most consistently cited enzymes are gelatinases — extracellular, zinc‑dependent metalloendopeptidases within the MMP family, chiefly MMP‑2 and MMP‑9 — identified by enzymology codes (EC 3.4.24.24 and 3.4.24.35 respectively) and known to cleave gelatin, collagen, elastin and other bioactive peptides [1] [3]. Older and broader studies also document that gelatin and collagen are susceptible to many proteolytic enzymes (trypsin and bacterial proteases such as those from Bacillus species) and to exo‑ and endo‑proteases used in industrial or laboratory settings [6] [7] [2]. Microbial proteases (e.g., from Bacillus spp., Pseudomonas, Serratia) and plant proteases like bromelain or papain are discussed in the context of gelatin degradation in food and experiment‑based reports [8] [9] [6].
3. Mechanisms and assays — how scientists know degradation occurs
Researchers detect gelatinase activity by zymography and substrate conversion assays; zymography is widely used to show MMP‑2/MMP‑9 forms and relative levels but does not measure net catalytic activity without standards [3]. Gelatin hydrolysis tests — microbiology protocols — detect extracellular gelatinases by liquefaction of a gelatin medium, and textbooks and protocol repositories describe the two‑step process: gelatin → polypeptides → amino acids [5] [4] [10].
4. What these sources say about interactions or “drug interactions”
None of the provided gelatin/gelatinase sources discuss pharmacokinetic drug–drug interactions tied to gelatin or to a compound named “gelatide.” The drug‑interaction sources supplied cover general frameworks and examples (common CYP enzyme roles, tools like interaction checkers, and interactions for specific drugs such as imatinib/Gleevec) but do not connect those interaction mechanisms to gelatin or gelatinases [11] [12] [13]. Therefore, there is no documented evidence in this set that enzymes that metabolize gelatin or gelatinases mediate clinically relevant drug interactions with a molecule called “gelatide” (available sources do not mention gelatide).
5. Competing viewpoints and limitations in the record
The literature here spans molecular enzyme biochemistry and practical microbiology: sources agree that gelatin is broadly susceptible to proteolysis and that MMP‑2/MMP‑9 are central gelatinases in mammals [1] [3] [2]. Limitations are explicit: zymography frequently used in MMP research reveals forms and relative levels but not true net activity without careful standardization [3]. Importantly, the supplied collection contains no pharmacology dossier, pharmacokinetic studies, or labeling for any marketed compound named “gelatide,” so claims about which human drug‑metabolizing enzymes process “gelatide” or produce interactions cannot be supported from these sources (available sources do not mention gelatide).
6. Practical takeaway and next reporting steps
If you are asking about a drug called gelatide, the proper next steps are to supply a canonical identifier (INN, trade name, active ingredient) or a primary source such as FDA label, EMA assessment, an NDA/SmPC, or a peer‑reviewed metabolism study. For questions about gelatinases or how proteases can affect protein‑based formulations or foods, the cited enzymology and microbiology reviews and protocols here are appropriate references [1] [4] [3] [2]. For clinical drug–drug interaction frameworks, consult pharmacology sources and interaction databases [11] [13].
Sources cited above are limited to the supplied search results: gelatin and gelatinases [1] [6] [10] [4] [3] [7] [8] [2] [5] and general drug‑interaction resources [11] [12] [13].